Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site.
about
Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibodyBasis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor XaCrystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor XThe linker connecting the two kringles plays a key role in prothrombin activationImplication of protein S thrombin-sensitive region with membrane binding via conformational changes in the gamma-carboxyglutamic acid-rich domainProthrombotic phenotype of protein Z deficiencyMutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site.Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. I. Application to blood coagulation: direct cation-protein electronic effects vs. indirect interactions through water networksProbing the structural changes in the light chain of human coagulation factor VIIa due to tissue factor associationModeling zymogen protein C.Isolation of a protein Z-dependent plasma protease inhibitorCapturing spontaneous partitioning of peripheral proteins using a biphasic membrane-mimetic model.Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preferenceThermodynamic and kinetic characterization of the protein Z-dependent protease inhibitor (ZPI)-protein Z interaction reveals an unexpected role for ZPI Lys-239.Phosphatidylserine and Phosphatidylethanolamine Bind to Protein Z Cooperatively and with Equal AffinityManipulation of the membrane binding site of vitamin K-dependent proteins: enhanced biological function of human factor VII.Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.Coagulation abnormalities of sickle cell disease: Relationship with clinical outcomes and the effect of disease modifying therapies.Factor VII and protein C are phosphatidic acid-binding proteins.Down-regulation of the clotting cascade by the protein C pathwayA chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity.Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization.Factor VIIa binding and internalization in hepatocytesSnake-venom-derived Factor IX-binding protein specifically blocks the gamma-carboxyglutamic acid-rich-domain-mediated membrane binding of human Factors IX and X.Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa.Association free energy of dipalmitoylphosphatidylserines in a mixed dipalmitoylphosphatidylcholine membrane.Multifunctional specificity of the protein C/activated protein C Gla domain.Kinetic characterization of the protein Z-dependent protease inhibitor reaction with blood coagulation factor Xa.The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes.Platelet factor 4 impairs the anticoagulant activity of activated protein C.Localization of phosphatidylserine binding sites to structural domains of factor Xa.Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes. A surface plasmon resonance study.A simple method to discriminate between beta2-glycoprotein I- and prothrombin-dependent lupus anticoagulants.Sphingolipids as bioactive regulators of thrombin generation.Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C.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.Lipid oxidation inactivates the anticoagulant function of protein Z-dependent protease inhibitor (ZPI).Surface-dependent coagulation enzymes. Flow kinetics of factor Xa generation on live cell membranes.Enhancement of human protein C function by site-directed mutagenesis of the gamma-carboxyglutamic acid domain.
P2860
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P2860
Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Comparison of naturally occurr ...... gests a membrane contact site.
@en
type
label
Comparison of naturally occurr ...... gests a membrane contact site.
@en
prefLabel
Comparison of naturally occurr ...... gests a membrane contact site.
@en
P2093
P356
P1433
P1476
Comparison of naturally occurr ...... gests a membrane contact site.
@en
P2093
Dahlbäck B
McDonald JF
Nelsestuen GL
Schwalbe RA
P304
P356
10.1021/BI9626160
P407
P577
1997-04-01T00:00:00Z