Platelets have more than one binding site for von Willebrand factor. - Wikidata - awgldk - TriplyDB

Platelets have more than one binding site for von Willebrand factor.

Platelets have more than one binding site for von Willebrand factor.

http://www.wikidata.org/entity/Q33821754

about

Evidence that the primary binding site of von Willebrand factor that mediates platelet adhesion on subendothelium is not collagen Isolation of the thrombospondin membrane receptor Identification of three tyrosine residues of glycoprotein Ib alpha with distinct roles in von Willebrand factor and alpha-thrombin binding ADAMTS13 substrate recognition of von Willebrand factor A2 domain Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib Variant Bernard-Soulier syndrome type bolzano. A congenital bleeding disorder due to a structural and functional abnormality of the platelet glycoprotein Ib-IX complex Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3 Evaluation of the role of proline residues flanking the RGD motif of dendroaspin, an inhibitior of platelet aggregation and cell adhesion On the association of glycoprotein Ib and actin-binding protein in human platelets Molecular imaging of activated von Willebrand factor to detect high-risk atherosclerotic phenotype.Activation-independent platelet adhesion and aggregation under elevated shear stress Size regulation of von Willebrand factor-mediated platelet thrombi by ADAMTS13 in flowing blood Cochlin and glaucoma: a mini-review.Genetic deletion of platelet glycoprotein Ib alpha but not its extracellular domain protects from atherosclerosis.Von Willebrand's disease with spontaneous platelet aggregation induced by an abnormal plasma von Willebrand factor.von Willebrand factor binds to platelets and induces aggregation in platelet-type but not type IIB von Willebrand disease Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment.von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure.Spontaneously occurring tumors of companion animals as models for human cancer.The role of von Willebrand factor and fibrinogen in platelet aggregation under varying shear stress Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor.Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association Distinct abnormalities in the interaction of purified types IIA and IIB von Willebrand factor with the two platelet binding sites, glycoprotein complexes Ib-IX and IIb-IIIa Combined blockade of ADP receptors and PI3-kinase p110β fully prevents platelet and leukocyte activation during hypothermic extracorporeal circulation Agkistrodon piscivorus piscivorus platelet aggregation inhibitor: a potent inhibitor of platelet activation.A myeloma paraprotein with specificity for platelet glycoprotein IIIa in a patient with a fatal bleeding disorder.Asialo von Willebrand factor interactions with platelets. Interdependence of glycoproteins Ib and IIb/IIIa for binding and aggregation.Functionally thrombasthenic state in normal platelets following the administration of ticlopidine.A monoclonal antibody to human platelet glycoprotein IIIa detects a related protein in cultured human endothelial cells.A new murine monoclonal antibody reports an activation-dependent change in the conformation and/or microenvironment of the platelet glycoprotein IIb/IIIa complex von Willebrand protein facilitates platelet incorporation in polymerizing fibrin Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type IIA von Willebrand disease from those generated by plasmin Fibrinogen-independent platelet adhesion and thrombus formation on subendothelium mediated by glycoprotein IIb-IIIa complex at high shear rate.Independent modulation of von Willebrand factor and fibrinogen binding to the platelet membrane glycoprotein IIb/IIIa complex as demonstrated by monoclonal antibody.von Willebrand factor interaction with the glycoprotein IIb/IIa complex. Its role in platelet function as demonstrated in patients with congenital afibrinogenemia.Interaction of von Willebrand factor with human platelets in the plasma milieu Interaction of asialo von Willebrand factor with glycoprotein Ib induces fibrinogen binding to the glycoprotein IIb/IIIa complex and mediates platelet aggregation.Platelet adhesion under flow.Thrombin-dependent Incorporation of von Willebrand Factor into a Fibrin Network.G protein-dependent basal and evoked endothelial cell vWF secretion.

P2860

Q24292860-CFF2BC4A-802F-4EE5-B0EE-9637987C4E4D Q24314835-3674D84B-442A-45D5-AA9E-CD927CDC4CD4 Q24314966-57C3BFF2-BD85-426D-807C-4BC7B1D3EE3C Q24338203-4826C902-0360-41B6-B658-7CC08B71B2AB Q24596704-41E8BFE8-2F58-43F3-8D35-301C57F674C8 Q24620409-4F7DC230-8DBA-449B-8D44-FE0C9AF3C203 Q28216733-A3F694BE-698B-40FD-AB4F-0603203D3B76 Q28363214-A595F248-AD22-475A-BAE2-C1FB8E62E8D7 Q28609736-76186DEE-55DA-46F1-9ECB-5A4F7FB595C5 Q30473382-BC6DE642-2C41-4C82-90CB-16944B978950 Q30479636-1AF49E74-4370-4D6D-B6FE-FDED3689C3E7 Q30479643-2F9CC154-4356-4045-AB9F-CA073717708D Q30499664-4135BC6D-C3A4-46E6-A164-1918A165E1DF Q30650321-D616384B-8EA5-4796-A7A2-557C5E9FA16D Q33444536-88838940-A5A2-45DA-A52D-B74F8EC44AEA Q33478102-2313F86B-4B58-41B0-B9D1-26DF8C8AC61D Q33899500-5FECBC9F-65E4-4E4A-8316-FC27FC0A9A93 Q33899746-B76F2168-1479-4857-A346-FC8D554074EA Q33927360-0B06C168-1564-4AA4-9E68-969300884CFC Q34182746-AE9C8478-A2CA-4D7D-B98E-C881F0D769CE Q34196324-5CB3F59F-2231-4A45-BA07-E739573A5231 Q34207017-C3F69538-28CC-42B9-8D0B-9C38F04CB316 Q34260216-79B4F758-EB61-4F1A-9275-10443CF270EC Q34305447-18C33999-7671-4E64-8F4B-7CA9F593355C Q34313515-D02AC7A9-2177-4F77-9293-48C5C51E58A2 Q34518712-7B764FAC-2355-4337-8B48-82F7D05B9F32 Q34521638-39CE39E2-B1E9-4AB2-99CD-FD2DA5F42835 Q34528200-37A99E8E-DDB7-4F63-89ED-14A4C37351ED Q34536168-0A656022-4981-464A-BEF2-D6D8BE8E1978 Q34541247-B75113B7-0842-4A50-AD21-0D934C5D75B1 Q34544068-16E186A9-89B2-4FD6-B0B3-B16042EA8FDD Q34560030-6AB62DD6-5EC1-4F7C-B6FF-768A83FA8D65 Q34564820-BED1E16E-7AB5-4EC9-B6B0-5E333965885D Q34565552-ECE87509-336B-4F04-945C-3B58864BA913 Q34574601-E8159075-8ACD-4307-9386-A9CEEE09EE36 Q34602783-A536DBDE-7FD3-40D7-B587-47ED05AD475E Q34624945-D816191B-475C-44E7-9B19-FD5B6E94D328 Q34673739-4CF77E1C-7B22-4C68-B40E-839E36D51F48 Q34774500-4FD032FD-BB34-46A2-BFFB-A0B8051DC8C5 Q35003012-6FCCA443-1A67-498C-A11A-D43787E2E392

P2860

Platelets have more than one binding site for von Willebrand factor.

http://www.wikidata.org/entity/Q33821754

description

1983 nî lūn-bûn

@nan

1983 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1983 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1983年の論文

@ja

1983年論文

@yue

1983年論文

@zh-hant

1983年論文

@zh-hk

1983年論文

@zh-mo

1983年論文

@zh-tw

1983年论文

@wuu

name

Platelets have more than one binding site for von Willebrand factor.

@ast

Platelets have more than one binding site for von Willebrand factor.

@en

type

label

Platelets have more than one binding site for von Willebrand factor.

@ast

Platelets have more than one binding site for von Willebrand factor.

@en

prefLabel

Platelets have more than one binding site for von Willebrand factor.

@ast

Platelets have more than one binding site for von Willebrand factor.

@en

P1433

Q33821754-B3A27D32-9E95-4CA6-A572-DC3F785D3429

P1476

Q33821754-5A30C4B3-3EDD-464B-95DF-0235A2FDB16A

P2093

Q33821754-11A1CD86-0564-4A8B-AA67-2703D463EDC9

Q33821754-1731222D-367F-4417-94C4-37DF372B0226

Q33821754-76E46940-DB0A-4DD3-9277-EBE14103EADC

Q33821754-C3A25C6E-938B-40BE-8A3A-CD90B721CF3D

Q33821754-D32D46C7-A2BB-4607-8E87-944E3E95DB06

P2860

Q33821754-1D0B23A6-BCE5-4571-82EC-E95262E7F44E

Q33821754-29FCF5E0-5657-47C2-BAB8-3952DB42A749

Q33821754-2DEF871C-17E5-4E2C-BD90-8EBE6C5F4DA9

Q33821754-38E4B980-400B-46D6-B0A8-DFD1B74F064C

Q33821754-41ED6F82-5A6D-49BD-9546-30AC49488A80

Q33821754-4EA4E130-FF46-42A7-BEF1-3FAE8B415203

Q33821754-550A4C09-2045-4DEF-84E5-ABB3A49D0217

Q33821754-550B06D8-C9BC-484F-80A1-7944ACA5E91F

Q33821754-56796BB4-E787-4749-81B3-72B644D98872

Q33821754-70EC3B20-0674-42D4-85DC-D5809BDC8F89

P304

Q33821754-8F114728-3609-4D9C-B4FB-C7A83403DF3E

P31

Q33821754-54033936-D6F3-4F49-9DCF-BF27346C228F

P356

Q33821754-74D795A5-17A1-4BDC-9142-A20E3E623F5D

P407

Q33821754-86359C1C-229A-4C85-89BB-EF7FD19EB277

P433

Q33821754-0447E1E8-77D0-42A7-AB96-651EB36A29C7

P478

Q33821754-A004E40F-92D1-4EE9-BC5A-BB44D42CB6B6

P577

Q33821754-F2A772E2-DE17-46FA-8D4C-CC4438BC21E0

P5875

Q33821754-25AAA8A6-45B7-4B94-9827-C79FD2C2390C

P698

Q33821754-889EC808-EA5F-4D20-8168-14195C970C36

P932

Q33821754-97C48FE6-2E94-46BE-BBDB-4CB23E361F04

P356

P1433

Journal of Clinical Investigation

P1476

Platelets have more than one binding site for von Willebrand factor.

@en

P2093

L De Marco

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

L Gatti

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

R Bader

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

R R Montgomery

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

Z M Ruggeri

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

P2860

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril

Preparation of iodine-131 labelled human growth hormone of high specific activity

Decreased adhesion of giant (Bernard-Soulier) platelets to subendothelium. Further implications on the role of the von Willebrand factor in hemostasis.

Platelet membrane defects in Glanzmann's thrombasthenia. Evidence for decreased amounts of two major glycoproteins

Studies on human antihemophilic factor. Evidence for a covalently linked subunit structure.

Diagnosis of Bernard-Soulier syndrome and Glanzmann's thrombasthenia with a monoclonal assay on whole blood.

Glanzmann thrombasthenia: deficient binding of von Willebrand factor to thrombin-stimulated platelets.

Thrombin-induced exposure and prostacyclin inhibition of the receptor for factor VIII/von Willebrand factor on human platelets.

Analysis of the glycoprotein and protein composition of Bernard-Soulier platelets by single and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

P304

1-12

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

P31

scholarly article

P356

10.1172/JCI110946

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

P407

P433

1

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

P478

72

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

P577

1983-07-01T00:00:00Z

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

P5875

16972209

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

P698

6223940

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

P932

1129155

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