Molecular determinants of phospholipid synergy in blood clotting. - Wikidata - awgldk - TriplyDB

Molecular determinants of phospholipid synergy in blood clotting.

Molecular determinants of phospholipid synergy in blood clotting.

http://www.wikidata.org/entity/Q35067808

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Tissue factor/factor VIIa complex: role of the membrane surface Tissue factor encryption and decryption: facts and controversies Accelerating membrane insertion of peripheral proteins with a novel membrane mimetic model.Phosphatidylserine and Phosphatidylethanolamine Bind to Protein Z Cooperatively and with Equal Affinity GPU/CPU Algorithm for Generalized Born/Solvent-Accessible Surface Area Implicit Solvent Calculations.Peripheral membrane associations of matrix metalloproteinases.Regulation of tissue factor coagulant activity on cell surfaces.Characterization of platelet aminophospholipid externalization reveals fatty acids as molecular determinants that regulate coagulation Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.Atomic-level description of protein-lipid interactions using an accelerated membrane model.Bacillus anthracis peptidoglycan activates human platelets through FcγRII and complement.Kinetic regulation of the binding of prothrombin to phospholipid membranes.Factor VII and protein C are phosphatidic acid-binding proteins.Exactin: A specific inhibitor of Factor X activation by extrinsic tenase complex from the venom of Hemachatus haemachatus.Partitioning of amino acids into a model membrane: capturing the interface.Lipid profile of platelets and platelet-derived microparticles in ovarian cancer.Nanodiscs in Membrane Biochemistry and Biophysics.The Charge Properties of Phospholipid Nanodiscs A new cell culture-based assay quantifies vitamin K 2,3-epoxide reductase complex subunit 1 function and reveals warfarin resistance phenotypes not shown by the dithiothreitol-driven VKOR assay.Kinetic analysis and binding studies of a new recombinant human factor VIIa for treatment of haemophilia.Networks of enzymatically oxidized membrane lipids support calcium-dependent coagulation factor binding to maintain hemostasis.Multiplexed silicon photonic sensor arrays enable facile characterization of coagulation protein binding to nanodiscs with variable lipid content.Lipid specificity of the membrane binding domain of coagulation factor X.Enzymatically oxidized phospholipids restore thrombin generation in coagulation factor deficiencies.Influence of membrane composition on the enhancement of factor VIIa/tissue factor activity by magnesium ions.Interactions in globular proteins with polyampholyte: coacervation route for protein separation Cell type-resolved human lung lipidome reveals cellular cooperation in lung function

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P2860

Molecular determinants of phospholipid synergy in blood clotting.

http://www.wikidata.org/entity/Q35067808

description

2011 nî lūn-bûn

@nan

2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Molecular determinants of phospholipid synergy in blood clotting.

@ast

Molecular determinants of phospholipid synergy in blood clotting.

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type

label

Molecular determinants of phospholipid synergy in blood clotting.

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Molecular determinants of phospholipid synergy in blood clotting.

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prefLabel

Molecular determinants of phospholipid synergy in blood clotting.

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Molecular determinants of phospholipid synergy in blood clotting.

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JBC.M111.251769

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Journal of Biological Chemistry

P1476

Molecular determinants of phospholipid synergy in blood clotting.

@en

P2093

Chad M Rienstra

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

Mary C Clay

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

Narjes Tavoosi

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

Rebecca L Davis-Harrison

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Y Zenmei Ohkubo

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P2860

Comparison of simple potential functions for simulating liquid water

Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins

VMD: visual molecular dynamics

Scalable molecular dynamics with NAMD

Exposure of platelet membrane phosphatidylserine regulates blood coagulation

Surface exposure of phosphatidylserine in pathological cells

Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations

Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types.

Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers.

Tissue factor: a key molecule in hemostatic and nonhemostatic systems.

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23247-23253

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scholarly article

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10.1074/JBC.M111.251769

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26

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286

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Emad Tajkhorshid

Taras Pogorelov

James H Morrissey

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2011-05-11T00:00:00Z

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51116802

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21561861

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3123091

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