Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity (Q74516778)

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11 November 2019

title

Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity (English)

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11 November 2019

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5

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11 November 2019

author name string

J Chang

1

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11 November 2019

J Jin

2

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11 November 2019

P Lollar

3

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11 November 2019

W Bode

4

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11 November 2019

N Hamaguchi

6

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11 November 2019

D L Straight

7

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11 November 2019

D W Stafford

8

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11 November 2019

language of work or name

English

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publication date

1 May 1998

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Journal of Biological Chemistry

11 November 2019

published in

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11 November 2019

volume

273

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11 November 2019

page(s)

12089-12094

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11 November 2019

issue

20

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The coagulation cascade: initiation, maintenance, and regulation

11 November 2019

cites work

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The molecular basis of blood coagulation

21 January 2018

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Redetermination of the rate-limiting step in the activation of factor IX by factor XIa and by factor VIIa/tissue factor. Explanation for different electrophoretic radioactivity profiles obtained on activation of 3H- and 125I-labeled factor IX.

21 January 2018

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Replacement of isoleucine-397 by threonine in the clotting proteinase factor IXa (Los Angeles and Long Beach variants) affects macromolecular catalysis but not L-tosylarginine methyl ester hydrolysis. Lack of correlation between the ox brain prothro

21 January 2018

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X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B

21 January 2018

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Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume and ability to maintain a membrane potential.

21 January 2018

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Characterization of the clotting activities of structurally different forms of activated factor IX. Enzymatic properties of normal human factor IXa alpha, factor IXa beta, and activated factor IX Chapel Hill

21 January 2018

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Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa Is required for its binding to cofactor VIIIa

21 January 2018

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Reactivity of bovine blood coagulation factor IXa beta, factor Xa beta, and factor XIa toward fluorogenic peptides containing the activation site sequences of bovine factor IX and factor X.

21 January 2018

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Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin

21 January 2018

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Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII

21 January 2018

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Molecular mapping of the heparin-binding exosite of thrombin

21 January 2018

1 reference

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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

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.20.12089

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11 November 2019

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