Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Laurence F. Morton"'
Autor:
Anthony R. Peachey, C. Graham Knight, Michael J. Barnes, Danny S. Tuckwell, Richard W. Farndale, Laurence F. Morton
Publikováno v:
Journal of Biological Chemistry. 275:35-40
We have previously assigned an integrin alpha(2)beta(1)-recognition site in collagen I to the sequence, GFOGERGVEGPOGPA (O = Hyp), corresponding to residues 502-516 of the alpha(1)(I) chain and located in the fragment alpha(1)(I)CB3 (Knight, C. G., M
Autor:
C.G. Knight, Verkleij Mw, M. J. W. Ijsseldijk, G.J. Heijnen-Snyder, Laurence F. Morton, J. J. Sixma, de Groot Pg, Huizinga Eg, Mike Barnes
Publikováno v:
Thrombosis and Haemostasis. 82:1137-1144
Seven overlapping peptides derived from the bovine alpha1(III)CB4 fragment of collagen III support static platelet adhesion, and an integrin alpha2beta1-recognition site has been assigned within this fragment to residues 522-528 of the collagen alpha
Autor:
C. Graham Knight, Laurence F. Morton, Anthony R. Peachey, David J. Onley, Peter A. Smethurst, Richard W. Farndale, Michael J. Barnes, Danny S. Tuckwell, Anthea J. Messent
Publikováno v:
Journal of Biological Chemistry. 273:33287-33294
The collagen type I-derived fragment alpha1(I)CB3 is known to recognize the platelet collagen receptor integrin alpha2beta1 as effectively as the parent collagen, although it lacks platelet-aggregatory activity. We have synthesized the fragment as se
Autor:
Michael J. Barnes, Marilyn W. Verkleij, Philip G. de Groot, Laurence F. Morton, Jan J. Sixma, C. Graham Knight
Publikováno v:
Blood. 91:3808-3816
The aim of this study was to define the need for specific collagen sequences and the role of their conformation in platelet adhesion to collagen under both static and flow conditions. We recently reported that simple triple-helical collagen-related p
Publikováno v:
Journal of Biological Chemistry. 272:11044-11048
The platelet-reactive collagen III-derived fragment alpha1(III)CB4 has been synthesized as seven overlapping peptides, each as a homotrimeric triple-helical species covalently linked at the C terminus. Additional Gly-Pro-Hyp triplets were introduced
Autor:
Marcus Achison, Laurence F. Morton, Mike Barnes, Young Han Lee, Richard W. Farndale, Steve P. Watson, J. Asselin, Jonathan M. Gibbins
Publikováno v:
Blood. 89:1235-1242
Activation of platelets by collagen is mediated through a tyrosine kinase-dependent pathway that is associated with phosphorylation of the Fc receptor gamma chain, the tyrosine kinase syk, and phospholipase C gamma2 (PLC gamma2). We recently describe
Publikováno v:
Biochemical Journal. 306:337-344
The platelet reactivities of two simple collagen-like synthetic peptides, Gly-Lys-Hyp-(Gly-Pro-Hyp)10-Gly-Lys-Hyp-Gly and Gly-Cys-Hyp-(Gly-Pro-Hyp)10-Gly-Cys-Hyp-Gly, were investigated. Both peptides adopted a stable triple-helical conformation in so
Autor:
David J. Onley, C.G. Knight, Tatsuo Ichinohe, Laurence F. Morton, Michael J. Barnes, Richard W. Farndale, Minoru Okuma, Anthony R. Peachey
Publikováno v:
Cardiovascular research. 41(2)
Peptides consisting of a repeat Gly-Pro-Hyp sequence are potent platelet agonists. The aim of this study was: (1) to examine the specificity of this sequence for platelet activation; (2) to confirm its recognition by platelet glycoprotein VI; and (3)
Autor:
Lesley Rawlinson, Richard W. Farndale, Mike Barnes, Laurence F. Morton, John C. Lee, R J Waller, Simon Sarsfield, J Saklatvala
Publikováno v:
The Journal of biological chemistry. 271(12)
p38 mitogen-activated protein kinase (MAPK) was identified in platelets on the basis of (a) its reactivity with antibodies to C-terminal and N-terminal peptides, and (b) its ability to activate MAPK-activated protein kinase-2, which phosphorylates th
Autor:
Michael J. Barnes, Martin J. Humphries, Lynn S. Zijenah, Laurence F. Morton, A H Goodall, Anthony R. Peachey
Publikováno v:
Europe PubMed Central
Platelet adhesion has been measured to type-I monomeric collagen, collagen fibres, alpha 1(I) and alpha 2(I) chains and the chain fragments alpha 1(I)CB3, alpha 1(I)CB6, alpha 1(I)CB7 and alpha 1(I)CB8, and alpha 2(I)CB3,5 and alpha 2(I)CB4. Little i