Abdallah Al-Hakim
Mount Sinai Hospital, Toronto
11 Papers
22 Citations
Abdallah Al-Hakim is an academic researcher from Mount Sinai Hospital, Toronto. The author has contributed to research in topics: Ubiquitin & Ubiquitin ligase. The author has an hindex of 10, co-authored 11 publications. Previous affiliations of Abdallah Al-Hakim include Mount Sinai Hospital & University of Dundee.
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Papers
The CRAPome: a contaminant repository for affinity purification–mass spectrometry data
Dattatreya Mellacheruvu,Zachary Wright,Amber L. Couzens,Jean-Philippe Lambert,Nicole St-Denis,Tuo Li,Yana Miteva,Simon Hauri,Mihaela E. Sardiu,Teck Yew Low,Vincentius A. Halim,Vincentius A. Halim,Richard D. Bagshaw,Nina C. Hubner,Abdallah Al-Hakim,Annie Bouchard,Denis Faubert,Damian Fermin,Wade H. Dunham,Marilyn Goudreault,Zhen Yuan Lin,Beatriz Gonzalez Badillo,Tony Pawson,Daniel Durocher,Benoit Coulombe,Ruedi Aebersold,Ruedi Aebersold,Giulio Superti-Furga,Jacques Colinge,Albert J. R. Heck,Hyungwon Choi,Matthias Gstaiger,Shabaz Mohammed,Ileana M. Cristea,Keiryn L. Bennett,Michael P. Washburn,Michael P. Washburn,Brian Raught,Rob M. Ewing,Rob M. Ewing,Anne-Claude Gingras,Alexey I. Nesvizhskii +41 more
TL;DR: The contaminant repository for affinity purification (the CRAPome) is presented and its use for scoring protein-protein interactions is described and aggregating negative controls from multiple AP-MS studies can increase coverage and improve the characterization of background associated with a given experimental protocol.
The RIDDLE Syndrome Protein Mediates a Ubiquitin-Dependent Signaling Cascade at Sites of DNA Damage
Grant S. Stewart,Stephanie Panier,Stephanie Panier,Kelly Townsend,Abdallah Al-Hakim,Nadine K. Kolas,Edward S. Miller,Shinichiro Nakada,Jarkko Ylanko,Jarkko Ylanko,Signe Olivarius,Megan Mendez,Ceri E. Oldreive,Jan Wildenhain,Andrea Tagliaferro,Laurence Pelletier,Laurence Pelletier,Nadine Taubenheim,Anne Durandy,Philip J. Byrd,Tatjana Stankovic,A. Malcolm R. Taylor,Daniel Durocher,Daniel Durocher +23 more
TL;DR: It is reported that the ubiquitin ligase RNF168 is mutated in the RIDDLE syndrome, a recently discovered immunodeficiency and radiosensitivity disorder and their loss is the likely cause of the cellular and developmental phenotypes associated with RIDdLE syndrome.
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The ubiquitous role of ubiquitin in the DNA damage response.
Abdallah Al-Hakim,Cristina Escribano-Diaz,Marie-Claude Landry,Lara O'Donnell,Stephanie Panier,Stephanie Panier,Rachel K. Szilard,Daniel Durocher,Daniel Durocher +8 more
TL;DR: How DNA repair and checkpoint pathways utilize the diversity offered by the ubiquitin conjugation system to modulate the response to genotoxic lesions in space and time is discussed.
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An Allosteric Inhibitor of the Human Cdc34 Ubiquitin-Conjugating Enzyme
Derek F. Ceccarelli,Xiaojing Tang,Benoit Pelletier,Stephen Orlicky,Weilin Xie,Veronique Plantevin,Dante Neculai,Dante Neculai,Yang-Chieh Chou,Yang-Chieh Chou,Abiodun A. Ogunjimi,Abdallah Al-Hakim,Xaralabos Varelas,Joanna Koszela,Gregory A. Wasney,Masoud Vedadi,Sirano Dhe-Paganon,Sarah Cox,Shuichan Xu,Antonia Lopez-Girona,Frank Mercurio,Jeff Wrana,Daniel Durocher,Sylvain Meloche,David R. Webb,Mike Tyers,Mike Tyers,Mike Tyers,Frank Sicheri,Frank Sicheri +29 more
TL;DR: E2 enzymes are susceptible to noncatalytic site inhibition and may represent a viable class of drug target in the UPS.
228
The MMS22L-TONSL complex mediates recovery from replication stress and homologous recombination
Lara O'Donnell,Stephanie Panier,Stephanie Panier,Jan Wildenhain,Johnny M. Tkach,Abdallah Al-Hakim,Marie-Claude Landry,Cristina Escribano-Diaz,Rachel K. Szilard,Jordan T.F. Young,Jordan T.F. Young,Meagan Munro,Marella D. Canny,Nadine K. Kolas,Wei Zhang,Wei Zhang,Shane M. Harding,Jarkko Ylanko,Megan Mendez,Michael Mullin,Thomas Sun,Bianca Habermann,Alessandro Datti,Alessandro Datti,Robert G. Bristow,Anne-Claude Gingras,Anne-Claude Gingras,Mike Tyers,Mike Tyers,Mike Tyers,Grant W. Brown,Daniel Durocher,Daniel Durocher +32 more
TL;DR: Results indicate that MMS22L and TONSL are genome caretakers that stimulate the recombination-dependent repair of stalled or collapsed replication forks.
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