Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo.
about
Structural basis of Na+ activation mimicry in murine thrombinMechanism of the Anticoagulant Activity of Thrombin Mutant W215A/E217AStabilization of the E* Form Turns Thrombin into an AnticoagulantMolecular basis of thrombomodulin activation of slow thrombinMutant N143P Reveals How Na+ Activates ThrombinRigidification of the autolysis loop enhances Na+ binding to thrombinCrystal structure of the prothrombinase complex from the venom of Pseudonaja textilisThrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.Structural and energetic determinants of the S1-site specificity in serine proteases.Engineering thrombin for selective specificity toward protein C and PAR1.Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Redesigning allosteric activation in an enzyme.Allostery in trypsin-like proteases suggests new therapeutic strategies.Thrombin-activatable procarboxypeptidase B regulates activated complement C5a in vivo.Relative antithrombotic and antihemostatic effects of protein C activator versus low-molecular-weight heparin in primates.Conformational selection in trypsin-like proteases.Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: free energies and kinetics.The status of new anticoagulants.Thrombin.Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants.Neprilysin Inhibits Coagulation through Proteolytic Inactivation of FibrinogenRegulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI).Rational Design of Protein C Activators.New anticoagulants: how to deal with treatment failure and bleeding complications.Emerging technologies for protease engineering: New tools to clear out disease.Crystal structure of wild-type human thrombin in the Na+-free state.Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains.Role of the A chain in thrombin functionThrombomodulin is required for the antithrombotic activity of thrombin mutant W215A/E217A in a mouse model of arterial thrombosis.Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.Crystal structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery.Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation.Functional requirements for inhibition of thrombin by antithrombin III in the presence and absence of heparin.Limited generation of activated protein C during infusion of the protein C activator thrombin analog W215A/E217A in primates.Interplay between conformational selection and zymogen activation.
P2860
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P2860
Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@en
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@nl
type
label
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@en
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@nl
prefLabel
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@en
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@nl
P2093
P356
P1433
P1476
Protein engineering thrombin f ...... nticoagulant activity in vivo.
@en
P2093
Matsumura SY
Matteucci MD
P304
16449-16457
P356
10.1021/BI9616108
P407
P577
1996-12-01T00:00:00Z