Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain - Wikidata - thesis-toulmin - TriplyDB

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

http://www.wikidata.org/entity/Q22253890

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Identification and characterization of AMACO, a new member of the von Willebrand factor A-like domain protein superfamily with a regulated expression in the kidney ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics Crystal structure of the platelet glycoprotein Ib(alpha) N-terminal domain reveals an unmasking mechanism for receptor activation Structural and functional features of a collagen-binding matrix protein from the mussel byssus A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor Platelets lacking PIP5KIγ have normal integrin activation but impaired cytoskeletal-membrane integrity and adhesion Localization of the adhesion receptor glycoprotein Ib-IX-V complex to lipid rafts is required for platelet adhesion and activation Functional display of platelet-binding VWF fragments on filamentous bacteriophage Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain.Platelet adhesion involves a novel interaction between vimentin and von Willebrand factor under high shear stress The interaction between factor H and Von Willebrand factor.Further characterization of ADAMTS-13 inactivation by thrombin.Misfolding of vWF to pathologically disordered conformations impacts the severity of von Willebrand disease Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stress The mechanism of VWF-mediated platelet GPIbalpha binding.Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond.Kinetics of GPIbalpha-vWF-A1 tether bond under flow: effect of GPIbalpha mutations on the association and dissociation rates.Mechanics of transient platelet adhesion to von Willebrand factor under flow GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease.Exploiting the kinetic interplay between GPIbα-VWF binding interfaces to regulate hemostasis and thrombosis The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis.N-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress.Cooperative unfolding of distinctive mechanoreceptor domains transduces force into signals.Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalpha.The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Ibα.Highly electronegative LDL from patients with ST-elevation myocardial infarction triggers platelet activation and aggregation Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibalpha.Platelets in leucocyte recruitment and function.Modelling platelet-blood flow interaction using the subcellular element Langevin method.New Concepts and Mechanisms of Platelet Activation Signaling.The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.Modifying murine von Willebrand factor A1 domain for in vivo assessment of human platelet therapies.The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen.A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct.A template-assembled synthetic protein surface mimetic of the von Willebrand factor A1 domain inhibits botrocetin-induced platelet aggregation.Inhibition of von Willebrand factor-GPIb/IX/V interactions as a strategy to prevent arterial thrombosis.The functions of the A1A2A3 domains in von Willebrand factor include multimerin 1 binding.

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Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

http://www.wikidata.org/entity/Q22253890

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2000 nî lūn-bûn

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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2000 թվականի հունիսին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

@ast

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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type

label

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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prefLabel

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

@ast

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

@en

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

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Journal of Biological Chemistry

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Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

@en

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J Emsley

http://www.w3.org/2001/XMLSchema#string

M A Cruz

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R I Handin

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R Liddington

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T G Diacovo

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Structural basis of collagen recognition by integrin alpha2beta1

Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab

Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib

Raster3D Version 2.0. A program for photorealistic molecular graphics

Substructure of human von Willebrand factor.

Platelet interaction with rabbit subendothelium in von Willebrand's disease: altered thrombus formation distinct from defective platelet adhesion

Interaction of asialo von Willebrand factor with glycoprotein Ib induces fibrinogen binding to the glycoprotein IIb/IIIa complex and mediates platelet aggregation.

Production in Escherichia coli of a biologically active subfragment of von Willebrand factor corresponding to the platelet glycoprotein Ib, collagen and heparin binding domains.

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19098-105

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scholarly article

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4498899

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10.1074/JBC.M002292200

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25

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275

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2000-06-23T00:00:00Z

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10764791

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Von Willebrand factor