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Maisonneuve-Rosemont Hospital Research Center and Department of Medicine
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The ubiquitin carboxyl hydrolase BAP1 forms a ternary complex with YY1 and HCF-1 and is a critical regulator of gene expression.
Molecular and cellular biology Nov, 2010 | Pubmed ID: 20805357
Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
Proceedings of the National Academy of Sciences of the United States of America Feb, 2011 | Pubmed ID: 21285374
Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
Proteomics Mar, 2013 | Pubmed ID: 23335398
Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O.
Molecular cell May, 2014 | Pubmed ID: 24703950
The IKAROS interaction with a complex including chromatin remodeling and transcription elongation activities is required for hematopoiesis.
PLoS genetics Dec, 2014 | Pubmed ID: 25474253
The BAP1/ASXL2 Histone H2A Deubiquitinase Complex Regulates Cell Proliferation and Is Disrupted in Cancer.
The Journal of biological chemistry Nov, 2015 | Pubmed ID: 26416890
Monoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1.
Nature communications 10, 2018 | Pubmed ID: 30349006
University of Montréal
Sinai Health System
Louis Masclef*,1,
Uriarte Maxime*,1,
Oumaima Ahmed1,
Nadine Sen Nkwe1,
Haithem Barbour1,
Nicholas V.G. Iannantuono1,
Amina Boubekeur1,
Salima Daou1,2,
El Bachir Affar1,2
1Maisonneuve-Rosemont Hospital Research Center and Department of Medicine, University of Montréal,
2Lunenfeld-Tanenbaum Research Institute, Sinai Health System
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