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        <title>Advances in Biophysics via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Advances in Biophysics' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Advances+in+Biophysics&t=Advances+in+Biophysics&s=Search&f=source]]></link>
        <lastBuildDate>Sat, 10 Oct 2009 19:27:14 +0100</lastBuildDate>
        <item>
            <title>Structural and thermodynamic aspects of the hydrophobic effect.</title>
            <link>http://www.medworm.com/index.php?rid=369589&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8140943%26dopt%3DAbstract</link>
            <description>Authors: Soda K
    From analyses of the solvation structure around HS solutes for HS solvents and various water models by the RISM integral equation method, the following conclusions are drawn: 1) Water has more small cavities than HS solvents, which makes it easier for water to accommodate small solutes with a radius less than about 1A. 2) With increasing solute radius from 0 to 3A, the average orientation of hydrating water varies from an inward to an outward orientation, which shows that some reorganization of water occurs in response to the change in solute size. 3) The hydration structure is formed as a network structure due to H-bonding interactions between water molecules being supported by the cooperation of repulsive forces between solute and water. Repulsive interactions of not ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369589</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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        <item>
            <title>The mechanism of accumulation of high levels of vanadium by ascidians from seawater: biophysical approaches to a remarkable phenomenon.</title>
            <link>http://www.medworm.com/index.php?rid=369588&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8140944%26dopt%3DAbstract</link>
            <description>Authors: Michibata H
    
    PMID: 8140944 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369588</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369588</guid>        </item>
        <item>
            <title>Equilibrium muscle crossbridge behavior: the interaction of myosin crossbridges with actin.</title>
            <link>http://www.medworm.com/index.php?rid=369587&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8140945%26dopt%3DAbstract</link>
            <description>Authors: Schoenberg M
    The interaction of myosin crossbridges with actin under equilibrium conditions is reviewed. Similarities and differences between the weakly- and strongly-binding interactions of myosin crossbridges with actin filaments are discussed. A precise, narrow definition of weakly-binding crossbridges is given. It is postulated that the fundamental difference between the weakly- and strongly-binding equilibrium interaction of crossbridges with actin is that the crossbridge heads are mobile after attachment in the first case but not in the second. It is argued that because the weakly-binding crossbridge heads are mobile after attachment, the heads appear to function independently of each other. The lack of head mobility in attached strongly-binding crossbridges makes the st...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369587</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369587</guid>        </item>
        <item>
            <title>The mechanism of intracellular Ca2+ oscillation and electrical bursting in pancreatic beta-cells.</title>
            <link>http://www.medworm.com/index.php?rid=369586&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8140946%26dopt%3DAbstract</link>
            <description>Authors: Chay TR
    
    PMID: 8140946 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369586</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369586</guid>        </item>
        <item>
            <title>Structure of RecA-DNA complex and mechanism of DNA strand exchange reaction in homologous recombination.</title>
            <link>http://www.medworm.com/index.php?rid=369585&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7709802%26dopt%3DAbstract</link>
            <description>Authors: Takahashi M, Nordén B
    The importance of filament formation of RecA for the DNA strand exchange reaction, both in vivo and in vitro, is established. RecA forms a very long and relatively stiff filament by binding around DNA with high cooperativity. The monomer units are assembled in the filament in a head-to-tail arrangement in a helical manner, similar to the organization of RecA molecules found in the crystal of pure RecA or including ADP. This filament of RecA, containing a DNA molecule in its interior, can bind another DNA molecule and yet a third one in the presence of cofactor (ATP or its analogs). Each filament may have three DNA binding sites, each able to bind one DNA strand of either ss or ds DNA. According to linear dichroism and fluorescence spectroscopies, the DNA...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369585</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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            <title>Thermodynamics of protein folding: effects of hydration and electrostatic interactions.</title>
            <link>http://www.medworm.com/index.php?rid=369584&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7709803%26dopt%3DAbstract</link>
            <description>Authors: Ooi T
    DNA base sequences contain a variety of information, and this information flows from DNA to a protein through the steps of transcription and translation. The one dimensional information given from DNA is the amino acid sequence of the protein. In an organism, a nascent chain synthesized in vivo from the N-terminus according to the information in DNA folds spontaneously to a native conformation under a given environmental condition, i.e., water is the solvent and concentration of salts, pH, temperature, and pressure are appropriate. The polypeptide chain synthesized chemically from the C-terminus also folds to the native conformation, and often exhibits the proper enzymic activity. X-ray crystallography reveals the three dimensional structure of a protein in crystal, indi...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369584</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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        <item>
            <title>Conformational comparison between alpha-lactalbumin and lysozyme.</title>
            <link>http://www.medworm.com/index.php?rid=369583&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7709804%26dopt%3DAbstract</link>
            <description>Authors: Sugai S, Ikeguchi M
    Comparisons of the conformation behavior between LA and LZ (especially BLA and HEL) are described, which have contributed to the development and understanding of the molten globule folding intermediate of protein. BLA (and other LAs) is clearly a very good model protein for fundamental studies of molten globule protein conformation and the mechanism of protein unfolding/folding in vitro. Our work for about 20 years, on the conformational characterizations of proteins in the LA-LZ family, primarily based on macroscopic observations, led to three important findings: 1) equilibrium intermediate of unfolding/folding of LA is in the molten globule state, as assumed later for many proteins; 2) kinetic (transient) folding intermediates of BLA and HEL are the same ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369583</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369583</guid>        </item>
        <item>
            <title>Fundamental significance of DNA mass-sequencing factory for biological sciences in future.</title>
            <link>http://www.medworm.com/index.php?rid=369582&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7709805%26dopt%3DAbstract</link>
            <description>Authors: Wada A
    We are now entering an era of the mass-analysis of genetic information, which will signal the beginning of the study of living organisms on the basis of their most detailed plan: the DNA base-sequence. The researcher's essential requirement in reading and deciphering the DNA base-sequence is the precision, speed, reliability, and low cost of such operation. I have long stressed that these requirements can only be satisfied by establishing a centralized organization, a DNA sequencing factory, where a large-scale and international operation of the sequencing can be carried out with the assistance of high technologies and under an administration which equitably represents the research interests of researchers worldwide. In this context, the basic concept and aims of the Ja...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369582</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369582</guid>        </item>
        <item>
            <title>Meiosis specific transcription and functional proteins.</title>
            <link>http://www.medworm.com/index.php?rid=369581&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625268%26dopt%3DAbstract</link>
            <description>Authors: Hotta Y, Furukawa K, Tabata S
    We have discussed and/or demonstrated the following: 1. Many enzymes and structural proteins have been identified as meiosis-specific proteins. These can be classified according to their metabolic behavior. 2. We obtained and analyzed 18 cDNA clones from lily meiocytes. One of them, LIM15, was similar to known genes like RecA, RAD57, and DMC1/ISC2, and might function in pairing and recombination. 3. Transcription of these genes is regulated by their regulator region(s). When such a regulator, mei2 promoter sequence isolated from S. pombe, was ligated with the proper vector and transfected, it functioned specifically in meiotic cells but not in the somatic cells tested. 4. Presence of a new lamin, lamin B3 was identified in mammalian spermatocytes ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369581</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369581</guid>        </item>
        <item>
            <title>Hotspots of homologous recombination in mouse meiosis.</title>
            <link>http://www.medworm.com/index.php?rid=369580&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625269%26dopt%3DAbstract</link>
            <description>Authors: Shiroishi T, Koide T, Yoshino M, Sagai T, Moriwaki K
    The molecular mapping of recombinational breakpoints in the proximal region of the mouse MHC has revealed four hotspots at which breakpoints are clustered. A direct comparison of the nucleotide sequences of two independent hotspots revealed common molecular elements: a consensus sequence of the middle-repetitive MT-family, a repeat of tetramer sequences and a sequence homologous to a solitary LTR of mouse retroviruses. Extremely high frequency of recombination is observed at these hotspots when particular MHC haplotypes are used in genetic crosses. Wild mouse-derived wm7 haplotype instigates recombination at the hotspot located at the 3'-end of the Lmp-2 gene only during female meiosis. Fine genetic analysis demonstrated tha...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369580</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369580</guid>        </item>
        <item>
            <title>A new type of E. coli recombinational hotspot which requires for activity both DNA replication termination events and the Chi sequence.</title>
            <link>http://www.medworm.com/index.php?rid=369579&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625270%26dopt%3DAbstract</link>
            <description>Authors: Horiuchi T, Nishitani H, Kobayashi T
    In E. coli rnh- mutants we identified chromosome-derived, specific DNA fragments termed Hot DNA. When the DNA in the ccc form is integrated into the E. coli genome by homologous recombination to form a directly repeated structure, a striking enhancement of excisional recombination between the repeats occurs. We obtained 8 groups of such Hot DNA, 7 of which were clustered in a narrow region called the replication terminus region (about 280 kb) on the circular E. coli genome. A Ter site can impede the replication fork in a polar fashion. The six Ter sites are approximately symmetrical in the terminus and surrounding region. To block the fork at the Ter site, a protein factor, Ter binding protein encoded in the tau (or tus) gene, is required. ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369579</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369579</guid>        </item>
        <item>
            <title>A differential cloning procedure for rearranged or altered genomic DNA based on in-gel competitive reassociation.</title>
            <link>http://www.medworm.com/index.php?rid=369578&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625271%26dopt%3DAbstract</link>
            <description>Authors: Kiyama R, Inoue S, Ohki R, Kikuya E, Yokota H, Oishi M
    We have developed a substantially improved differential cloning procedure designed for cloning anonymous altered restriction DNA fragments from higher organisms. The improvements include (i) in-gel dissociation and reassociation of biotinylated restriction digests of target DNA fragments, (ii) replacement of agarose gel by a synthetic gel material for electrophoresis, (iii) use of a reassociation enhancing reagent (CTAB) for in-gel reassociation, and (iv) introduction of PCR. After several cycles of IGCR, we attained considerable enrichment of altered or rearranged DNA fragments which were originally present at one copy or less per complex eukaryotic genome. Examples of enrichment include those of an exogenously added DNA ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369578</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369578</guid>        </item>
        <item>
            <title>V(D)J recombination of immunoglobulin genes.</title>
            <link>http://www.medworm.com/index.php?rid=369577&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625272%26dopt%3DAbstract</link>
            <description>Authors: Oka C, Kawaichi M
    We have constructed transgenic mice carrying an artificial substrate of V(D)J recombination. In this substrate, the only DNA fragments derived from Ig genes were short stretches of recombination signal sequences. This artificial substrate was rearranged at high frequency in lymphocytes, although in non-lymphoid cells no rearrangement was detected even by a sensitive PCR assay. This result indicates that the V(D)J recombination requires only the signal sequences and that a recombination similar to the V(D)J recombination does not occur in non-lymphoid tissues including the central nervous tissue. A protein binding to the V(D)J recombination signals was purified and its cDNA was cloned. This protein, termed RBP-J kappa, was initially considered to be involved i...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369577</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369577</guid>        </item>
        <item>
            <title>Mating variation by DNA inversions of shufflon in plasmid R64.</title>
            <link>http://www.medworm.com/index.php?rid=369576&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625273%26dopt%3DAbstract</link>
            <description>Authors: Komano T, Kim SR, Yoshida T
    Gene organization of the 54-kb transfer region of IncI1 plasmid R64 was deduced from the DNA sequence. Forty-eight ORFs were found in this region. A unique DNA rearrangement designated shufflon is located at the downstream region of an operon responsible for synthesis of thin pilus. The shufflon of R64 consists of four DNA segments, designated as A, B, C, and D, which are flanked and separated by seven 19-bp repeat sequences. Site-specific recombination mediated by the product of the rci gene between any two inverted repeats results in a complex DNA rearrangement. An analysis of open reading frames revealed that the shufflon is a biological switch to select one of seven C-terminal segments of the pilV genes. The products of pilV genes were shown to ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369576</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369576</guid>        </item>
        <item>
            <title>A novel assay for illegitimate recombination in Escherichia coli: stimulation of lambda bio transducing phage formation by ultra-violet light and its independence from RecA function.</title>
            <link>http://www.medworm.com/index.php?rid=369575&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625274%26dopt%3DAbstract</link>
            <description>Authors: Ikeda H, Shimizu H, Ukita T, Kumagai M
    We developed a novel assay system for illegitimate recombination, in which the frequency of the formation of lambda Spi- phages formed during prophage induction was measured with an E. coli P2 lysogen as the indicator bacteria. Since almost all of the lambda Spi- phages thus detected contain attR, they have essentially the same structures as lambda bio transducing phages, indicating that this assay system enables us to detect specialized transducing phages that produce heterogenote transductants, thus ignoring the occurrences of docL and docR particles which carry only one cohesive end. The following results on the formation of specialized transducing phages have been obtained by this assay system to date. (1) Irradiation with UV light gr...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369575</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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        <item>
            <title>IS1-encoded proteins, InsA and the InsA-B'-InsB transframe protein (transposase): functions deduced from their DNA-binding ability.</title>
            <link>http://www.medworm.com/index.php?rid=369574&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625275%26dopt%3DAbstract</link>
            <description>Authors: Sekino N, Sekine Y, Ohtsubo E
    Insertion sequence IS1 encodes a transframe protein, InsA-B'-InsB, which is produced from two out-of-phase reading frames, insA and B'-insB, by translational frameshifting at a run of adenines. Unless the frameshifting event occurs, the InsA protein is produced from IS1. We found that cells harboring a plasmid carrying an IS1 mutant with a single adenine insertion in the run of adenines contained miniplasmids. Cloning and DNA sequencing analyses of the miniplasmids revealed that they had a deletion extending from an inverted repeat (IR) at the left end of IS1. This indicates that they were generated by IS1-mediated deletion due to efficient production of the InsA-B'-InsB transframe protein that is IS1 transposase. Both the InsA protein and transpo...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369574</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369574</guid>        </item>
        <item>
            <title>Analysis of the DNA binding site of Escherichia coli RecA protein.</title>
            <link>http://www.medworm.com/index.php?rid=369573&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625276%26dopt%3DAbstract</link>
            <description>Authors: Morimatsu K, Horii T
    To investigate the DNA binding site of RecA protein, we constructed 15 recA mutants having alterations in the regions homologous to the other ssDNA binding proteins. The in vivo analyses showed that the mutational change at Arg243, Lys248, Tyr264, or simultaneously at Lys6 and Lys19, or Lys6 and Lys23 caused severe defects in the recA functions, while other mutational changes did not. Purified RecA-K6A-K23A (Lys6 and Lys23 changed to Ala and Ala, respectively) protein was indistinguishable from the wild-type RecA protein in its binding to DNA. However, the RecA-R243A (Arg243 changed to Ala) and RecA-Y264A (Tyr264 changed to Ala) proteins were defective in binding to both ss- and ds-DNA. In self-oligomerization property, RecA-R243A was proficient but RecA-Y...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369573</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369573</guid>        </item>
        <item>
            <title>Recombination apparatus of T4 phage.</title>
            <link>http://www.medworm.com/index.php?rid=369572&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625277%26dopt%3DAbstract</link>
            <description>Authors: Yonesaki T
    The substantial process of general DNA recombination consists of production of ssDNA, exchange of the ssDNA and its homologous strand in a duplex, and cleavage of branched DNA to maturate recombination intermediates. Ten genes of T4 phage are involved in general recombination and apparently encode all of the proteins required for its own recombination. Several proteins among them interact with each other in a highly specific manner based on a protein-protein affinity and constitute a multicomponent protein machine to create an ssDNA gap essential for production of recombinogenic ssDNA, a machine to supply recombinogenic ssDNA which has a free end, or a machine to transfer the recombinogenic single strand into a homologous duplex.
    PMID: 7625277 [PubMed - indexed ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369572</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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            <title>Molecular mechanisms of Holliday junction processing in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=369571&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625278%26dopt%3DAbstract</link>
            <description>Authors: Shinagawa H, Iwasaki H
    Recent genetic and biochemical studies revealed the mechanisms of late stage of homologous recombination in E. coli. A central intermediate of recombination called &quot;Holliday structure&quot;, in which two homologous duplex DNA molecules are linked by a single-stranded crossover, is formed by the functions of RecA and several other proteins. The products of the ruvA and ruvB genes, which constitute an SOS regulated operon, form a functional complex that promotes migration of Holliday junctions by catalyzing strand exchange reaction, thus enlarging the heteroduplex region. RuvA is a DNA-binding protein specific for these junctions, and RuvB is a motor molecule for branch migration providing energy by hydrolyzing ATP. The product of the ruvC gene, which is not re...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369571</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
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        <item>
            <title>Functions of the yeast meiotic recombination genes, MRE11 and MRE2.</title>
            <link>http://www.medworm.com/index.php?rid=369570&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625279%26dopt%3DAbstract</link>
            <description>In conclusion, MRE genes are involved in the initiation of meiotic recombination through the formation of DSBs at recombination hot-spots in S. cerevisiae.
    PMID: 7625279 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369570</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369570</guid>        </item>
        <item>
            <title>Multi-site-specific endonucleases and the initiation of homologous genetic recombination in yeast.</title>
            <link>http://www.medworm.com/index.php?rid=369569&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625280%26dopt%3DAbstract</link>
            <description>Authors: Shibata T, Nakagawa K, Morishima N
    The notion that homologous recombination is a regulated biological process is not a familiar one. In yeasts, homologous recombination and most site-specific ones are initiated by site-specific double-stranded breaks that are introduced within cis-acting elements for the recombination. On the other hand, yeasts have a group of site-specific endonucleases (multi-site-specific endonucleases) that have a number of cleavage sites on each DNA. One of them, Endo.SceI of S. cerevisiae, was shown to introduce double-stranded breaks at a number of well-defined sites on the mitochondrial DNA in vivo. An Endo.SceI-induced double-stranded break was demonstrated to induce homologous recombination in mitochondria. Like the case of homologous recombination o...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369569</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369569</guid>        </item>
        <item>
            <title>A species-specific interaction of rad51 and rad52 proteins in eukaryotes.</title>
            <link>http://www.medworm.com/index.php?rid=369568&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D7625281%26dopt%3DAbstract</link>
            <description>Authors: Ogawa T, Shinohara A, Ikeya T
    The structures and properties of the Rad51 and Rad52 proteins in eukaryotes are described. Both proteins form a complex and are responsible for recombination and repair reactions. The N-terminal region of the Rad51 protein interacts with the C-terminal region of the Rad52 protein. Species-specific interaction is probably essential for the functioning of these genes.
    PMID: 7625281 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369568</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369568</guid>        </item>
        <item>
            <title>Biophysics: fifty years after Schrödinger.</title>
            <link>http://www.medworm.com/index.php?rid=369567&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781282%26dopt%3DAbstract</link>
            <description>Authors: Oosawa F
    
    PMID: 8781282 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369567</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369567</guid>        </item>
        <item>
            <title>Fluorescence photobleaching in DNA sequencing.</title>
            <link>http://www.medworm.com/index.php?rid=369566&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781283%26dopt%3DAbstract</link>
            <description>Authors: Chu B
    
    PMID: 8781283 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369566</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369566</guid>        </item>
        <item>
            <title>Multi-helical DNA-binding domains: their structures and modes of DNA-binding.</title>
            <link>http://www.medworm.com/index.php?rid=369565&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781284%26dopt%3DAbstract</link>
            <description>Authors: Suzuki M, Suckow J, Kisters-Woike B, Aramaki H, Makino K
    
    PMID: 8781284 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369565</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369565</guid>        </item>
        <item>
            <title>DNA conformation and its changes upon binding transcription factors.</title>
            <link>http://www.medworm.com/index.php?rid=369564&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781285%26dopt%3DAbstract</link>
            <description>Authors: Suzuki M, Loakes D, Yagi N
    
    PMID: 8781285 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369564</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369564</guid>        </item>
        <item>
            <title>Origin and early evolution of eukaryotes inferred from the amino acid sequences of translation elongation factors 1alpha/Tu and 2/G.</title>
            <link>http://www.medworm.com/index.php?rid=369563&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781286%26dopt%3DAbstract</link>
            <description>Authors: Hashimoto T, Hasegawa M
    
    PMID: 8781286 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369563</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369563</guid>        </item>
        <item>
            <title>Ribosome recycling by ribosome recycling factor (RRF)--an important but overlooked step of protein biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=369562&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8781287%26dopt%3DAbstract</link>
            <description>Authors: Janosi L, Hara H, Zhang S, Kaji A
    
    PMID: 8781287 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369562</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369562</guid>        </item>
        <item>
            <title>A systematic search of the data bases for sequences homologous to titan/connectin.</title>
            <link>http://www.medworm.com/index.php?rid=369561&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922098%26dopt%3DAbstract</link>
            <description>Authors: Kolmerer B, Olivieri N, Herrmann B, Labeit S
    
    PMID: 8922098 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369561</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369561</guid>        </item>
        <item>
            <title>cDNA sequence of rabbit cardiac titin/connectin.</title>
            <link>http://www.medworm.com/index.php?rid=369560&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922099%26dopt%3DAbstract</link>
            <description>Authors: Greaser ML, Sebestyen MG, Fritz JD, Wolff JA
    
    PMID: 8922099 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369560</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369560</guid>        </item>
        <item>
            <title>The super-repeats of titin/connectin and their interactions: glimpses at sarcomeric assembly.</title>
            <link>http://www.medworm.com/index.php?rid=369559&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922100%26dopt%3DAbstract</link>
            <description>Authors: Gautel M
    
    PMID: 8922100 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369559</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369559</guid>        </item>
        <item>
            <title>Elastic filaments in situ in striated muscle revealed by selective removal of thin filaments with plasma gelsolin.</title>
            <link>http://www.medworm.com/index.php?rid=369558&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922101%26dopt%3DAbstract</link>
            <description>Authors: Funatsu T
    
    PMID: 8922101 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369558</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369558</guid>        </item>
        <item>
            <title>Proteolytic cleavage of connectin/titin.</title>
            <link>http://www.medworm.com/index.php?rid=369557&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922102%26dopt%3DAbstract</link>
            <description>Authors: Suzuki A, Kim K, Ikeuchi Y
    
    PMID: 8922102 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369557</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369557</guid>        </item>
        <item>
            <title>Splitting of connectin/titin filaments into beta-connectin/T2 and a 1,200-kDa subfragment by 0.1 mM calcium ions.</title>
            <link>http://www.medworm.com/index.php?rid=369556&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922103%26dopt%3DAbstract</link>
            <description>Authors: Tatsumi R, Hattori A, Takahashi K
    
    PMID: 8922103 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369556</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369556</guid>        </item>
        <item>
            <title>Interaction of titin/connectin with the thick filament.</title>
            <link>http://www.medworm.com/index.php?rid=369555&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922104%26dopt%3DAbstract</link>
            <description>Authors: Trinick J
    
    PMID: 8922104 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369555</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369555</guid>        </item>
        <item>
            <title>Myomesin, M-protein and the structure of the sarcomeric M-band.</title>
            <link>http://www.medworm.com/index.php?rid=369554&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922105%26dopt%3DAbstract</link>
            <description>Authors: Van Der Ven PF, Obermann WM, Weber K, Fürst DO
    
    PMID: 8922105 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369554</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369554</guid>        </item>
        <item>
            <title>Structure and physiological functions of ubiquitous and tissue-specific calpain species. Muscle-specific calpain, p94, interacts with connectin/titin.</title>
            <link>http://www.medworm.com/index.php?rid=369553&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922106%26dopt%3DAbstract</link>
            <description>Authors: Sorimachi H, Kimura S, Kinbara K, Kazama J, Takahashi M, Yajima H, Ishiura S, Sasagawa N, Nonaka I, Sugita H, Maruyama K, Suzuki K
    
    PMID: 8922106 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369553</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369553</guid>        </item>
        <item>
            <title>Titin/connectin and nebulin: giant protein rulers of muscle structure and function.</title>
            <link>http://www.medworm.com/index.php?rid=369552&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922107%26dopt%3DAbstract</link>
            <description>Authors: Wang K
    
    PMID: 8922107 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369552</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369552</guid>        </item>
        <item>
            <title>Microscopic analysis of the elastic properties of connectin/titin and nebulin in myofibrils.</title>
            <link>http://www.medworm.com/index.php?rid=369551&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922108%26dopt%3DAbstract</link>
            <description>Authors: Ishiwata S, Yasuda K, Shindo Y, Fujita H
    
    PMID: 8922108 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369551</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369551</guid>        </item>
        <item>
            <title>Nebulin and nebulin-related proteins in striated muscle.</title>
            <link>http://www.medworm.com/index.php?rid=369550&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922109%26dopt%3DAbstract</link>
            <description>Authors: Horowits R, Luo G, Zhang JQ, Herrera AH
    
    PMID: 8922109 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369550</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369550</guid>        </item>
        <item>
            <title>Physiological significance of viscoelastic structures in myoplasm.</title>
            <link>http://www.medworm.com/index.php?rid=369549&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922110%26dopt%3DAbstract</link>
            <description>Authors: Takemori S, Yamaguchi M, Umazume Y
    
    PMID: 8922110 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369549</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369549</guid>        </item>
        <item>
            <title>Viscoelasticity and function of connectin/titin filaments in skinned muscle fibers.</title>
            <link>http://www.medworm.com/index.php?rid=369548&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922111%26dopt%3DAbstract</link>
            <description>Authors: Higuchi H
    
    PMID: 8922111 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369548</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369548</guid>        </item>
        <item>
            <title>Comparative aspects of muscle elastic proteins.</title>
            <link>http://www.medworm.com/index.php?rid=369547&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922112%26dopt%3DAbstract</link>
            <description>Authors: Kawamura Y, Ohtsuka H, Murata H, Maki S, Ohtani Y, Manabe T, Kimura S, Maruyama K
    
    PMID: 8922112 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369547</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369547</guid>        </item>
        <item>
            <title>Twitchin and related giant Ig superfamily members of C. elegans and other invertebrates.</title>
            <link>http://www.medworm.com/index.php?rid=369546&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922113%26dopt%3DAbstract</link>
            <description>Authors: Benian GM, Tang X, Tinley TL
    
    PMID: 8922113 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369546</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369546</guid>        </item>
        <item>
            <title>Structure and distribution of mini-titins.</title>
            <link>http://www.medworm.com/index.php?rid=369545&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922114%26dopt%3DAbstract</link>
            <description>Authors: Vibert P, York ML, Castellani L, Edelstein S, Elliott B, Nyitray L
    
    PMID: 8922114 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369545</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369545</guid>        </item>
        <item>
            <title>Modular proteins of insect muscle.</title>
            <link>http://www.medworm.com/index.php?rid=369544&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922115%26dopt%3DAbstract</link>
            <description>Authors: Bullard B, Leonard K
    
    PMID: 8922115 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369544</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369544</guid>        </item>
        <item>
            <title>Development of connectin/titin and nebulin in striated muscles of chicken.</title>
            <link>http://www.medworm.com/index.php?rid=369543&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D8922116%26dopt%3DAbstract</link>
            <description>Authors: Shimada Y, Komiyama M, Begum S, Maruyama K
    
    PMID: 8922116 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369543</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369543</guid>        </item>
        <item>
            <title>Protein arrays: concepts and subjects.</title>
            <link>http://www.medworm.com/index.php?rid=369542&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204123%26dopt%3DAbstract</link>
            <description>Authors: Nagayama K
    To adapt proteins, the materials in life, for use as materials in science and technology, we focused not only on the biological aspects (functional aspects) but also on the material aspects as matter (structural and physical aspects). Engineering with protein arrays will develop under such consideration and advance toward stable devices made of protein molecules. The protein arrays with 2D crystalline order provide a primary model of macroscopic protein-based devices. The combination of protein engineering, the leading edge of life science, and array engineering, the leading edge of materials science, will provide clues to the controlled integration of protein molecules to a form of functional supramolecules on proper surfaces.
    PMID: 9204123 [PubMed - indexed fo...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369542</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369542</guid>        </item>
        <item>
            <title>Lateral forces acting between particles in liquid films or lipid membranes.</title>
            <link>http://www.medworm.com/index.php?rid=369541&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204124%26dopt%3DAbstract</link>
            <description>Authors: Kralchevsky PA
    To investigate the mechanism of formation of 2D arrays of protein macromolecules in liquid films we carried out model experiments with micron-sized latex particles. The direct observations revealed that the process of ordering is triggered by attractive lateral capillary forces due to the overlap of the menisci formed around the particles. Two types of lateral capillary forces, flotation and immersion, can be distinguished, and a theory of these interactions is developed. Similar forces are operative between inclusions (proteins) incorporated in lipid membranes. We develop an appropriate model of a lipid bilayer, which is described as an elastic layer (the hydrocarbon chain region) sandwiched between two Gibbs dividing surfaces (the two headgroup regions). The r...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369541</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369541</guid>        </item>
        <item>
            <title>Significant role of electrostatic interactions for stabilization of protein assemblies.</title>
            <link>http://www.medworm.com/index.php?rid=369540&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204125%26dopt%3DAbstract</link>
            <description>This study offers a method which can improve the stability of protein crystals by introducing polar or charged residues that are properly designed to form specific hydrogen bonds or salt bridges between neighboring protein molecules. This method is also applicable to crystallography, because it improves refinement of protein structures in crystals by taking the inter-protein interactions into account.
    PMID: 9204125 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369540</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369540</guid>        </item>
        <item>
            <title>Criticality found in a model for orientational ordering of protein arrays.</title>
            <link>http://www.medworm.com/index.php?rid=369539&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204126%26dopt%3DAbstract</link>
            <description>Authors: Hogyoku M
    MC-PSRG analysis allowed us to reduce criticalities A, B, and C found in the poker chip model, respectively, to ones of the Ising universality, of the 3-state Potts universality, and of the KT-like phase. We note that not only the KT-like phase but also the Ising and 3-state Potts universality have been predicted to appear in the generalized 6-state clock model. We expect that the criticality inherent in actual protein array systems, whose Hamiltonians might be more complex than those of the poker chip model, can also be reduced to the criticality clarified with the aid of the naive models. However, we have to direct our attention to nonuniversal behavior like criticality C. Several two-dimensional systems having the two-component order parameter exhibit nonuniversal...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369539</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369539</guid>        </item>
        <item>
            <title>Advances in S-layer nanotechnology and biomimetics.</title>
            <link>http://www.medworm.com/index.php?rid=369538&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204127%26dopt%3DAbstract</link>
            <description>Authors: Sleytr UB, Pum D, Sára M
    Two-dimensional crystalline bacterial S-layers composed of identical protein or glycoprotein subunits turned out to be ideal materials for the development of biomimetic membranes and new approaches in molecular nanotechnology. These isoporous protein lattices have already been used as (i) structure for producing isoporous ultrafiltration membranes with very precisely defined molecular sieving properties, (ii) matrices for immobilizing monolayers of functional molecules, (iii) stabilizing structure for LB-films and liposomes, and (iv) patterning elements in molecular nanotechnology.
    PMID: 9204127 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369538</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369538</guid>        </item>
        <item>
            <title>Assembly process of 2D protein arrays in wetting films.</title>
            <link>http://www.medworm.com/index.php?rid=369537&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204128%26dopt%3DAbstract</link>
            <description>Authors: Adachi E, Nagayama K
    We were successful in developing a technique to form protein array developed directly on solid surfaces. This promising array formation revealed two new concepts of the ordering mechanism: the lifetime of a secondary minimum and secondary films. These concepts are not limited to our film formation technique. Any electrolytic thin film on a solid surfaces or any free film may contain a secondary film. If the secondary film can be retained in an electrolytic thin film for a sufficient period, a large single domain of small colloidal particles, such as proteins, fine metal particles, fine semi-conductive particles, etc., can be produced by an Alder-type transition.
    PMID: 9204128 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369537</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369537</guid>        </item>
        <item>
            <title>Two-dimensional crystals of apoferritin.</title>
            <link>http://www.medworm.com/index.php?rid=369536&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204129%26dopt%3DAbstract</link>
            <description>Authors: Yoshimura H
    A simple 2D crystallization method using unfolded protein film as a supporting film of crystals was described, which allows modification of protein surfaces by injecting chemical reagents into the subphase after the crystal formation. As an example, glutaraldehyde was used to cross-link adjacent proteins and then stabilize protein crystals. The second layer of other proteins can also be formed on the apoferritin array using cross-linkers. The array of apoferritin is not only beneficial for electron crystallography but also for practical applications. For example, apoferritin produces a mineral core with a size which can be adjusted by the size to the cavity (i.e. 6 nm). Fabrication of such a small size of well defined fine particles is currently not easy using phys...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369536</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369536</guid>        </item>
        <item>
            <title>Molecular handling of photosynthetic proteins for molecular assembly construction.</title>
            <link>http://www.medworm.com/index.php?rid=369535&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204130%26dopt%3DAbstract</link>
            <description>Authors: Miyake J, Hara M
    Methods of constructing proteins were examined with special reference to the molecular assembly using photosynthetic RCs as membrane proteins. Molecular assemblies at the interfaces were studied by LB films, adsorption to the surface and reconstitution into liposomes and bilayer lipid membranes. The applications of biological specific ligands (recognition and binding), combinatorial chemical method, 2-D and 3-D order array assemblies and modification of protein molecules to make fusion proteins, as well as physical methods of manipulation of molecules by AFM tips and electric fields were reviewed.
    PMID: 9204130 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369535</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369535</guid>        </item>
        <item>
            <title>Supramolecular assembly using helical peptides.</title>
            <link>http://www.medworm.com/index.php?rid=369534&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204131%26dopt%3DAbstract</link>
            <description>Authors: Fujita K, Kimura S, Imanishi Y, Rump E, Ringsdorf H
    We investigated supramolecular assemblies of various hydrophobic helical peptides. The assemblies were formed at the air/water interface or in aqueous medium. The hexadecapeptide, Boc-(Ala-Aib)s-OMe (BA16M), was reported to take alpha-helical structure by X-ray analysis. Several derivatives were prepared, which have the repeating sequence of Ala-Aib, Lys(Z)-Aib or Leu-Aib, or have the terminal chemically modified. CD spectra of the peptides indicated helical conformation in ethanol solution. The surface pressure-area isotherms of the peptide monolayers showed an inflection at the surface area corresponding to the cross section along the helix axis, and the monolayers were collapsed by further compression. All the helical pept...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369534</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369534</guid>        </item>
        <item>
            <title>Assembly of protein structures on liposomes by non-specific and specific interactions.</title>
            <link>http://www.medworm.com/index.php?rid=369533&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204132%26dopt%3DAbstract</link>
            <description>Authors: Velev OD
    We investigate different schemes for fabrication of nanometer sized assemblies that consist of a liposome core over which a shell of ferritin is attached. Three distinct interactions were used for this assembly: (i) Electrostatic attraction. The liposomes are charged by the presence of cationic surfactant (HTAB) and at an appropriate pH collect the ferritin molecules into a 2D-ordered ferritin shell. The protein shells can be fixed by glutaraldehyde. Next, the liposomes can be removed by solubilisation, leaving behind ordered ferritin clusters. (ii) Specific avidin-biotin or streptavidin-biotin binding. The ferritin molecules are conjugated to avidin or streptavidin and the liposomes incorporate biotinylated lipid. We found that the specific binding can be completely ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369533</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369533</guid>        </item>
        <item>
            <title>Electron crystallography of macromolecular periodic arrays on phospholipid monolayers.</title>
            <link>http://www.medworm.com/index.php?rid=369532&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204133%26dopt%3DAbstract</link>
            <description>Authors: Chiu W, Avila-Sakar AJ, Schmid MF
    Electron crystallography has the potential of yielding structural information equivalent to x-ray diffraction. The major difficulty has been preparing specimens with the required structural order and size for diffraction and imaging in the electron microscope. 2D crystallization on phospholipid monolayers is capable of fulfilling both of these requirements. Crystals can form as a result of specific interactions with a protein's ligand or an analog, suitably linked to a lipid tail; or on a surface of complementary head-group charge. With such choices, the availability of a suitable lipid is limited only by synthetic chemistry. Ultimately, it is the quality and regularity of the protein-protein interactions that determine the crystalline order, ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369532</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369532</guid>        </item>
        <item>
            <title>The influence of protein and interfacial structure on the self-assembly of oriented protein arrays.</title>
            <link>http://www.medworm.com/index.php?rid=369531&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204134%26dopt%3DAbstract</link>
            <description>Authors: Leckband DE
    These results demonstrate the complexity of factors that impact the self-assembly of protein arrays via the specific binding to receptor-functionalized interfaces. Both the composition and colloidal properties of the protein and target membrane surfaces will affect the protein-surface interactions. However, different structural features control the interactions over different distance regimes and with different consequences. The long-range interactions that control the adsorption kinetics are sensitive not only to the charge on the target surface but also by the topological charge distribution on the protein exterior. Short-range repulsive interactions rooted in both the protein topology and in the membrane structure, by contrast, can significantly alter both the r...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369531</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369531</guid>        </item>
        <item>
            <title>Single molecular functional assay of ferritin arrays.</title>
            <link>http://www.medworm.com/index.php?rid=369530&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204135%26dopt%3DAbstract</link>
            <description>Authors: Yamaki M
    In situ functional assay of each ferritin molecule in single-layer 2D arrays for horse spleen apoferritin and recombinant horse L- and human H-apoferritins was conducted by observing the iron-cores formed in the arrays by TEM. The study of the time-course, pH-dependence, and temperature-dependence of the function confirmed the iron-core formation to be due to the native function of apoferritins in array. Dark-field TEM imaging revealed that there was crystallinity in the cores in the array of recombinant human H-apoferritin. This iron-core formation was perfectly preserved in the array even after 3 months of storage at room temperature and low humidity. Moreover, about 50% of the function was found to remain in the array after it was exposed to 150 degrees C in vacuum...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369530</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369530</guid>        </item>
        <item>
            <title>Novel biosensoric devices based on molecular protein hetero-multilayer films.</title>
            <link>http://www.medworm.com/index.php?rid=369529&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204136%26dopt%3DAbstract</link>
            <description>Authors: Diederich A, Lösche M
    We have developed a novel concept for the modification of technical surfaces with molecularly well-organized layers of bioorganic components. A molecular construction set has been used to implement this concept which is based on molecularly stratified polyelectrolyte films as a structure decoupling protein layers from solid substrates. Utilizing this technology, one can start from a number of different substrates to obtain the same surface structures, on which protein hetero-multilayer films can be prepared to functionalize the interface for (potentially very different) purposes. We have demonstrated the viability of this concept by constructing a biosensor surface that was characterized by x-ray, spectroscopic, and immunological techniques. For the prep...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369529</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369529</guid>        </item>
        <item>
            <title>Supramolecular architectures for the functionalization of solid surfaces.</title>
            <link>http://www.medworm.com/index.php?rid=369528&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204137%26dopt%3DAbstract</link>
            <description>Authors: Knoll W, Liley M, Piscevic D, Spinke J, Tarlov MJ
    Surface plasmon optical techniques are described as sensitive tools that allow for the on-line characterization of supramolecular biofunctional architectures at solid/solution interfaces. After a short introduction into the fundamentals of surface plasmon optics the observation of the build up of a functional bio-interface by the self-assembly process of long chain thiolates at an Au surface is described. Criteria are developed for tailoring the SAM architectures optimized for maximum protein binding from solution by specific bio-recognition reactions. SPM is employed to image the selective binding of streptavidin to a functionalized SAM laterally patterned by UV-photolithographic techniques.
    PMID: 9204137 [PubMed - indexed...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369528</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369528</guid>        </item>
        <item>
            <title>Natural and artificial carbohydrate-glued protein aggregates.</title>
            <link>http://www.medworm.com/index.php?rid=369527&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9204138%26dopt%3DAbstract</link>
            <description>Authors: Matsubara K, Ebina S
    Carbohydrate gluing (which may have a carbohydrate-lectin binding mechanism) was first recognized as a major contributor in the supramolecular assembly of annelid giant Hb from the marine-worm P. aibuhitensis. Although this assembly obviously also relies on protein-protein interactions, the authors tested the application of carbohydrate gluing in the assembly of a protein aggregate using a lectin and a carbohydrate-containing protein. The resultant aggregate was a mixture of the protein aggregate and the ingredient proteins. The significance of the method is that the assembly of the aggregate can be controlled by using a hapten sugar. This controllability, in conjunction with newly developing glyco-technology, has great potential for the construction of ar...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369527</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369527</guid>        </item>
        <item>
            <title>Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II.</title>
            <link>http://www.medworm.com/index.php?rid=369526&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9949764%26dopt%3DAbstract</link>
            <description>Authors: Sasaki N, Sutoh K
    Three loop structures called the P-loop, switch I loop and switch II loop of myosin are major components of its ATPase site, and share structural and functional homology with the loop structures in other ATPases and GTPases such as kinesin and G-protein. Using the alanine scanning mutagenesis, structure-function relationship of the switch I and switch II loops in Dictyostelium myosin II was examined. Based on crystal structures of Dictyostelium myosin motor domain, functions of each residue in those loops are discussed.
    PMID: 9949764 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369526</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369526</guid>        </item>
        <item>
            <title>The structural study of membrane proteins by electron crystallography.</title>
            <link>http://www.medworm.com/index.php?rid=369525&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9949765%26dopt%3DAbstract</link>
            <description>Authors: Fujiyoshi Y
    A high-resolution electron cryo-microscope equipped with a top-entry specimen stage has been refined by modifying a previously described superfluid helium stage. Instruments equipped with such a cryo-stage achieve a resolution of better than 2.0 A and have proved extremely powerful in the high-resolution structure analysis of membrane proteins. Improvement of the electron microscopic system in combination with improved specimen preparation techniques allowed the structure of bR to be analyzed to a resolution of 3.0 A. The 3D structure of bR, especially the surface features, revealed the structural basis for the efficient guidance of protons to the entrance of the transmembrane channel. Based on the characteristic difference of the atomic scattering factors for elec...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369525</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369525</guid>        </item>
        <item>
            <title>Neural systems for control of voluntary action--a hypothesis.</title>
            <link>http://www.medworm.com/index.php?rid=369524&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9949766%26dopt%3DAbstract</link>
            <description>Authors: Hikosaka O
    Action is the means by which we and animals survive. It consists of a complex combination of movements which are either innately endowed or acquired by learning. In this article, I propose a hypothesis on the relationship between the organization of action and the organization of the brain. Innate and learned actions are controlled by different levels of neural networks: innate actions are controlled by reflex mechanisms and pattern generators in the spinal cord and brainstem, while learned actions are controlled by the cerebral cortex, basal ganglia, and cerebellum. However, these mechanisms are by no means independent. Phylogenetically, animals have acquired progressively more complex actions by gaining neural connections between different neural mechanisms. This ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369524</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369524</guid>        </item>
        <item>
            <title>The neuronal basis of visual memory and imagery in the primate: a neurophysiological approach.</title>
            <link>http://www.medworm.com/index.php?rid=369523&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9949767%26dopt%3DAbstract</link>
            <description>Authors: Nakahara K, Ohbayashi M, Tomita H, Miyashita Y
    To understand the biological basis of memory is one of the most exciting frontiers of science. Single unit recording is a powerful method to investigate neuronal correlates of various brain functions such as memory in awake animals. Anatomical, neuropsychological, and neurophysiological evidence indicates that the IT has an important role not only for synthesizing the analyzed visual attribute into a unique configuration, but also for the storehouse of visual memory in humans and primates. We performed single unit recordings in the primate IT, and found neuronal correlates of visual long-term memory: the IT neurons could reflect learned associative relations among stimuli. The findings reviewed here support the hypothesis that the...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369523</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369523</guid>        </item>
        <item>
            <title>Design of protein function by physical perturbation method.</title>
            <link>http://www.medworm.com/index.php?rid=369522&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D9949768%26dopt%3DAbstract</link>
            <description>Authors: Kidokoro S
    Based on three-dimensional structure of proteins, a rational strategy to design the protein function by physical perturbation method was proposed and tested on one of the well-examined enzymes, thermolysin for higher catalytic activity. An attempt was made to change the electrostatic potential and the dynamic property of three-dimensional structure around the active sites by single-amino-acid mutations, and the physical property of the mutants was then evaluated. Several mutants were found to have remarkably higher enzymatic activity than wild type. The multiple mutation was introduced and the logarithm of the activity was found to be almost additive. A ten times higher active mutant was realized by simultaneously introducing three single-mutations. This strategy ca...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369522</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369522</guid>        </item>
        <item>
            <title>Biophysical studies on ATP synthase.</title>
            <link>http://www.medworm.com/index.php?rid=369521&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D10463071%26dopt%3DAbstract</link>
            <description>Authors: Kagawa Y
    The isolation of ATP synthase (F0F1) (82) and F0 (83) 34 years ago finally revealed that F0F1 is a motor composed of F0 (ion-motor, abc subunits) and F1 (ATP-motor, alpha 3 beta 3 gamma delta epsilon subunits) (Fig. 1). The single molecule videotape (4, 5, 65, 66) revealed that gamma epsilon axis of F1 rotates counterclockwise, proceeds by each 2 pi/3 step, and is driven by torque of 42 pN.nm (12) with nearly 100% efficiency (5) (Fig. 4). The motor is composed of a rotor (gamma epsilon-F0-c) and a stator (alpha 3 beta 3 delta-F0-ab), and the rotor is connected to a shaft (gamma epsilon). Since F0F1 is driven by delta microH+ (9, 10, 84), biophysical studies on stable TF0F1 (1, 7) are essential to elucidate the mechanism. These include nanomechanics (4, 5) (Fig. 4), cr...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369521</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369521</guid>        </item>
        <item>
            <title>Ryanodine receptor isoforms in excitation-contraction coupling.</title>
            <link>http://www.medworm.com/index.php?rid=369520&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D10463072%26dopt%3DAbstract</link>
            <description>Authors: Ogawa Y, Kurebayashi N, Murayama T
    Three genomically distinct isoforms of RyR are now known. RyR1 homologue is the primary isoform in skeletal muscles, whereas in cardiac muscles it is RyR2 homologue. RyR3 homologue occurs ubiquitously in many cells, but the biological function is little known, partly because of its minuscule amount in mammalian cells. The difference among RyR isoforms may not be so great in CICR activity, in other words, in the interaction of RyR isoforms with Ca2+, adenine nucleotides and caffeine. Species specificity among RyR1 homologues may be more important in the apparent difference between RyR1 and RyR3 homologues. CICR is likely to be the dominant underlying mechanism for E-C coupling in the cardiac muscle and probably in cells other than the skeletal...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369520</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369520</guid>        </item>
        <item>
            <title>Evolution of the carabid ground beetles.</title>
            <link>http://www.medworm.com/index.php?rid=369519&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D10463073%26dopt%3DAbstract</link>
            <description>Authors: Osawa S, Su ZH, Kim CG, Okamoto M, Tominaga O, Imura Y
    The phylogenetic relationships of the carabid ground beetles have been estimated by analysing a large part of the ND5 gene sequences of more than 1,000 specimens consisting of the representative species and geographic races covering most of the genera and subgenera known in the world. From the phylogenetic analyses in conjunction with the mtDNA-based dating, a scenario of the establishment of the present habitats of the respective Japanese carabids has been constructed. The carabid diversification took place ca. 40 MYA as an explosive radiation of the major genera. During evolution, occasional small or single bangs also took place, sometimes accompanied by parallel morphological evolution in phylogenetically remote as well...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369519</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369519</guid>        </item>
        <item>
            <title>Induced potential model of muscular contraction mechanism and myosin molecular structure.</title>
            <link>http://www.medworm.com/index.php?rid=369518&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D10463074%26dopt%3DAbstract</link>
            <description>Authors: Mitsui T
    The proposed model is characterized by the constant r (Eq. 2-1), the induced potential (Fig. 1), two attached states of a myosin head (Fig. 1), the nonlinear elastic property of the crossbridge (Eq. 2-7), and the expression of U* (Eqs. 3-8 and 3-9), which led us to the following conclusions. 1. The following various magnitudes of myosin head motion are compatible with each other: about 2 nm of the quantity called power stroke by Irving (27), which is the mean moving distance of myosin head in the isometric tension in our model, 4-5 nm of the displacement of a single myosin head during one ATP hydrolysis cycle (Molloy et al. (20)) or a few tens of nm when the actin and myosin filaments are set parallel (Tanaka et al. (21) and Kitamura et al. (42)), and more than 200 nm...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369518</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369518</guid>        </item>
        <item>
            <title>Multiple sequence alignment: algorithms and applications.</title>
            <link>http://www.medworm.com/index.php?rid=369517&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D10463075%26dopt%3DAbstract</link>
            <description>Authors: Gotoh O
    Elucidation of interrelationships among sequence, structure, function, and evolution (FESS relationships) of a family of genes or gene products is a central theme of modern molecular biology. Multiple sequence alignment has been proven to be a powerful tool for many fields of studies such as phylogenetic reconstruction, illumination of functionally important regions, and prediction of higher order structures of proteins and RNAs. However, it is far too trivial to automatically construct a multiple alignment from a set of related sequences. A variety of methods for solving this computationally difficult problem are reviewed. Several important applications of multiple alignment for elucidation of the FESS relationships are also discussed. For a long period, progressive m...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369517</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369517</guid>        </item>
        <item>
            <title>Brain neurosteroids are 4th generation neuromessengers in the brain: cell biophysical analysis of steroid signal transduction.</title>
            <link>http://www.medworm.com/index.php?rid=369516&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D12954551%26dopt%3DAbstract</link>
            <description>Authors: Kawato S, Yamada M, Kimoto T
    
    PMID: 12954551 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369516</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369516</guid>        </item>
        <item>
            <title>Fertilization and development initiation in orthodox and unorthodox ways: from normal fertilization to cloning.</title>
            <link>http://www.medworm.com/index.php?rid=369515&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D12954552%26dopt%3DAbstract</link>
            <description>Authors: Yanagimachi R
    
    PMID: 12954552 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369515</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369515</guid>        </item>
        <item>
            <title>Studies and perspectives of calponin in smooth muscle regulation and cancer gene therapy.</title>
            <link>http://www.medworm.com/index.php?rid=369514&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D12954553%26dopt%3DAbstract</link>
            <description>Authors: Takahashi K, Yamamura H
    
    PMID: 12954553 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369514</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369514</guid>        </item>
        <item>
            <title>Preface.</title>
            <link>http://www.medworm.com/index.php?rid=369513&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476888%26dopt%3DAbstract</link>
            <description>Authors: Ebashi S, Noda H
    
    PMID: 15476888 [PubMed - as supplied by publisher] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369513</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369513</guid>        </item>
        <item>
            <title>Preface to volume 38.</title>
            <link>http://www.medworm.com/index.php?rid=369512&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476889%26dopt%3DAbstract</link>
            <description>Authors: Ikeda H, Iida S, Ohtsubo E
    
    PMID: 15476889 [PubMed - as supplied by publisher] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369512</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369512</guid>        </item>
        <item>
            <title>Illegitimate recombination mediated by double-strand break and end-joining in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=369511&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476890%26dopt%3DAbstract</link>
            <description>Authors: Ikeda H, Shiraishi K, Ogata Y
    The frequency of illegitimate recombination has been measured by a lambdabio transducing phage assay during the induction of the E. coli lambda c1857 lysogen. Illegitimate recombination falls into two classes, short homology-independent and short homology-dependent illegitimate recombination. The former involves sequences with virtually no homology, and is mediated by DNA topoisomerases and controlled by the DNA binding protein HU. The latter is induced by UV irradiation or other DNA damaging agents and requires short regions of homology, usually contain 4 to 13 base pairs, at sites involved in recombination. It has been shown that the RecJ exonuclease promotes short homology-dependent illegitimate recombination, but that the RecQ helicase suppres...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369511</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369511</guid>        </item>
        <item>
            <title>Genetic and physiological regulation of non-homologous end-joining in mammalian cells.</title>
            <link>http://www.medworm.com/index.php?rid=369510&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476891%26dopt%3DAbstract</link>
            <description>Authors: Tachibana A
    Repair of DSBs is important to prevent chromosomal fragmentation, translocations and deletions. To investigate the process in NHEJ, we have established an in vitro system to clarify the measurement and analysis of the efficiency and the fidelity of rejoining of DSBs, and applied the method to investigate NHEJ in human cells derived from patients suffering from cancer-prone hereditary diseases. A DSB was introduced in plasmid pZErO-2 at a specific site within the ccdB gene that is lethal to E. coli cells, and treated with nuclear extracts from human cells. The efficiency of rejoining in the nuclear extract from an A-T cell line was comparable to that from a control cell line. However, the accuracy of rejoining was much lower for the A-T cell extract than for the con...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369510</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369510</guid>        </item>
        <item>
            <title>The function of RecQ helicase gene family (especially BLM) in DNA recombination and joining.</title>
            <link>http://www.medworm.com/index.php?rid=369509&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476892%26dopt%3DAbstract</link>
            <description>Authors: Kaneko H, Fukao T, Kondo N
    Bloom syndrome is a rare autosomal recessive genetic disorder characterized by lupus-like erythematous telangiectasias of the face, sun sensitivity, stunted growth, and immunodeficiency. Chromosome instability syndromes have a common feature, being associated at high frequency with neoplasia. BS is considered as one of the chromosome instability syndromes since the fibroblasts or lymphocytes of BS patients show excessive spontaneous chromosome instability. The causative gene of BS (BLM) was identified as a RecQ helicase homologue. In this review, we showed the characteristic phenotypes of BS, especially two Japanese siblings. In the latter of the review, the functional domains of BLM, those are nuclear localization signal and the interacting proteins...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369509</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369509</guid>        </item>
        <item>
            <title>Nijmegen breakage syndrome and DNA double strand break repair by NBS1 complex.</title>
            <link>http://www.medworm.com/index.php?rid=369508&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476893%26dopt%3DAbstract</link>
            <description>Authors: Matsuura S, Kobayashi J, Tauchi H, Komatsu K
    The isolation of the NBS1 gene revealed the molecular mechanisms of DSB repair. In response to DNA damage, histone H2AX in the vicinity of DSBs is phosphorylated by ATM. NBS1 then targets the MRE11/RAD50 complex to the sites of DSBs through interaction of the FHA/BRCT domain with gamma-H2AX. NBSI complex binds to damaged-DNA directly, and HR repair is initiated. To collaborate DSB repair, ATM also regulates cell cycle checkpoints at GI, G2, and intra-S phases via phosphorylation of SMC, CHK2 and FANCD2. The phosphorylation of these proteins require NBS1 complex. Thus, NBSI has at least two important roles in genome maintenance, as a DNA repair protein in HR pathway and as a signal modifier in intra-S phase checkpoints. NBSI is also ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369508</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369508</guid>        </item>
        <item>
            <title>Cell death promoted by homologous DNA interaction from bacteria to humans.</title>
            <link>http://www.medworm.com/index.php?rid=369507&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476894%26dopt%3DAbstract</link>
            <description>Authors: Kusano K
    Pairing between homologous DNA controls cellular functions including double-strand break repair, mitotic recombination, and progression of DNA replication forks, as well as chiasma formation during meiosis. Here I summarize that homologous interaction could promote the cell killing in bacteria, yeast, and multicellular organisms. The mechanisms of cell killing are categorized into two types: (1) the killing due to the accumulation of extrachromosomal DNA; (2) the killing induced by Holliday junction structures. I propose that the mechanisms of such killing function as novel apoptotic pathways in the cells carrying severe DNA damages to eliminate such damages from cell population.
    PMID: 15476894 [PubMed - as supplied by publisher] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369507</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369507</guid>        </item>
        <item>
            <title>Gpt delta transgenic mouse: A novel approach for molecular dissection of deletion mutations in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=369506&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476895%26dopt%3DAbstract</link>
            <description>Authors: Nohmi T, Masumura KI
    Human genome is continuously exposed to various DNA damaging agents including reactive oxygen species. Of various forms of DNA damage, double-strand breaks (DSBs) in DNA are the most detrimental because of the mutagenicity and cytotoxicity. To combat the serious threats posed by DSBs, cells evolved various homologous and non-homologous recombination repair mechanisms. However, some repair mechanisms appear to be involved in the induction of genome rearrangements such as deletions. To analyze the deletion mutations in a whole body system, gpt delta mice were established. In this mouse model, deletions in lambda, DNA integrated in the chromosome are preferentially selected as Spi(-) phages, which can then be subjected for molecular analysis. Here, we reporte...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369506</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369506</guid>        </item>
        <item>
            <title>Intermediate molecules generated by transposase in the pathways of transposition of bacterial insertion element 1S3.</title>
            <link>http://www.medworm.com/index.php?rid=369505&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476896%26dopt%3DAbstract</link>
            <description>Authors: Ohtsubo E, Minematsu H, Tsuchida K, Ohtsubo H, Sekine Y
    
    PMID: 15476896 [PubMed - as supplied by publisher] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369505</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369505</guid>        </item>
        <item>
            <title>Genetics and epigenetics in flower pigmentation associated with transposable elements in morning glories.</title>
            <link>http://www.medworm.com/index.php?rid=369504&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476897%26dopt%3DAbstract</link>
            <description>Authors: Iida S, Morita Y, Choi JD, Park KI, Hoshino A
    Among the genus Ipomoea, three morning glories, I. nil the Japanese morning glory), I. purpurea (the common morning glory), and I. tricolor, were domesticated well for floricultural plants, and many spontaneous mutants displaying various flower pigmentation patterns were isolated. Most of these spontaneous mutations were found to be caused by the insertion of DNA transposable elements in the genes for the anthocyanin pigmentation in flowers, and many of them exhibited variegated flowers, such as white flowers with pigmented spots and sectors. Here, we describe the historical background of the mutants displaying variegated flowers and review the genetic and epigenetic regulation in flower pigmentation associated with transposable el...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369504</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369504</guid>        </item>
        <item>
            <title>Transposition mechanisms and biothechnology applications of the medaka fish tol2 transposable element.</title>
            <link>http://www.medworm.com/index.php?rid=369503&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476898%26dopt%3DAbstract</link>
            <description>Authors: Koga A
    The Tol2 element of the medaka fish is a member of the hAT (hobo/Activator/Tam3) transposable element family. About 20 copies are present in the medaka fish genome and, unlike many other hAT family elements, virtually all the copies are autonomous or potentially autonomous, containing an intact transposase gene. Excision of Tol2 is not precise at the nucleotide sequence level, excision footprints being heterogeneous. In more than half of excision events, however, breakage and rejoining of DNA molecules occur within the 8-bp target site duplication region, removing the entire Tol2 sequence and retaining parts of the target site duplications. In the reminder of the excision events, either the left or the right terminal region is left and the other end is lost together wit...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369503</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369503</guid>        </item>
        <item>
            <title>Structure and function of the shufflon in plasmid r64.</title>
            <link>http://www.medworm.com/index.php?rid=369502&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476899%26dopt%3DAbstract</link>
            <description>Authors: Gyohda A, Furuya N, Ishiwa A, Zhu S, Komano T
    Conservative site-specific recombination plays key roles in creating biological diversity in prokaryotes. Most site-specific inversion systems consist of two recombination sites and a recombinase gene. In contrast, the shufflon multiple inversion system of plasmid R64 consists of seven sfx recombination sites, which separate four invertible DNA segments, and the rci gene encoding a site-specific recombinase of the integrase family. The rci product mediates recombination between any two inverted sfx sites, resulting in the inversion of four DNA segments independently or in groups. Random shufflon inversions construct seven pilV genes encoding constant N-terminal segment with different C-terminal segments. The pilV products are tip-l...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369502</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369502</guid>        </item>
        <item>
            <title>Molecular mechanism of vde-initiated intein homing in yeast nuclear genome.</title>
            <link>http://www.medworm.com/index.php?rid=369501&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15476900%26dopt%3DAbstract</link>
            <description>Authors: Fukuda T, Nagai Y, Ohya Y
    In Saccharomyces cerevisiae, VMAI intein encodes a homing endonuclease termed VDE which is produced by an autocatalytic protein splicing reaction. VDE introduces a DSB at its recognition sequence on intein-minus allele, resulting in the lateral transfer of VMAI intein. In this review, we summarize a decade of in vitro study on VDE and describe our recent study on the in vivo behavior of both VDE and host proteins involved in intein mobility. Meiotic DSBs caused by VDE are repaired in the similar pathway to that working in meiotic recombination induced by Spollp-mediated DSBs. Meiosis-specific DNA cleavage and homing is shown to be guaranteed by the two distinct mechanisms, the subcellular localization of VDE and a requirement of premeiotic DNA replica...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369501</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369501</guid>        </item>
        <item>
            <title>Illegitimate recombination mediated by double-strand break and end-joining in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=369500&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493325%26dopt%3DAbstract</link>
            <description>Authors: Ikeda H, Shiraishi K, Ogata Y
    The frequency of illegitimate recombination has been measured by a lambda bio transducing phage assay during the induction of the E. coli lambda cI857 lysogen. Illegitimate recombination falls into two classes, short homology-independent and short homology-dependent illegitimate recombination. The former involves sequences with virtually no homology, and is mediated by DNA topoisomerases and controlled by the DNA binding protein HU. The latter is induced by UV irradiation or other DNA damaging agents and requires short regions of homology, usually contain 4 to 13 base pairs, at sites involved in recombination. It has been shown that the RecJ exonuclease promotes short homology-dependent illegitimate recombination, but that the RecQ helicase suppre...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369500</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369500</guid>        </item>
        <item>
            <title>Genetic and physiological regulation of non-homologous end-joining in mammalian cells.</title>
            <link>http://www.medworm.com/index.php?rid=369499&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493326%26dopt%3DAbstract</link>
            <description>Authors: Tachibana A
    Repair of DSBs is important to prevent chromosomal fragmentation, translocations and deletions. To investigate the process in NHEJ, we have established an in vitro system to clarify the measurement and analysis of the efficiency and the fidelity of rejoining of DSBs, and applied the method to investigate NHEJ in human cells derived from patients suffering from cancer-prone hereditary diseases. A DSB was introduced in plasmid pZErO-2 at a specific site within the ccdB gene that is lethal to E. coli cells, and treated with nuclear extracts from human cells. The efficiency of rejoining in the nuclear extract from an A-T cell line was comparable to that from a control cell line. However, the accuracy of rejoining was much lower for the A-T cell extract than for the con...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369499</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369499</guid>        </item>
        <item>
            <title>The function of RecQ helicase gene family (especially BLM) in DNA recombination and joining.</title>
            <link>http://www.medworm.com/index.php?rid=369498&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493327%26dopt%3DAbstract</link>
            <description>Authors: Kaneko H, Fukao T, Kondo N
    Bloom syndrome is a rare autosomal recessive genetic disorder characterized by lupus-like erythematous telangiectasias of the face, sun sensitivity, stunted growth, and immunodeficiency. Chromosome instability syndromes have a common feature, being associated at high frequency with neoplasia. BS is considered as one of the chromosome instability syndromes since the fibroblasts or lymphocytes of BS patients show excessive spontaneous chromosome instability. The causative gene of BS (BLM) was identified as a RecQ helicase homologue. In this review, we showed the characteristic phenotypes of BS, especially two Japanese siblings. In the latter of the review, the functional domains of BLM, those are nuclear localization signal and the interacting proteins...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369498</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369498</guid>        </item>
        <item>
            <title>Nijmegen breakage syndrome and DNA double strand break repair by NBS1 complex.</title>
            <link>http://www.medworm.com/index.php?rid=369497&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493328%26dopt%3DAbstract</link>
            <description>Authors: Matsuura S, Kobayashi J, Tauchi H, Komatsu K
    The isolation of the NBS1 gene revealed the molecular mechanisms of DSB repair. In response to DNA damage, histone H2AX in the vicinity of DSBs is phosphorylated by ATM. NBS1 then targets the MRE11/RAD50 complex to the sites of DSBs through interaction of the FHA/BRCT domain with gamma-H2AX. NBS1 complex binds to damaged-DNA directly, and HR repair is initiated. To collaborate DSB repair, ATM also regulates cell cycle checkpoints at G1, G2, and intra-S phases via phosphorylation of SMC, CHK2 and FANCD2. The phosphorylation of these proteins require NBS1 complex. Thus, NBS1 has at least two important roles in genome maintenance, as a DNA repair protein in HR pathway and as a signal modifier in intra-S phase checkpoints. NBS1 is also ...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369497</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369497</guid>        </item>
        <item>
            <title>Cell death promoted by homologous DNA interaction from bacteria to humans.</title>
            <link>http://www.medworm.com/index.php?rid=369494&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493329%26dopt%3DAbstract</link>
            <description>Authors: Kusano K
    Pairing between homologous DNA controls cellular functions including double-strand break repair, mitotic recombination, and progression of DNA replication forks, as well as chiasma formation during meiosis. Here I summarize that homologous interaction could promote the cell killing in bacteria, yeast, and multicellular organisms. The mechanisms of cell killing are categorized into two types: (1) the killing due to the accumulation of extrachromosomal DNA; (2) the killing induced by Holliday junction structures. I propose that the mechanisms of such killing function as novel apoptotic pathways in the cells carrying severe DNA damages to eliminate such damages from cell population.
    PMID: 15493329 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369494</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369494</guid>        </item>
        <item>
            <title>Gpt delta transgenic mouse: a novel approach for molecular dissection of deletion mutations in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=369491&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493330%26dopt%3DAbstract</link>
            <description>Authors: Nohmi T, Masumura K
    Human genome is continuously exposed to various DNA damaging agents including reactive oxygen species. Of various forms of DNA damage, double-strand breaks (DSBs) in DNA are the most detrimental because of the mutagenicity and cytotoxicity. To combat the serious threats posed by DSBs, cells evolved various homologous and non-homologous recombination repair mechanisms. However, some repair mechanisms appear to be involved in the induction of genome rearrangements such as deletions. To analyze the deletion mutations in a whole body system, gpt delta mice were established. In this mouse model, deletions in lambda DNA integrated in the chromosome are preferentially selected as Spi- phages, which can then be subjected for molecular analysis. Here, we reported th...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369491</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369491</guid>        </item>
        <item>
            <title>Intermediate molecules generated by transposase in the pathways of transposition of bacterial insertion element IS3.</title>
            <link>http://www.medworm.com/index.php?rid=369488&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493331%26dopt%3DAbstract</link>
            <description>Authors: Ohtsubo E, Minematsu H, Tsuchida K, Ohtsubo H, Sekine Y
    
    PMID: 15493331 [PubMed - indexed for MEDLINE] (Source: Advances in Biophysics)</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369488</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369488</guid>        </item>
        <item>
            <title>Genetics and epigenetics in flower pigmentation associated with transposable elements in morning glories.</title>
            <link>http://www.medworm.com/index.php?rid=369484&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493332%26dopt%3DAbstract</link>
            <description>Authors: Iida S, Morita Y, Choi JD, Park KI, Hoshino A
    Among the genus Ipomoea, three morning glories, I. nil (the Japanese morning glory), I. purpurea (the common morning glory), and I. tricolor, were domesticated well for floricultural plants, and many spontaneous mutants displaying various flower pigmentation patterns were isolated. Most of these spontaneous mutations were found to be caused by the insertion of DNA transposable elements in the genes for the anthocyanin pigmentation in flowers, and many of them exhibited variegated flowers, such as white flowers with pigmented spots and sectors. Here, we describe the historical background of the mutants displaying variegated flowers and review the genetic and epigenetic regulation in flower pigmentation associated with transposable e...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369484</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369484</guid>        </item>
        <item>
            <title>Transposition mechanisms and biotechnology applications of the medaka fish Tol2 transposable element.</title>
            <link>http://www.medworm.com/index.php?rid=369481&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493333%26dopt%3DAbstract</link>
            <description>Authors: Koga A
    The Tol2 element of the medaka fish is a member of the hAT (hobo/Activator/ Tam3) transposable element family. About 20 copies are present in the medaka fish genome and, unlike many other hAT family elements, virtually all the copies are autonomous or potentially autonomous, containing an intact transposase gene. Excision of Tol2 is not precise at the nucleotide sequence level, excision foot-prints being heterogeneous. In more than half of excision events, however, breakage and rejoining of DNA molecules occur within the 8-bp target site duplication region, removing the entire Tol2 sequence and retaining parts of the target site duplications. In the reminder of the excision events, either the left or the right terminal region is left and the other end is lost together w...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369481</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369481</guid>        </item>
        <item>
            <title>Structure and function of the shufflon in plasmid R64.</title>
            <link>http://www.medworm.com/index.php?rid=369478&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493334%26dopt%3DAbstract</link>
            <description>Authors: Gyohda A, Furuya N, Ishiwa A, Zhu S, Komano T
    Conservative site-specific recombination plays key roles in creating biological diversity in prokaryotes. Most site-specific inversion systems consist of two recombination sites and a recombinase gene. In contrast, the shufflon multiple inversion system of plasmid R64 consists of seven sfx recombination sites, which separate four invertible DNA segments, and the rci gene encoding a site-specific recombinase of the integrase family. The rci product mediates recombination between any two inverted sfx sites, resulting in the inversion of four DNA segments independently or in groups. Random shufflon inversions construct seven pilV genes encoding constant N-terminal segment with different C-terminal segments. The pilV products are tip-l...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369478</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369478</guid>        </item>
        <item>
            <title>Molecular mechanism of VDE-initiated intein homing in yeast nuclear genome.</title>
            <link>http://www.medworm.com/index.php?rid=369476&amp;cid=s_34376_75_f&amp;fid=34376&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15493335%26dopt%3DAbstract</link>
            <description>Authors: Fukuda T, Nagai Y, Ohya Y
    In Saccharomyces cerevisiae, VMA1 intein encodes a homing endonuclease termed VDE which is produced by an autocatalytic protein splicing reaction. VDE introduces a DSB at its recognition sequence on intein-minus allele, resulting in the lateral transfer of VMA1 intein. In this review, we summarize a decade of in vitro study on VDE and describe our recent study on the in vivo behavior of both VDE and host proteins involved in intein mobility. Meiotic DSBs caused by VDE are repaired in the similar pathway to that working in meiotic recombination induced by Spo11p-mediated DSBs. Meiosis-specific DNA cleavage and homing is shown to be guaranteed by the two distinct mechanisms, the subcellular localization of VDE and a requirement of premeiotic DNA replica...</description>
            <author>Advances in Biophysics</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=369476</comments>
            <pubDate>Mon, 22 Jan 2007 16:11:02 +0100</pubDate>
            <guid isPermaLink="false">369476</guid>        </item>
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