The interaction of thrombin with fibrinogen. A structural basis for its specificity.
about
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexesCrystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism.Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptidesInteraction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complexCrystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolutionCrystal Structure of Thrombin Bound to the Uncleaved Extracellular Fragment of PAR1Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junctionCrystal Structure of Thrombin in Complex with S-Variegin: Insights of a Novel Mechanism of Inhibition and Design of Tunable Thrombin InhibitorsExposure of R169 controls protein C activation and autoactivationCrystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombinX-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognitionCrystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bugX-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombinExamining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutationDynamics Govern Specificity of a Protein-Protein Interface: Substrate Recognition by ThrombinDeterminants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Identification and characterisation of C1q-binding phage displayed peptides.From natural to synthetic multisite thrombin inhibitors.Identification of residues linked to the slow-->fast transition of thrombin.Engineering thrombin for selective specificity toward protein C and PAR1.The structure of thrombin, a chameleon-like proteinase.The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand bindingHirunorms are true hirudin mimetics. The crystal structure of human alpha-thrombin-hirunorm V complexThrombin.Crystal structure of the complex between thrombin and the central "E" region of fibrin.Structural basis for sequential cleavage of fibrinopeptides upon fibrin assemblyNeprilysin Inhibits Coagulation through Proteolytic Inactivation of FibrinogenRole of P2 glycine in determining the specificity of antithrombin reaction with coagulation proteases.Protease Inhibitors in View of Peptide Substrate Databases.Identification of key residues involved in mediating the in vivo anti-tumor/anti-endothelial activity of Alphastatin.High-affinity RNA ligands to human alpha-thrombin.The N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates alpha-thrombin activity: potential clinical implications.Effects of introducing fibrinogen Aalpha character into the factor XIII activation peptide segment.Contribution of interactions with the core domain of hirudin to the stability of its complex with thrombin.Interaction of activated protein C with serpins.The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulinFunctional mapping of the surface residues of human thrombin.Hirulog-1 and -B2 thrombin specificity.Synthesis of oligopeptide chloromethanes to investigate extended binding regions of proteinases: application to the interaction of fibrinogen with thrombin.
P2860
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P2860
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
description
1992 nî lūn-bûn
@nan
1992 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@ast
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@en
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@nl
type
label
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@ast
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@en
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@nl
prefLabel
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@ast
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@en
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@nl
P2093
P1433
P1476
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1992.TB16916.X
P407
P577
1992-05-01T00:00:00Z