R
Rebecca Wilson
Researcher at Institute of Cancer Research
Publications - 13
Citations - 11771
Rebecca Wilson is an academic researcher from Institute of Cancer Research. The author has contributed to research in topics: Caspase & Apoptosis. The author has an hindex of 11, co-authored 13 publications receiving 10978 citations. Previous affiliations of Rebecca Wilson include Breast Cancer Now & The Breast Cancer Research Foundation.
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Journal ArticleDOI
Mutations of the BRAF gene in human cancer
Helen Davies,Graham R. Bignell,Charles Cox,Philip J. Stephens,Sarah Edkins,S. M. Clegg,Jon W. Teague,Hayley Woffendin,Mathew J. Garnett,William Bottomley,Neil Davis,Ed Dicks,Rebecca Ewing,Yvonne Floyd,Kristian Gray,S. Hall,Rachel Hawes,Jaime Hughes,Vivian Kosmidou,Andrew Menzies,Catherine Mould,Adrian Parker,Claire Stevens,Stephen Watt,Steven Hooper,Rebecca Wilson,Hiran Jayatilake,Barry A. Gusterson,Colin Cooper,Janet Shipley,Darren Hargrave,Kathy Pritchard-Jones,Norman J. Maitland,Georgia Chenevix-Trench,Gregory J. Riggins,Darell D. Bigner,Giuseppe Palmieri,Antonio Cossu,Adrienne M. Flanagan,Andrew G. Nicholson,Judy W. C. Ho,Suet Yi Leung,Siu Tsan Yuen,Barbara L. Weber,Hilliard F. Seigler,Timothy L. Darrow,Hugh Paterson,Richard Marais,Christopher J. Marshall,Richard Wooster,Michael R. Stratton,P. Andrew Futreal +51 more
TL;DR: BRAF somatic missense mutations in 66% of malignant melanomas and at lower frequency in a wide range of human cancers, with a single substitution (V599E) accounting for 80%.
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Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
TL;DR: In the p38 SAP kinase pathway, MAPKAP kinase-2 serves both as an effector of p38 by phosphorylating substrates and as a determinant of cellular localisation of p 38.
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The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
Rebecca Wilson,Lakshmi Goyal,Mark Ditzel,Anna Zachariou,David A Baker,Julie Agapite,Hermann Steller,Pascal Meier +7 more
TL;DR: In vivo, the RING finger of DIAP1 is essential for the regulation of apoptosis induced by Rpr, Hid and Dronc, and the data suggest that IAPs suppress apoptosis by binding to and targeting caspases for ubiquitination.
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Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis.
TL;DR: It is shown that Drosophila IAP 1 (DIAP1) is degraded by the 'N-end rule' pathway and that this process is indispensable for regulating apoptosis, and suggested that DIAP1 instability, mediated through caspase activity and subsequent exposure of the N- end rule pathway, is essential for suppression of apoptosis.
Journal ArticleDOI
MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death
Isabel Jaco,Alessandro Annibaldi,Najoua Lalaoui,Najoua Lalaoui,Rebecca Wilson,Tencho Tenev,Lucie Laurien,Chun Kim,Kunzah Jamal,Sidonie Wicky John,Gianmaria Liccardi,Diep Chau,Diep Chau,James M. Murphy,James M. Murphy,Gabriela Brumatti,Gabriela Brumatti,Rebecca Feltham,Rebecca Feltham,Rebecca Feltham,Manolis Pasparakis,John Silke,John Silke,Pascal Meier +23 more
TL;DR: MK2-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF signaling pathway that integrates cell survival and cytokine production, and contributes to complex-II-mediated cell death, independent of its recruitment tocomplex-I.