Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate.
about
Coagulation Factor XIIIA Subunit Missense Mutations Affect Structure and Function at the Various Steps of Factor XIII ActionMolecular recognition mechanisms of thrombin.Autoantibodies to thrombin directed against both of its cryptic exosites.Thrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.How Na+ activates thrombin--a review of the functional and structural data.A hereditary bleeding disorder resulting from a premature stop codon in thrombomodulin (p.Cys537Stop)Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants.Factor XIII: a coagulation factor with multiple plasmatic and cellular functions.Fibrin(ogen) and thrombotic disease.The interaction between fibrinogen and zymogen FXIII-A2B2 is mediated by fibrinogen residues γ390-396 and the FXIII-B subunits.Polyphosphate binds with high affinity to exosite II of thrombin.Elimination of coagulation factor XIII from fibrinogen preparations.Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.The effect of blood coagulation factor XIII on fibrin clot structure and fibrinolysis.Screening cleavage of Factor XIII V34X Activation Peptides by thrombin mutants: A strategy for controlling fibrin architecture.
P2860
Q28114772-8D8E1341-65AF-47C4-BF50-09E69F1FEA63Q33221756-2021244C-BB41-4619-98CA-254903F55BB3Q33231591-CF6EDBD8-C61D-4FC6-9E3A-846523A0F5DAQ33328373-C6EE5BC6-AB62-45E5-98A4-8BCCAF4F231CQ33382168-466ED6F4-6E3E-4222-B479-0AF655D829ECQ34209350-592E2797-3AAF-4AD0-8BF0-7C92543A70A3Q36819410-DFA0A52B-3597-4016-8F44-6330587E5E3AQ37899674-21914E2F-080E-41F8-9DBC-39CE877B43E0Q38117741-E8DE3C56-FF57-4635-8E80-95933EC56EE8Q39453804-D0454FEC-4FF3-4E4D-8D7B-AB411CD698B7Q40092357-B5FA8219-2367-4C18-8600-A23F8675DA0CQ40796682-A512A108-2C64-4B09-830E-9FCAED7A474BQ45176583-B67FEF51-EE94-47BE-943F-9C5EB648EA08Q45906428-9AF3C760-A253-4637-9E69-473250E42A80Q48728275-2966AE6A-5108-46B9-9C77-F1EEC5685388
P2860
Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Roles of low specificity and c ...... thrombin determines its fate.
@en
Roles of low specificity and c ...... thrombin determines its fate.
@nl
type
label
Roles of low specificity and c ...... thrombin determines its fate.
@en
Roles of low specificity and c ...... thrombin determines its fate.
@nl
prefLabel
Roles of low specificity and c ...... thrombin determines its fate.
@en
Roles of low specificity and c ...... thrombin determines its fate.
@nl
P2093
P2860
P356
P1476
Roles of low specificity and c ...... thrombin determines its fate.
@en
P2093
David A Lane
Helen Philippou
James Rance
Lawrence Leung
Peter J Grant
Scott W Hall
Timothy Myles
P2860
P304
32020-32026
P356
10.1074/JBC.M305364200
P407
P577
2003-06-06T00:00:00Z