Identification of residues linked to the slow-->fast transition of thrombin. - Wikidata - awgldk - TriplyDB

Identification of residues linked to the slow-->fast transition of thrombin.

Identification of residues linked to the slow-->fast transition of thrombin.

http://www.wikidata.org/entity/Q33763127

about

Unexpected crucial role of residue 225 in serine proteases Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery Crystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of Activation Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.How Na+ activates thrombin--a review of the functional and structural data.Residue 225 determines the Na(+)-induced allosteric regulation of catalytic activity in serine proteases.Histone H4 promotes prothrombin autoactivation.An extensive interaction interface between thrombin and factor V is required for factor V activation.Localization of phosphatidylserine binding sites to structural domains of factor Xa.Allosteric effects potentiating the release of the second fibrinopeptide A from fibrinogen by thrombin.The structural integrity of anion binding exosite I of thrombin is required and sufficient for timely cleavage and activation of factor V and factor VIII.

P2860

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P2860

Identification of residues linked to the slow-->fast transition of thrombin.

http://www.wikidata.org/entity/Q33763127

description

1995 nî lūn-bûn

@nan

1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

Identification of residues linked to the slow-->fast transition of thrombin.

@ast

Identification of residues linked to the slow-->fast transition of thrombin.

@en

type

label

Identification of residues linked to the slow-->fast transition of thrombin.

@ast

Identification of residues linked to the slow-->fast transition of thrombin.

@en

prefLabel

Identification of residues linked to the slow-->fast transition of thrombin.

@ast

Identification of residues linked to the slow-->fast transition of thrombin.

@en

P1433

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P1476

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P2860

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P356

PNAS.92.24.11185

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Identification of residues linked to the slow-->fast transition of thrombin.

@en

P2093

A Vindigni

http://www.w3.org/2001/XMLSchema#string

E Di Cera

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E R Guinto

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Q D Dang

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Y M Ayala

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P2860

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

Refined structure of the hirudin-thrombin complex

Rapid and efficient site-specific mutagenesis without phenotypic selection

An allosteric switch controls the procoagulant and anticoagulant activities of thrombin

The interaction of thrombin with fibrinogen. A structural basis for its specificity.

Glu-192----Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin.

Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin.

Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA.

Alpha-thrombin-catalyzed hydrolysis of fibrin I. Alternative binding modes and the accessibility of the active site in fibrin I-bound alpha-thrombin.

Thrombin is a Na(+)-activated enzyme.

P304

11185-11189

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P31

scholarly article

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10.1073/PNAS.92.24.11185

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24

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P478

92

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1995-11-01T00:00:00Z

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15719063

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7479962

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P932

40596

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