Prothrombin kringle 1 domain interacts with factor Va during the assembly of prothrombinase complex.
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Crystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of ActivationThe linker connecting the two kringles plays a key role in prothrombin activationRole of activated protein C in Helicobacter pylori-associated gastritisProthrombin structure: unanticipated features and opportunities.What the structure of angiostatin may tell us about its mechanism of action.How the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of ProthrombinHD1, a thrombin-directed aptamer, binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.The Dual Regulatory Role of Amino Acids Leu480 and Gln481 of Prothrombin.Prothrombin kringle-2 domain has a growth inhibitory activity against basic fibroblast growth factor-stimulated capillary endothelial cells.Intratracheal administration of activated protein C inhibits bleomycin-induced lung fibrosis in the mouse.Neutral glycosphingolipid-dependent inactivation of coagulation factor Va by activated protein C and protein S.Role of prothrombin fragment 1 in the pathway of regulatory exosite I formation during conversion of human prothrombin to thrombin.Prothrombin residues 473-487 contribute to factor Va binding in the prothrombinase complex.Identification of distinct sequences in human blood coagulation factor Xa and prothrombin essential for substrate and cofactor recognition in the prothrombinase complex.Effects of prothrombin on the individual activated protein C-mediated cleavages of coagulation factor Va.Prothrombin amino terminal region helps protect coagulation factor Va from proteolytic inactivation by activated protein C.A control switch for prothrombinase: characterization of a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain that regulates the rate and pathway for prothrombin activation.Structure of Coagulation Factor II: Molecular Mechanism of Thrombin Generation and Development of Next-Generation Anticoagulants
P2860
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P2860
Prothrombin kringle 1 domain interacts with factor Va during the assembly of prothrombinase complex.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@en
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@nl
type
label
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@en
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@nl
prefLabel
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@en
Prothrombin kringle 1 domain i ...... bly of prothrombinase complex.
@nl
P2093
P2860
P356
P1433
P1476
Prothrombin kringle 1 domain i ...... mbly of prothrombinase complex
@en
P2093
P2860
P304
P356
10.1042/BJ3210729
P407
P478
321 ( Pt 3)
P577
1997-02-01T00:00:00Z