Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glicoprotein IIb/IIIa. Influence of peptide length-Reference-Cited by-同舟云学术

Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glicoprotein IIb/IIIa. Influence of peptide length

Published:1992-06 Issue:3 Volume:206 Page:759-765
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

CALVETE Juan J.,SCHAFER Wolfram,MANN Karlheinz,HENSCHEN Agnes,GONZALEZ-RODRIGUEZ Jose

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb16982.x/fullpdf

Reference44 articles.

1. Tryptic digestion of human GPIIIa. Isolation and biochemical characterization of the 23 kDa N-terminal glycopeptide carrying the antigenic determinant for a monoclonal antibody (P37) which inhibits platelet aggregation

2. Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the α-subunit of human platelet glycoprotein IIb

3. Characterization of the β-chain N-terminus heterogeneity and the α-chain C-terminus of human platelet GPIIb

4. Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the β-subunits of the integrin family

5. Further studies on the topography of human platelet glycoprotein IIb. Localization of monoclonal antibody epitopes and the putative glycoprotein IIIa- and fibrinogen-binding regions

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