M
Michael J. Barnes
Researcher at University of Cambridge
Publications - 52
Citations - 4749
Michael J. Barnes is an academic researcher from University of Cambridge. The author has contributed to research in topics: Integrin & Collagen receptor. The author has an hindex of 29, co-authored 51 publications receiving 4526 citations. Previous affiliations of Michael J. Barnes include Brigham and Women's Hospital.
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Journal ArticleDOI
Structural Basis of Collagen Recognition by Integrin α2β1
Jonas Emsley,C. Graham Knight,Richard W. Farndale,Michael J. Barnes,Robert C. Liddington,Robert C. Liddington +5 more
TL;DR: The crystal structure of a complex between the I domain of integrin alpha2beta1 and a triple helical collagen peptide containing a critical GFOGER motif is determined, suggesting both a basis for affinity regulation and a pathway for signal transduction.
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The Collagen-binding A-domains of Integrins α1β1 and α2β1Recognize the Same Specific Amino Acid Sequence, GFOGER, in Native (Triple-helical) Collagens
C. Graham Knight,Laurence F. Morton,Anthony R. Peachey,Danny S. Tuckwell,Richard W. Farndale,Michael J. Barnes +5 more
TL;DR: It is shown that the sequence GFOGER represents a high-affinity binding site in collagens I and IV for α2β1 and in collagen I for α1β1, and that the same sequence binds integrin α1 A-domain and supports integrin β-mediated cell adhesion.
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The role of collagen in thrombosis and hemostasis.
TL;DR: The role of collagen in the regulation of hemostasis, embracing both coagulation and platelet aggregation is reviewed, with ample evidence that collagen is one of the major activators of the platelet response after injury.
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Integrin alpha 2 beta 1-independent activation of platelets by simple collagen-like peptides: collagen tertiary (triple-helical) and quaternary (polymeric) structures are sufficient alone for alpha 2 beta 1-independent platelet reactivity.
TL;DR: Collagen can activate platelets by a mechanism that is independent of integrin alpha 2 beta 1 and for which collagen tertiary and quaternary structures are sufficient alone for activity without the involvement of highly specific cell-recognition sequences.
Journal ArticleDOI
Identification in Collagen Type I of an Integrin α2β1-binding Site Containing an Essential GER Sequence
C. Graham Knight,Laurence F. Morton,David J. Onley,Anthony R. Peachey,Anthea J. Messent,Peter A. Smethurst,Danny S. Tuckwell,Richard W. Farndale,Michael J. Barnes +8 more
TL;DR: The collagen type I-derived fragment α1(I)CB3 is known to recognize the platelet collagen receptor integrin α2β1 as effectively as the parent collagen, although it lacks platelet-aggregatory activity, so seven overlapping peptides that spontaneously assemble into triple helices are synthesized.