Zobrazeno 1 - 10
of 98
pro vyhledávání: '"G Vilaire"'
Publikováno v:
Blood. 88:167-173
The integrin alpha IIb beta 3, a calcium-dependent heterodimer, plays a critical role in platelet aggregation. The alpha IIb subunit of the heterodimer contains four highly conserved putative calcium-binding domains in its extracellular portion. Duri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a9152d34083528099f6759872d51b78
https://doi.org/10.1182/blood.v88.1.167.167
https://doi.org/10.1182/blood.v88.1.167.167
Determinants of the intracellular fate of truncated forms of the platelet glycoproteins IIb and IIIa
Publikováno v:
Journal of Biological Chemistry. 268:3580-3585
The platelet glycoproteins GPIIb and GPIIIa are integral membrane proteins and form calcium-dependent heterodimers in the endoplasmic reticulum (ER). In the absence of heterodimer formation, GPIIb and GPIIIa are retained in the ER and degraded. To pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c91bd704fc84376fe5398800ea349249
https://doi.org/10.1016/s0021-9258(18)53733-9
https://doi.org/10.1016/s0021-9258(18)53733-9
Publikováno v:
Journal of Biological Chemistry. 266:23499-23504
The precursor of platelet membrane glycoprotein IIb (GPIIb) undergoes endoproteolytic cleavage into heavy and light chains post-translation. Endoproteolysis occurs within a 17-amino acid stretch of the precursor that contains 4 arginine residues, 3 i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1fe7fa35e408f96e40bd9da06582692b
https://doi.org/10.1016/s0021-9258(18)54525-7
https://doi.org/10.1016/s0021-9258(18)54525-7
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 1(4)
The integrin alphavbeta3 mediates platelet adhesion to the matrix protein osteopontin and likely is the predominant integrin mediating platelet adhesion to the matrix protein vitronectin. To address the mechanism that regulates alphavbeta3 activity i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::db62cb74367e9357611f1b0a5e130865
https://pubmed.ncbi.nlm.nih.gov/12871420
https://pubmed.ncbi.nlm.nih.gov/12871420
Autor:
R B, Basani, D L, French, G, Vilaire, D L, Brown, F, Chen, B S, Coller, J M, Derrick, T K, Gartner, J S, Bennett, M, Poncz
Publikováno v:
Blood. 95(1)
Decreased expression of functional alphaIIbbeta3 complexes on the platelet surface produces Glanzmann thrombasthenia. We have identified mutations of alphaIIb(P145) in 3 ethnically distinct families affected by Glanzmann thrombasthenia. Affected Menn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1528c8aa2413452774196da926637004
https://pubmed.ncbi.nlm.nih.gov/10607701
https://pubmed.ncbi.nlm.nih.gov/10607701
Publikováno v:
The Journal of biological chemistry. 273(24)
We studied the function of the platelet integrin alphaIIb beta3 using a B lymphocyte model in which alphaIIb beta3 can be induced to interact with fibrinogen using phorbol myristate acetate (PMA). To determine whether a G protein-coupled receptor cou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a841e648c2c10dd077316e8f75f27e22
https://pubmed.ncbi.nlm.nih.gov/9614143
https://pubmed.ncbi.nlm.nih.gov/9614143
Publikováno v:
Blood. 90(8)
We report a case of Glanzmann thrombasthenia in a Pakistani child whose platelets express less than 10% of the normal amount of alphaIIb beta3 on their surface. Single-stranded conformation polymorphism analysis of the exons of the patient's alphaIIb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3ef40be9f9da228b7f81960f069aa017
https://pubmed.ncbi.nlm.nih.gov/9376589
https://pubmed.ncbi.nlm.nih.gov/9376589
Determinants of the intracellular fate of truncated forms of the platelet glycoproteins IIb and IIIa
Publikováno v:
The Journal of biological chemistry. 268(5)
The platelet glycoproteins GPIIb and GPIIIa are integral membrane proteins and form calcium-dependent heterodimers in the endoplasmic reticulum (ER). In the absence of heterodimer formation, GPIIb and GPIIIa are retained in the ER and degraded. To pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::40cda8daf0eebb97a4df80268f001016
https://pubmed.ncbi.nlm.nih.gov/8429034
https://pubmed.ncbi.nlm.nih.gov/8429034
Publikováno v:
The Journal of biological chemistry. 267(23)
The platelet integrin, glycoprotein IIb-IIIa (GPIIb-IIIa), is a calcium-dependent heterodimer that binds fibrinogen, von Willebrand factor, and fibronectin after platelet activation. We examined GPIIb-IIIa alone and bound to these ligands by electron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8dc23b7ca30897853aee857d961c3c58
https://pubmed.ncbi.nlm.nih.gov/1644841
https://pubmed.ncbi.nlm.nih.gov/1644841
Publikováno v:
The Journal of biological chemistry. 266(34)
The precursor of platelet membrane glycoprotein IIb (GPIIb) undergoes endoproteolytic cleavage into heavy and light chains post-translation. Endoproteolysis occurs within a 17-amino acid stretch of the precursor that contains 4 arginine residues, 3 i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ea3cd2c630d4521b1baefa123f4758f5
https://pubmed.ncbi.nlm.nih.gov/1744141
https://pubmed.ncbi.nlm.nih.gov/1744141