Modulation of prothrombinase assembly and activity by phosphatidylethanolamine - Wikidata - wikimedia - TriplyDB

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

http://www.wikidata.org/entity/Q24634989

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Traumatic brain injury-associated coagulopathy Soluble phosphatidylserine binds to two sites on human factor IXa in a Ca2+ dependent fashion to specifically regulate structure and activity Lyso-Sulfatide Binds Factor Xa and Inhibits Thrombin Generation by the Prothrombinase Complex.Phosphatidylserine and Phosphatidylethanolamine Bind to Protein Z Cooperatively and with Equal Affinity Networks of enzymatically oxidized membrane lipids support calcium-dependent coagulation factor binding to maintain hemostasis.Enzymatically oxidized phospholipids restore thrombin generation in coagulation factor deficiencies.Factor Xa dimerization competes with prothrombinase complex formation on platelet-like membrane surfaces

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

http://www.wikidata.org/entity/Q24634989

description

2011 nî lūn-bûn

@nan

2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

@ast

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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type

label

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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prefLabel

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

@ast

Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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JBC.M111.260141

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Journal of Biological Chemistry

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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine

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P2093

Barry R Lentz

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

Mary Ann Quinn-Allen

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

William H Kane

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Xiaoe Liang

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

P2860

A cell-based model of hemostasis

The contribution of bovine Factor V and Factor Va to the activity of prothrombinase

Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders

The phosphatidylserine binding site of the factor Va C2 domain accounts for membrane binding but does not contribute to the assembly or activity of a human factor Xa-factor Va complex

Binding of human factor VIII to phospholipid vesicles

Insights into the complex association of bovine factor Va with acidic-lipid-containing synthetic membranes.

Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusion

Mutation in blood coagulation factor V associated with resistance to activated protein C.

A phosphatidylserine binding site in factor Va C1 domain regulates both assembly and activity of the prothrombinase complex.

Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids.

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35535-35542

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scholarly article

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3758995

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10.1074/JBC.M111.260141

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41

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286

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21859710

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3195639

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