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A. Paul Mould
Researcher at University of Manchester
Publications - 58
Citations - 4272
A. Paul Mould is an academic researcher from University of Manchester. The author has contributed to research in topics: Integrin & Ligand (biochemistry). The author has an hindex of 31, co-authored 58 publications receiving 4011 citations. Previous affiliations of A. Paul Mould include Wellcome Trust Centre for Cell-Matrix Research & Manchester Academic Health Science Centre.
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Journal ArticleDOI
Demonstration of catch bonds between an integrin and its ligand
TL;DR: Catch bond formation appears to involve force-assisted activation of the headpiece but not integrin extension, and binding of monoclonal antibodies that induce the active conformation of the integrin headpiece shifted catch bonds to a lower force range.
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Linking integrin conformation to function.
TL;DR: In this Commentary, some of the key remaining questions that surround integrin structure-function relationships are posed and the evidence that supports the current models is reviewed.
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The Cell-binding Domain of Intimin from Enteropathogenic Escherichia coli Binds to β1 Integrins
Gad Frankel,Ofer Lider,Rami Hershkoviz,A. Paul Mould,Sylvia G. Kachalsky,David C. A. Candy,Liora Cahalon,Martin J. Humphries,Gordon Dougan +8 more
TL;DR: Results demonstrate a specific integrin binding activity for intimin that is related to, but distinct from, that of invasin, and specifically blocked by an RGD-containing peptide and by antibodies directed against the integrin subunits β1, α4, and α5.
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Integrin αvβ1 Is a Receptor for Foot-and-Mouth Disease Virus
TL;DR: It is shown that the integrin αvβ1, when expressed as a human/hamster heterodimer on transfected CHOB2 cells, is a receptor for FMDV, and data are presented suggesting that amino acid residues near the RGD motif may be important for differentiating between the binding specificities of α vβ1 and αv β6.
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Defining the Topology of Integrin α5β1-Fibronectin Interactions Using Inhibitory Anti-α5 and Anti-β1 Monoclonal Antibodies: EVIDENCE THAT THE SYNERGY SEQUENCE OF FIBRONECTIN IS RECOGNIZED BY THE AMINO-TERMINAL REPEATS OF THE α5 SUBUNIT *
A. Paul Mould,Janet A. Askari,Shin Ichi Aota,Kenneth M. Yamada,Atsushi Irie,Yoshikazu Takada,Helen J. Mardon,Martin J. Humphries +7 more
TL;DR: The results indicate that the synergy region is recognized primarily by the α5 subunit but that the β1 subunit plays the major role in binding of the RGD sequence.