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Salima Daou

Researcher at Lunenfeld-Tanenbaum Research Institute

Publications -  16
Citations -  1182

Salima Daou is an academic researcher from Lunenfeld-Tanenbaum Research Institute. The author has contributed to research in topics: Ubiquitin & Deubiquitinating enzyme. The author has an hindex of 11, co-authored 15 publications receiving 931 citations. Previous affiliations of Salima Daou include Université de Montréal.

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Journal ArticleDOI

Tumor suppressor and deubiquitinase BAP1 promotes DNA double-strand break repair.

TL;DR: It is shown that BAP1 is recruited to double-strand DNA break sites and promotes error-free repair of these lesions, providing the first evidence that phosphorylation coordinates the function of B AP1 in promoting cellular recovery from DNA damage.
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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

TL;DR: The findings establish a direct link between BAP1 and the transcriptional control of genes regulating cell growth and proliferation and shed light on a novel mechanism of transcription regulation involving ubiquitin signaling.
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Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O.

TL;DR: UBE2O defines an atypical ubiquitin-signaling pathway that coordinates the function of BAP1 and establishes a paradigm for regulation of nuclear trafficking of chromatin-associated proteins.
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The BAP1/ASXL2 Histone H2A Deubiquitinase Complex Regulates Cell Proliferation and is Disrupted in Cancer

TL;DR: BAP1 forms two mutually exclusive complexes with the transcriptional regulators ASXL1 and ASXL2, which are necessary for maintaining proper protein levels of this DUB, and it is demonstrated that BAP1 interaction with AsXL2 regulates cell senescence and that AS XL2 cancer-associated mutations disrupt B AP1 DUB activity.
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Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway

TL;DR: It is reported that HCF-1 proteolysis is a regulated process and O-GlcNAcylation of H CF-1 is a signal for its proteolytic processing and a unique crosstalk between these posttranslational modifications is revealed.