The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa. (Q44258972)

1 December 2017

title

The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa. (English)

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1 December 2017

Aysar Aktimur

1

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1 December 2017

Melanie A Gabriel

series ordinal

2

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1 December 2017

David Gailani

series ordinal

3

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1 December 2017

John R Toomey

series ordinal

4

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1 December 2017

language of work or name

English

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publication date

20 December 2002

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Journal of Biological Chemistry

1 December 2017

published in

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1 December 2017

volume

278

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1 December 2017

issue

10

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1 December 2017

page(s)

7981-7987

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Regulation of coagulation by a multivalent Kunitz-type inhibitor

1 December 2017

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Kinetics of the Factor XIa catalyzed activation of human blood coagulation Factor IX

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Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein

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Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains

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21 January 2018

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Identification of functionally important residues of the epidermal growth factor-2 domain of factor IX by alanine-scanning mutagenesis. Residues Asn(89)-Gly(93) are critical for binding factor VIIIa.

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21 January 2018

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Identification of the endothelial cell binding site for factor IX.

21 January 2018

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The Interaction between the Endothelial Cell Protein C Receptor and Protein C Is Dictated by the γ-Carboxyglutamic Acid Domain of Protein C

21 January 2018

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21 January 2018

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Prothrombin Is a Cofactor for the Binding of Factor XI to the Platelet Surface and for Platelet-Mediated Factor XI Activation by Thrombin

21 January 2018

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3 January 2024

https://opencitations.net/index/api/v1/citations/10.1021/BI972113+

Identifiers

DOI

10.1074/JBC.M212748200

1 reference

1 December 2017

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