Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa (Q43509911)

24 November 2017

title

Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa (English)

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24 November 2017

Petrovan RJ

1

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24 November 2017

Ruf W

series ordinal

2

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24 November 2017

language of work or name

English

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publication date

14 November 2000

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Journal of Biological Chemistry

24 November 2017

published in

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24 November 2017

volume

276

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24 November 2017

issue

9

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24 November 2017

page(s)

6616-6620

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Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa.

24 November 2017

cites work

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21 January 2018

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Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa

21 January 2018

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21 January 2018

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Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage

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Factor VIIa residue Arg290 is required for efficient activation of the macromolecular substrate factor X.

21 January 2018

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Two sites in the tissue factor extracellular domain mediate the recognition of the ligand factor VIIa

21 January 2018

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Regulation of the catalytic function of coagulation factor VIIa by a conformational linkage of surface residue Glu 154 to the active site

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Active Site Modification of Factor VIIa Affects Interactions of the Protease Domain with Tissue Factor

21 January 2018

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Thermal effects on an enzymatically latent conformation of coagulation factor VIIa

21 January 2018

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Role of residue Phe225 in the cofactor-mediated, allosteric regulation of the serine protease coagulation factor VIIa

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M004726200

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24 November 2017

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