Zobrazeno 1 - 10
of 56
pro vyhledávání: '"M. C. Berndt"'
Publikováno v:
The Journal of Immunology. 156:284-288
Evidence is presented that the mAb 25E11, directed against the platelet integrin alpha IIb beta 3 (glycoprotein IIbIIIa;CD41b/CD61) also binds the distinct myeloid cell integrin alpha M beta 2 (Mac-1;CDIIb/CD18). The Ab is shown to identify only the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b867d1ae79b1826063307c9dced1eaee
https://doi.org/10.4049/jimmunol.156.1.284
https://doi.org/10.4049/jimmunol.156.1.284
Publikováno v:
The Journal of Immunology. 153:3199-3209
P-selectin is an adhesion molecule for myeloid cells that seems to be essential for the development of cellular inflammatory responses. We show that adhesion of neutrophils to purified and recombinant P-selectin enhances the phagocytosis of unopsoniz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5246916e6fc67be418b8318f0776c2a6
https://doi.org/10.4049/jimmunol.153.7.3199
https://doi.org/10.4049/jimmunol.153.7.3199
Publikováno v:
Blood. 77:2190-2199
Sera of 12 patients with quinine/quinidine-induced thrombocytopenia showed drug-dependent antibody binding to glycoprotein (GP) Ib-IX complex. The reaction with GPIb-IX complex of 11 of these 12 sera was strongly inhibited by the complex-specific mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67dddc6d3d2b7fb5f5122b858187b85a
https://doi.org/10.1182/blood.v77.10.2190.bloodjournal77102190
https://doi.org/10.1182/blood.v77.10.2190.bloodjournal77102190
Publikováno v:
Journal of thrombosis and haemostasis : JTH. 2(12)
Binding of von Willebrand factor (VWF) to the platelet membrane glycoprotein (GP) Ib-IX-V complex initiates a cascade of events leading to alphaIIbbeta3 activation and platelet aggregation. The roles of ADP and thromboxane A2 (TXA2) in agglutination-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5b1ba3282e8bbe0b895404c7153cfeec
https://pubmed.ncbi.nlm.nih.gov/15613029
https://pubmed.ncbi.nlm.nih.gov/15613029
Autor:
M I, Furman, P, Nurden, M C, Berndt, A T, Nurden, S E, Benoit, M R, Barnard, F A, Ofosu, A D, Michelson
Publikováno v:
Thrombosis and haemostasis. 84(5)
The only known function of the 41 amino acid cleaved peptide (TR1-41) of the seven transmembrane domain thrombin receptor (PARI) is to activate platelets (as determined by aggregation, surface P-selectin, and fibrinogen binding to activated GPIIb-III
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0641318db48262eb2dcf9044316a02b8
https://pubmed.ncbi.nlm.nih.gov/11127874
https://pubmed.ncbi.nlm.nih.gov/11127874
Autor:
M A, Guthridge, F C, Stomski, E F, Barry, W, Winnall, J M, Woodcock, B J, McClure, M, Dottore, M C, Berndt, A F, Lopez
Publikováno v:
Molecular cell. 6(1)
In the hemopoietic compartment, IL-3, GM-CSF, and IL-5 receptors are major transducers of survival signals; however, the receptor-proximal events that determine this vital function have not been defined. We have found that IL-3 stimulation induces ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b5ede987afd0be61fdc0416ab647ccd2
https://pubmed.ncbi.nlm.nih.gov/10949031
https://pubmed.ncbi.nlm.nih.gov/10949031
Publikováno v:
Blood. 96(2)
The binding of von Willebrand factor (vWF) to glycoprotein (GP) Ib-IX-V stimulates transmembrane signaling events that lead to platelet adhesion and aggregation. Recent studies have revealed that the signaling protein 14-3-3 zeta binds directly to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::827e7cba64bb4e1f56e45b033cdcfecc
https://pubmed.ncbi.nlm.nih.gov/10887121
https://pubmed.ncbi.nlm.nih.gov/10887121
Autor:
Y, Shen, G M, Romo, J F, Dong, A, Schade, L V, McIntire, D, Kenny, J C, Whisstock, M C, Berndt, J A, López, R K, Andrews
Publikováno v:
Blood. 95(3)
The platelet glycoprotein (GP) Ib-IX-V complex mediates adhesion to von Willebrand factor (vWf) in (patho)physiologic thrombus formation. The vWf-binding site on GP Ib-IX-V is within the N-terminal 282 residues of GP Ibalpha, which consist of an N-te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::622127cb1aaecb6232fbe2af221ce030
https://pubmed.ncbi.nlm.nih.gov/10648402
https://pubmed.ncbi.nlm.nih.gov/10648402
Publikováno v:
Blood. 95(2)
Shear stress causes the platelet glycoprotein (Gp) Ib/IX/V to bind to von Willebrand factor, resulting in platelet adhesion. GpIb/IX/V also functions to stimulate transmembranous signaling, leading to platelet activation and the expression of a ligan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::226683d2fa8eefab0cbac1adcfa14197
https://pubmed.ncbi.nlm.nih.gov/10627461
https://pubmed.ncbi.nlm.nih.gov/10627461
Autor:
M, De Luca, D A, Facey, E J, Favaloro, M S, Hertzberg, J C, Whisstock, T, McNally, R K, Andrews, M C, Berndt
Publikováno v:
Blood. 95(1)
Binding of the adhesive glycoprotein, von Willebrand factor (vWf), to the platelet membrane glycoprotein (GP) Ib-IX-V complex initiates platelet adhesion and aggregation at high shear stress in hemostasis and thrombosis. In this study, the GP Ib-IX-V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fd2744dc0b93a518fc270637d731f0e
https://pubmed.ncbi.nlm.nih.gov/10607699
https://pubmed.ncbi.nlm.nih.gov/10607699