Conversion of thrombin into an anticoagulant by protein engineering.
about
Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complexCrystal structure of the anticoagulant slow form of thrombinStructural 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 AnticoagulantMutant N143P Reveals How Na+ Activates ThrombinRigidification of the autolysis loop enhances Na+ binding to thrombinRole of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.How Na+ activates thrombin--a review of the functional and structural data.Engineering thrombin for selective specificity toward protein C and PAR1.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.The development of inflammatory joint disease is attenuated in mice expressing the anticoagulant prothrombin mutant W215A/E217A.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.Determinants of specificity in coagulation proteases.Salmon-derived thrombin inhibits development of chronic pain through an endothelial barrier protective mechanism dependent on APC.The status of new anticoagulants.Role of Na+ and K+ in enzyme function.Factor Va alters the conformation of the Na+-binding loop of factor Xa in the prothrombinase complexThrombin.Exosites in the substrate specificity of blood coagulation reactions.Serine proteases.Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI).Mutagenesis studies toward understanding allostery in thrombin.Rational Design of Protein C Activators.Proteases as therapeutics.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.Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants.Changes in amino-terminal portion of human B2 receptor selectively increase efficacy of synthetic ligand HOE 140 but not of cognate ligand bradykinin.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.Functional requirements for inhibition of thrombin by antithrombin III in the presence and absence of heparin.Molecular dissection of Na+ binding to thrombin.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
Conversion of thrombin into an anticoagulant by protein engineering.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh-hant
name
Conversion of thrombin into an anticoagulant by protein engineering.
@en
Conversion of thrombin into an anticoagulant by protein engineering.
@nl
type
label
Conversion of thrombin into an anticoagulant by protein engineering.
@en
Conversion of thrombin into an anticoagulant by protein engineering.
@nl
prefLabel
Conversion of thrombin into an anticoagulant by protein engineering.
@en
Conversion of thrombin into an anticoagulant by protein engineering.
@nl
P2093
P356
P1433
P1476
Conversion of thrombin into an anticoagulant by protein engineering.
@en
P2093
Matsumura SY
P2888
P304
P356
10.1038/378413A0
P407
P577
1995-11-01T00:00:00Z
P6179
1040789707