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Institution

Université de Montréal

EducationMontreal, Quebec, Canada
About: Université de Montréal is a education organization based out in Montreal, Quebec, Canada. It is known for research contribution in the topics: Population & Context (language use). The organization has 45641 authors who have published 100476 publications receiving 4004007 citations. The organization is also known as: University of Montreal & UdeM.


Papers
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Journal ArticleDOI
TL;DR: PP2A activation results in growth suppression, enhanced apoptosis, restored differentiation, impaired clonogenic potential, and decreased in vivo leukemogenesis of imatinib-sensitive and -resistant BCR/ABL+.

479 citations

Journal ArticleDOI
TL;DR: Study on the substrate specificity with ribonuclease as the substrate revealed that the staphylococcal protease specifically cleaves peptide bonds on the COOH-terminal side of either aspartic acid or glutamic acid.

478 citations

Journal ArticleDOI
TL;DR: In this article, the authors presented the first systematic attempt to use a meta-analysis and controlled, longitudinal studies to examine the relations of specific types of motivation to overall academic achievement.

478 citations

Journal ArticleDOI
TL;DR: In this paper, sequence analysis revealed phospholipase A2 motifs in the capsid proteins of parvoviruses and showed that PLA2 activity is critical for efficient transfer of the viral genome from late endosomes/lysosomes to the nucleus to initiate replication.

478 citations

Journal ArticleDOI
TL;DR: The recent discovery that the catalytic activity of RAF depends on an allosteric mechanism driven by kinase domain dimerization is providing a vital new piece of information towards a comprehensive model of RAF function.
Abstract: RAF family kinases were among the first oncoproteins to be described more than 30 years ago. They primarily act as signalling relays downstream of RAS, and their close ties to cancer have fuelled a large number of studies. However, we still lack a systems-level understanding of their regulation and mode of action. The recent discovery that the catalytic activity of RAF depends on an allosteric mechanism driven by kinase domain dimerization is providing a vital new piece of information towards a comprehensive model of RAF function. The fact that current RAF inhibitors unexpectedly induce ERK signalling by stimulating RAF dimerization also calls for a deeper structural characterization of this family of kinases.

477 citations


Authors

Showing all 45957 results

NameH-indexPapersCitations
Yoshua Bengio2021033420313
Alan C. Evans183866134642
Richard H. Friend1691182140032
Anders Björklund16576984268
Charles N. Serhan15872884810
Fernando Rivadeneira14662886582
C. Dallapiccola1361717101947
Michael J. Meaney13660481128
Claude Leroy135117088604
Georges Azuelos134129490690
Phillip Gutierrez133139196205
Danny Miller13351271238
Henry T. Lynch13392586270
Stanley Nattel13277865700
Lucie Gauthier13267964794
Network Information
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023118
2022485
20216,077
20205,753
20195,212
20184,696