Conformational changes in the A1 domain of von Willebrand factor modulating the interaction with platelet glycoprotein Ibalpha.
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Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibalpha binding mechanism induced by snake venom proteinsLateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3A molten globule intermediate of the von Willebrand factor A1 domain firmly tethers platelets under shear flowMisfolding of vWF to pathologically disordered conformations impacts the severity of von Willebrand diseaseEnhanced Local Disorder in a Clinically Elusive von Willebrand Factor Provokes High-Affinity Platelet Clumping.The mechanism of VWF-mediated platelet GPIbalpha binding.Identification of a selective agonist for liver X receptor α (LXRα) via screening of a synthetic compound library.PPARalpha agonist-induced rodent tumors: modes of action and human relevance.Adhesive properties of the isolated amino-terminal domain of platelet glycoprotein Ibalpha in a flow fieldDifferential surface activation of the A1 domain of von Willebrand factor.A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.Distinct mechanisms of platelet aggregation as a consequence of different shearing flow conditions.Glycans and the platelet life cycle.A biophysical view on von Willebrand factor activation.Distinct structural attributes regulating von Willebrand factor A1 domain interaction with platelet glycoprotein Ibalpha under flow.Modeling and functional analysis of the interaction between von Willebrand factor A1 domain and glycoprotein Ibalpha.Cloning of the cDNA for murine von Willebrand factor and identification of orthologous genes reveals the extent of conservation among diverse species.Factor XI interacts with the leucine-rich repeats of glycoprotein Ibalpha on the activated platelet.Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets.Specific electrostatic interactions between charged amino acid residues regulate binding of von Willebrand factor to blood platelets.A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor.The functions of the A1A2A3 domains in von Willebrand factor include multimerin 1 binding.von Willebrand Factor, Free Hemoglobin and Thrombosis in ECMO
P2860
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P2860
Conformational changes in the A1 domain of von Willebrand factor modulating the interaction with platelet glycoprotein Ibalpha.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Conformational changes in the ...... platelet glycoprotein Ibalpha.
@en
type
label
Conformational changes in the ...... platelet glycoprotein Ibalpha.
@en
prefLabel
Conformational changes in the ...... platelet glycoprotein Ibalpha.
@en
P2093
P2860
P356
P1476
Conformational changes in the ...... platelet glycoprotein Ibalpha.
@en
P2093
P2860
P304
P356
10.1074/JBC.271.15.9046
P407
P577
1996-04-01T00:00:00Z