A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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Recent estimates of the structure of the factor VIIa (FVIIa)/tissue factor (TF) and factor Xa (FXa) ternary complex.

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Q37692638-AD7DA013-2432-43D1-8009-CE4BC836C874

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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http://www.wikidata.org/entity/Q58211010

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im Dezember 2006 veröffentlichter wissenschaftlicher Artikel

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scientific article published on 11 December 2006

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wetenschappelijk artikel

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наукова стаття, опублікована в грудні 2006

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

@nl

P1476

A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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Hanne B Rasmussen

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Jais R Bjelke

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Ole H Olsen

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

Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells

Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.

Structure, function, and activation of coagulation factor VII.

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

Alteration of the substrate and inhibitor specificities of blood coagulation factor VIIa: importance of amino acid residue K192.

Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin.

Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking.

Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement.

Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA.

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71-76

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scholarly article

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10.1016/J.FEBSLET.2006.11.079

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English

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581

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Birthe B Kragelund

Egon Persson

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2006-12-11T00:00:00Z

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17182039

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A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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P2860

P2860

A loop of coagulation factor VIIa influencing macromolecular substrate specificity

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921