Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.

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Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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Stabilizing interactions betwe ...... in the blood clotting pathway.

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P1476

Stabilizing interactions betwe ...... in the blood clotting pathway.

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P2093

A E Griffiths

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H Wakabayashi

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M Monaghan

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P J Fay

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P2860

The tertiary structure and domain organization of coagulation factor VIII

Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex

Calibrated automated thrombin generation measurement in clotting plasma

Molecular cloning of a cDNA encoding human antihaemophilic factor

Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity

Structure of human factor VIII

Activation of factor VIII by thrombin increases its affinity for binding to synthetic phospholipid membranes and activated platelets

Cofactor activity in factor VIIIa of the blood clotting pathway is stabilized by an interdomain bond between His281 and Ser524 formed in factor VIII.

Search for allosteric disulfide bonds in NMR structures.

Activation of factor VIII and mechanisms of cofactor action.

P304

1021-1030

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scholarly article

P356

10.1111/JTH.13292

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P478

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2016-02-15T00:00:00Z

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26878264

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4870127

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