J
Jenson Lim
Researcher at University of Stirling
Publications - 28
Citations - 797
Jenson Lim is an academic researcher from University of Stirling. The author has contributed to research in topics: Integrin & Galleria mellonella. The author has an hindex of 14, co-authored 24 publications receiving 710 citations. Previous affiliations of Jenson Lim include Imperial College London & Keele University.
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Journal ArticleDOI
The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis
Yotis A. Senis,Michael G. Tomlinson,Stuart Ellison,Alexandra Mazharian,Jenson Lim,Yan Zhao,Kristin N. Kornerup,Jocelyn M. Auger,Steve G. Thomas,Tarvinder S. Dhanjal,Neena Kalia,Jing W. Zhu,Arthur Weiss,Steve P. Watson +13 more
TL;DR: CD148 is highlighted as a global regulator of platelet activation and a novel antithrombotic drug target after basal SFK activity was found to be markedly reduced in CD148-deficient platelets, resulting in a global hyporesponsiveness to agonists that signal through SFKs, including collagen and fibrinogen.
Journal ArticleDOI
An Essential Role for Talin during αMβ2-mediated Phagocytosis
Jenson Lim,Agnès Wiedemann,George Tzircotis,Susan J. Monkley,David R. Critchley,Emmanuelle Caron +5 more
TL;DR: The results establish for the first time at least two distinct roles for talin during CR3/alpha(M)beta(2)-mediated phagocytosis, most noticeably activation of the CR3/(M) beta(2) receptor andphagocytic uptake.
Journal ArticleDOI
Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS
David Albesa-Jové,Thomas Bertrand,Elisabeth P. Carpenter,Gemma V. Swain,Jenson Lim,Jiancheng Zhang,Lesley F. Haire,N. Vasisht,Veit Braun,Anton Lange,Christoph v. Prof. Eichel-Streiber,Dmitri I. Svergun,Neil F. Fairweather,Katherine A. Brown +13 more
TL;DR: Knowledge of the shapes and relative orientations of toxin domains provides new insight into defining functional domain boundaries and provides a framework for understanding how potential intra-domain interactions enable conformational changes to propagate between domains to facilitate intoxication processes.
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Two distinct cytoplasmic regions of the beta2 integrin chain regulate RhoA function during phagocytosis.
TL;DR: It is reported that the binding of C3bi-opsonized sheep red blood cells (RBCs) to αMβ2 increases Rho-GTP, but not Rac- GTP, levels, and shed light on the mechanism of outside-in signaling, from ligated integrins to the activation of Rho GTPase signaling.
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Phagocytosis, an alternative model system for the study of cell adhesion.
TL;DR: Some of the similarities between the formation and maintenance of adhesive contacts and phagocytic uptake are highlighted and why the study ofphagocytosis can help understand more complex adhesion processes are discussed.