An in silico and in vitro approach to elucidate the impact of residues flanking the cleavage scissile bonds of FVIII.

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An in silico and in vitro approach to elucidate the impact of residues flanking the cleavage scissile bonds of FVIII.

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2017 nî lūn-bûn

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2017年論文

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An in silico and in vitro appr ...... avage scissile bonds of FVIII.

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An in silico and in vitro appr ...... avage scissile bonds of FVIII.

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An in silico and in vitro appr ...... avage scissile bonds of FVIII.

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P1476

An in silico and in vitro appr ...... eavage scissile bonds of FVIII

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P2093

Ann-Cristin Berkemeier

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Anna Pavlova

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Jens Müller

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Johannes Oldenburg

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Julia Driesen

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Ursula Schreck

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P2860

Interaction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complex

Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field

Cofactor proteins in the assembly and expression of blood clotting enzyme complexes

Exosite-driven substrate specificity and function in coagulation

In situ-generated thrombin is the only enzyme that effectively activates factor VIII and factor V in thromboplastin-activated plasma

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

YASARA View - molecular graphics for all devices - from smartphones to workstations.

Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin.

A strategy to profile prime and non-prime proteolytic substrate specificity.

The Importance of Exosite Interactions for Substrate Cleavage by Human Thrombin.

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e0180456

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scholarly article

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10.1371/JOURNAL.PONE.0180456

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English

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P478

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Arijit Biswas

B Pezeshkpoor

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2017-07-06T00:00:00Z

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28683085

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5500338

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