G
Geraldine Mbamalu
Researcher at Lunenfeld-Tanenbaum Research Institute
Publications - 19
Citations - 5363
Geraldine Mbamalu is an academic researcher from Lunenfeld-Tanenbaum Research Institute. The author has contributed to research in topics: SH2 domain & Receptor tyrosine kinase. The author has an hindex of 16, co-authored 18 publications receiving 5165 citations. Previous affiliations of Geraldine Mbamalu include University of Toronto & Mount Sinai Hospital, Toronto.
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Journal ArticleDOI
Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases.
M. Rozakis-Adcock,J McGlade,Geraldine Mbamalu,Giuliana Pelicci,Roger J. Daly,W. Li,A. Batzer,Sheila M. Thomas,Joan S. Brugge,Pier Giuseppe Pelicci,Joseph Schlessinger,Tony Pawson,Tony Pawson +12 more
TL;DR: The results suggest that She tyrosine phosphorylation can couple tyosine kinases to Grb2/Sem-5, through formation of a Shc-Grb2-Sem- 5 complex, and thereby regulate the mammalian Ras signalling pathway.
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A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity.
Dan Lin,Amelia S. Edwards,James P. Fawcett,Geraldine Mbamalu,John D. Scott,Tony Pawson,Tony Pawson +6 more
TL;DR: It is shown that homologues of proteins necessary for asymmetric cell division in Caenorhabditis elegans associate with each other in mammalian cells and tissues and have a scaffolding function, coordinating the activities of several signalling proteins that are implicated in mammalian cell polarity.
Journal ArticleDOI
Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
Sacha J. Holland,Nicholas W. Gale,Geraldine Mbamalu,George D. Yancopoulos,Mark Henkemeyer,Mark Henkemeyer,Tony Pawson,Tony Pawson +7 more
TL;DR: It is shown that challenging cells that express the TM ligands Elk-L or Htk-L with the clustered ectodomain of Nuk induces phosphorylation of the ligands on tyrosine, a process that can be mimicked both in vitro and in vivo by an activated Src tyrosINE kinase.
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A Drosophila SH2-SH3 Adaptor Protein Implicated in Coupling the Sevenless Tyrosine Kinase to an Activator of Ras Guanine Nucleotide Exchange, Sos
Jean Paul Olivier,Thomas Raabe,Mark Henkemeyer,Barry J. Dickson,Geraldine Mbamalu,Ben Margolis,Joseph Schlessinger,Ernst Hafen,Tony Pawson +8 more
TL;DR: Results suggest that drk binds autophosphorylated receptor tyrosine kinases with its SH2 domain and the Sos GNRP through its SH3 domains, thereby coupling receptor tyrose kinases to Ras activation.
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Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway.
Lorri Puil,Jiaxin Liu,Gerald D. Gish,Geraldine Mbamalu,David D.L. Bowtell,Pier Giuseppe Pelicci,Ralph Arlinghaus,Tony Pawson +7 more
TL;DR: Results suggest that autophosphorylation within the Bcr element of Bcr‐Abl creates a direct physical link to Grb2‐mSos1, and potentially to the Ras pathway, and thereby modifies the target specificity of the Abl tyrosine kinase.