Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa (Q45858909)

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scientific article published in June 1999

Language	Label	Description	Also known as
English	Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa	scientific article published in June 1999

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scholarly article

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa (English)

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

author name string

Mathur A

1

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

Bajaj SP

2

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Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

language of work or name

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publication date

1 June 1999

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Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

number of pages

10

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Journal of Biological Chemistry

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Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

274

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Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

26

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Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

18477-18486

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

The coagulation cascade: initiation, maintenance, and regulation

1 reference

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

1 reference

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Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species

1 reference

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The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor

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The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions

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Antibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domain

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Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX

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First epidermal growth factor-like domain of human blood coagulation factor IX is required for its activation by factor VIIa/tissue factor but not by factor XIa.

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21 January 2018

Ca2+ binding to the first epidermal growth factor-like domain of human blood coagulation factor IX promotes enzyme activity and factor VIII light chain binding.

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The role of the second growth-factor domain of human factor IXa in binding to platelets and in factor-X activation

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Haemophilia B: database of point mutations and short additions and deletions--eighth edition

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

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Nucleotide sequence of the gene for human factor IX (antihemophilic factor B)

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A general method of site-specific mutagenesis using a modification of the Thermus aquaticus polymerase chain reaction

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Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation

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DNA sequencing with chain-terminating inhibitors

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The A2 subunit of factor VIIIa modulates the active site of factor IXa.

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32 Concentrations of binding protein and labeled analyte that are appropriate for measuring at any analyte concentration range in radioimmunoassays

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Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

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Characterization of three abnormal factor IX variants (Bm Lake Elsinore, Long Beach, and Los Angeles) of hemophilia-B. Evidence for defects affecting the latent catalytic site

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21 January 2018

Replacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B.

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21 January 2018

Blood coagulation factor IX residues Glu78 and Arg94 provide a link between both epidermal growth factor-like domains that is crucial in the interaction with factor VIII light chain

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21 January 2018

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

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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

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Interaction of calcium with native and decarboxylated human factor X. Effect of proteolysis in the autolysis loop on catalytic efficiency and factor Va binding

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Localization of factor IXa and factor VIIIa interactive sites

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Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X

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High affinity Ca(2+)-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity

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The activation of bovine factor X by bovine factor Xa

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

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21 January 2018

Identifiers

10.1074/JBC.274.26.18477

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

1 reference

Europe PubMed Central

17 December 2017

http://europepmc.org/abstract/MED/10373456

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