Validation of GCN5L1/BLOC1S1/BLOS1 Antibodies Using Knockout Cells and Tissue
In this report we tested several commercially-available antibodies for GCN5L1, and found that two-thirds of those available did not unambiguously detect the protein by western blot in cultured mouse cells or ex vivo liver tissue. These data suggest that previously published studies which used these unverified antibodies to measure GCN5L1 protein abundance, in the absence of other independent methods of corroboration, should be interpreted with appropriate caution.PMID:38683688 | DOI:10.1042/BCJ20230302 (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 29, 2024 Category: Biochemistry Authors: Paramesha Bugga Michael W Stoner Janet R Manning Bellina Mushala Nisha Bhattarai Maryam Sharifi-Sanjani Bradley R Webster Dharendra Thapa Iain Scott Source Type: research

Validation of GCN5L1/BLOC1S1/BLOS1 Antibodies Using Knockout Cells and Tissue
In this report we tested several commercially-available antibodies for GCN5L1, and found that two-thirds of those available did not unambiguously detect the protein by western blot in cultured mouse cells or ex vivo liver tissue. These data suggest that previously published studies which used these unverified antibodies to measure GCN5L1 protein abundance, in the absence of other independent methods of corroboration, should be interpreted with appropriate caution.PMID:38683688 | DOI:10.1042/BCJ20230302 (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 29, 2024 Category: Biochemistry Authors: Paramesha Bugga Michael W Stoner Janet R Manning Bellina Mushala Nisha Bhattarai Maryam Sharifi-Sanjani Bradley R Webster Dharendra Thapa Iain Scott Source Type: research

Validation of GCN5L1/BLOC1S1/BLOS1 Antibodies Using Knockout Cells and Tissue
In this report we tested several commercially-available antibodies for GCN5L1, and found that two-thirds of those available did not unambiguously detect the protein by western blot in cultured mouse cells or ex vivo liver tissue. These data suggest that previously published studies which used these unverified antibodies to measure GCN5L1 protein abundance, in the absence of other independent methods of corroboration, should be interpreted with appropriate caution.PMID:38683688 | DOI:10.1042/BCJ20230302 (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 29, 2024 Category: Biochemistry Authors: Paramesha Bugga Michael W Stoner Janet R Manning Bellina Mushala Nisha Bhattarai Maryam Sharifi-Sanjani Bradley R Webster Dharendra Thapa Iain Scott Source Type: research

Validation of GCN5L1/BLOC1S1/BLOS1 Antibodies Using Knockout Cells and Tissue
In this report we tested several commercially-available antibodies for GCN5L1, and found that two-thirds of those available did not unambiguously detect the protein by western blot in cultured mouse cells or ex vivo liver tissue. These data suggest that previously published studies which used these unverified antibodies to measure GCN5L1 protein abundance, in the absence of other independent methods of corroboration, should be interpreted with appropriate caution.PMID:38683688 | DOI:10.1042/BCJ20230302 (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 29, 2024 Category: Biochemistry Authors: Paramesha Bugga Michael W Stoner Janet R Manning Bellina Mushala Nisha Bhattarai Maryam Sharifi-Sanjani Bradley R Webster Dharendra Thapa Iain Scott Source Type: research

RNF138 inhibits transcription factor C/EBP α protein turnover leading to differentiation arrest in AML
Biochem J. 2024 Apr 26:BCJ20240027. doi: 10.1042/BCJ20240027. Online ahead of print.ABSTRACTE3 ubiquitin ligase, ring finger protein 138 (RNF138) is involved in several biological processes; however, its role in myeloid differentiation or tumorigenesis remains unclear. RNAseq data from TNMplot showed that RNF138 mRNA levels are highly elevated in Acute Myeloid Leukemia (AML) bone marrow samples as compared to bone marrow of normal volunteers. Here, we show that RNF138 serves as an E3 ligase for the tumor suppressor CCAAT/enhancer binding protein (C/EBPα) and promotes its degradation leading to myeloid differentiation arre...
Source: The Biochemical Journal - April 26, 2024 Category: Biochemistry Authors: Anil Kumar Singh Vishal Upadhyay Arppita Sethi Sangita Chaowdhury Shivkant Mishra Shailednra Prasad Verma Madan Lal Brahma Bhatt Arun Kumar Trivedi Source Type: research

RNF138 inhibits transcription factor C/EBP α protein turnover leading to differentiation arrest in AML
Biochem J. 2024 Apr 26:BCJ20240027. doi: 10.1042/BCJ20240027. Online ahead of print.ABSTRACTE3 ubiquitin ligase, ring finger protein 138 (RNF138) is involved in several biological processes; however, its role in myeloid differentiation or tumorigenesis remains unclear. RNAseq data from TNMplot showed that RNF138 mRNA levels are highly elevated in Acute Myeloid Leukemia (AML) bone marrow samples as compared to bone marrow of normal volunteers. Here, we show that RNF138 serves as an E3 ligase for the tumor suppressor CCAAT/enhancer binding protein (C/EBPα) and promotes its degradation leading to myeloid differentiation arre...
Source: The Biochemical Journal - April 26, 2024 Category: Biochemistry Authors: Anil Kumar Singh Vishal Upadhyay Arppita Sethi Sangita Chaowdhury Shivkant Mishra Shailednra Prasad Verma Madan Lal Brahma Bhatt Arun Kumar Trivedi Source Type: research

RNF138 inhibits transcription factor C/EBP α protein turnover leading to differentiation arrest in AML
Biochem J. 2024 Apr 26:BCJ20240027. doi: 10.1042/BCJ20240027. Online ahead of print.ABSTRACTE3 ubiquitin ligase, ring finger protein 138 (RNF138) is involved in several biological processes; however, its role in myeloid differentiation or tumorigenesis remains unclear. RNAseq data from TNMplot showed that RNF138 mRNA levels are highly elevated in Acute Myeloid Leukemia (AML) bone marrow samples as compared to bone marrow of normal volunteers. Here, we show that RNF138 serves as an E3 ligase for the tumor suppressor CCAAT/enhancer binding protein (C/EBPα) and promotes its degradation leading to myeloid differentiation arre...
Source: The Biochemical Journal - April 26, 2024 Category: Biochemistry Authors: Anil Kumar Singh Vishal Upadhyay Arppita Sethi Sangita Chaowdhury Shivkant Mishra Shailednra Prasad Verma Madan Lal Brahma Bhatt Arun Kumar Trivedi Source Type: research

Correction: Proteasome and thiol involvement in quality control of glycosylphosphatidylinositol anchor addition
Biochem J. 2024 Apr 10;481(7):565-566. doi: 10.1042/BJ3320111_COR.NO ABSTRACTPMID:38597906 | DOI:10.1042/BJ3320111_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Barry Wilbourn Darren N Nesbeth Linda J Wainwright Mark C Field Source Type: research

Expression of Concern: Protease-activated receptor-2 promotes kidney tubular epithelial inflammation by inhibiting autophagy via the PI3K/Akt/mTOR signalling pathway
Biochem J. 2024 Apr 10;481(7):567. doi: 10.1042/BCJ20170272_EOC.NO ABSTRACTPMID:38597907 | DOI:10.1042/BCJ20170272_EOC (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Chunyang Du Tao Zhang Xia Xiao Yonghong Shi Huijun Duan Yunzhuo Ren Source Type: research

Correction: Proteasome and thiol involvement in quality control of glycosylphosphatidylinositol anchor addition
Biochem J. 2024 Apr 10;481(7):565-566. doi: 10.1042/BJ3320111_COR.NO ABSTRACTPMID:38597906 | DOI:10.1042/BJ3320111_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Barry Wilbourn Darren N Nesbeth Linda J Wainwright Mark C Field Source Type: research

Expression of Concern: Protease-activated receptor-2 promotes kidney tubular epithelial inflammation by inhibiting autophagy via the PI3K/Akt/mTOR signalling pathway
Biochem J. 2024 Apr 10;481(7):567. doi: 10.1042/BCJ20170272_EOC.NO ABSTRACTPMID:38597907 | DOI:10.1042/BCJ20170272_EOC (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Chunyang Du Tao Zhang Xia Xiao Yonghong Shi Huijun Duan Yunzhuo Ren Source Type: research

Correction: Proteasome and thiol involvement in quality control of glycosylphosphatidylinositol anchor addition
Biochem J. 2024 Apr 10;481(7):565-566. doi: 10.1042/BJ3320111_COR.NO ABSTRACTPMID:38597906 | DOI:10.1042/BJ3320111_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Barry Wilbourn Darren N Nesbeth Linda J Wainwright Mark C Field Source Type: research

Expression of Concern: Protease-activated receptor-2 promotes kidney tubular epithelial inflammation by inhibiting autophagy via the PI3K/Akt/mTOR signalling pathway
Biochem J. 2024 Apr 10;481(7):567. doi: 10.1042/BCJ20170272_EOC.NO ABSTRACTPMID:38597907 | DOI:10.1042/BCJ20170272_EOC (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Chunyang Du Tao Zhang Xia Xiao Yonghong Shi Huijun Duan Yunzhuo Ren Source Type: research

Correction: Proteasome and thiol involvement in quality control of glycosylphosphatidylinositol anchor addition
Biochem J. 2024 Apr 10;481(7):565-566. doi: 10.1042/BJ3320111_COR.NO ABSTRACTPMID:38597906 | DOI:10.1042/BJ3320111_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Barry Wilbourn Darren N Nesbeth Linda J Wainwright Mark C Field Source Type: research

Expression of Concern: Protease-activated receptor-2 promotes kidney tubular epithelial inflammation by inhibiting autophagy via the PI3K/Akt/mTOR signalling pathway
Biochem J. 2024 Apr 10;481(7):567. doi: 10.1042/BCJ20170272_EOC.NO ABSTRACTPMID:38597907 | DOI:10.1042/BCJ20170272_EOC (Source: The Biochemical Journal)
Source: The Biochemical Journal - April 10, 2024 Category: Biochemistry Authors: Chunyang Du Tao Zhang Xia Xiao Yonghong Shi Huijun Duan Yunzhuo Ren Source Type: research