Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant
about
Structure of human factor VIIa and its implications for the triggering of blood coagulationPeptide exosite inhibitors of factor VIIa as anticoagulantsIsolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle TickMechanism of the Ca2+-induced Enhancement of the Intrinsic Factor VIIa ActivityStructural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activityDeciphering the shape and deformation of secondary structures through local conformation analysis.Engineering of substrate selectivity for tissue factor.factor VIIa complex signaling through protease-activated receptor 2.Substitution of valine for leucine 305 in factor VIIa increases the intrinsic enzymatic activity.Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.Computational alanine scanning with linear scaling semiempirical quantum mechanical methods.Engineering kunitz domain 1 (KD1) of human tissue factor pathway inhibitor-2 to selectively inhibit fibrinolysis: properties of KD1-L17R variantHeparin modulates the 99-loop of factor IXa: effects on reactivity with isolated Kunitz-type inhibitor domains.Recent estimates of the structure of the factor VIIa (FVIIa)/tissue factor (TF) and factor Xa (FXa) ternary complex.Structural biology of factor VIIa/tissue factor initiated coagulationProtein anticoagulants targeting factor VIIa-tissue factor complex: a comprehensive review.Properties of spin and fluorescent labels at a receptor-ligand interface.Characterization of mutations causing factor VII deficiency in 61 unrelated Israeli patients.A Machine Learning Approach for Hot-Spot Detection at Protein-Protein Interfaces.Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking.Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factorAugmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement.Homology modeling and structural validation of tissue factor pathway inhibitor.A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation.Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa.Predicted solution structure of zymogen human coagulation FVII.Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes.The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa.Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2.Severe factor XI deficiency caused by a Gly555 to Glu mutation (factor XI-Glu555): a cross-reactive material positive variant defective in factor IX activation.Crystal structure of Kunitz domain 1 (KD1) of tissue factor pathway inhibitor-2 in complex with trypsin. Implications for KD1 specificity of inhibition.High resolution structures of p-aminobenzamidine- and benzamidine-VIIa/soluble tissue factor: unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa.Calcium-Binding EGF-Like Domains
P2860
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P2860
Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@ast
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@en
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@nl
type
label
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@ast
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@en
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@nl
prefLabel
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@ast
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@en
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@nl
P2093
P3181
P356
P1476
Structure of extracellular tis ...... a inhibited with a BPTI mutant
@en
P2093
P304
P3181
P356
10.1006/JMBI.1998.2452
P407
P577
1999-02-05T00:00:00Z