D
Danny S. Tuckwell
Researcher at University of Manchester
Publications - 36
Citations - 3025
Danny S. Tuckwell is an academic researcher from University of Manchester. The author has contributed to research in topics: Integrin & Binding site. The author has an hindex of 27, co-authored 36 publications receiving 2902 citations. Previous affiliations of Danny S. Tuckwell include Wellcome Trust Centre for Cell-Matrix Research & University of Cambridge.
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Journal ArticleDOI
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.
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.
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Integrin alpha 2 I-domain is a binding site for collagens
TL;DR: In this article, a recombinant human alpha 2 I-domain (r alpha 2I) was generated by reverse transcriptase-polymerase chain reaction/bacterial expression and tested its ability to mediate the collagen-binding functions of alpha 2 beta 1.
Journal ArticleDOI
Fibrillar collagen: the key to vertebrate evolution? A tale of molecular incest.
TL;DR: Evidence is presented that the classical vertebrate fibrillar collagens share a single common ancestor that arose at the very dawn of the vertebrate world and prior to the associated genome duplication events.
Journal ArticleDOI
A novel and highly conserved collagen (proα1(XXVII)) with a unique expression pattern and unusual molecular characteristics establishes a new clade within the vertebrate fibrillar collagen family
Raymond P. Boot-Handford,Danny S. Tuckwell,Darren A. Plumb,Claire Farrington Rock,Richard Poulsom +4 more
TL;DR: Phylogenetic analyses revealed that type XXVII, together with the closely related type XXIV collagen gene, form a new, third clade (type C) within the vertebrate fibrillar collagen family.