C
C. Jane McGlade
Researcher at University of Toronto
Publications - 63
Citations - 6951
C. Jane McGlade is an academic researcher from University of Toronto. The author has contributed to research in topics: Signal transducing adaptor protein & NUMB. The author has an hindex of 37, co-authored 62 publications receiving 6517 citations. Previous affiliations of C. Jane McGlade include Sunnybrook Research Institute.
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Journal ArticleDOI
T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
Stephen C. Bunnell,David I. Hong,Julia R. Kardon,Tetsuo Yamazaki,C. Jane McGlade,Valarie A. Barr,Lawrence E. Samelson +6 more
TL;DR: It is indicated that these complexes can form within seconds of TCR engagement, in the absence of either lipid raft aggregation or the formation of a central TCR-rich cluster.
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Attenuation of Leptin Action and Regulation of Obesity by Protein Tyrosine Phosphatase 1B
Alan Cheng,Noriko Uetani,Paul Daniel Simoncic,Paul Daniel Simoncic,Vikas P. Chaubey,Ailsa Lee-Loy,C. Jane McGlade,Brian P. Kennedy,Michel L. Tremblay +8 more
TL;DR: It is suggested that PTP1B negatively regulates leptin signaling, and provide one mechanism by which it may regulate obesity.
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Mammalian Numb Proteins Promote Notch1 Receptor Ubiquitination and Degradation of the Notch1 Intracellular Domain
TL;DR: The results suggest that Numb recruits components of the ubiquitination machinery to the Notch receptor thereby facilitating Notch1 ubiquitinations at the membrane, which in turn promotes degradation of the intracellular domain circumventing its nuclear translocation and downstream activation of Notch 1 target genes.
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Crumbs, the Drosophila homologue of human CRB1/RP12, is essential for photoreceptor morphogenesis
Milena Pellikka,Milena Pellikka,Guy Tanentzapf,Guy Tanentzapf,Madalena Pinto,Christian A. Smith,C. Jane McGlade,Donald F. Ready,Ulrich Tepass +8 more
TL;DR: It is proposed that Crumbs is a central component of a molecular scaffold that controls zonula adherens assembly and defines the stalk as an apical membrane subdomain, which may contribute to human CRB1-related retinal dystrophies.
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Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling
David A. Calderwood,Yosuke Fujioka,José M. de Pereda,Begoña García-Álvarez,Tetsuya Nakamoto,Ben Margolis,C. Jane McGlade,Robert C. Liddington,Mark H. Ginsberg,Mark H. Ginsberg +9 more
TL;DR: These data establish that short integrin β tails interact with a large number of PTB domain-containing proteins through a structurally conserved mechanism.