The extended cleavage specificity of human thrombin

Thrombin is one of the most extensively studied of all proteases. Its central role in the coagulation cascade as well as several other areas has been thoroughly documented. Despite this, its consensus cleavage site has never been determined in detail. Here we have determined its extended substrate r...

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Veröffentlicht in:	PloS one 2012-02, Vol.7 (2), p.e31756-e31756
Hauptverfasser:	Gallwitz, Maike, Enoksson, Mattias, Thorpe, Michael, Hellman, Lars
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Sequence Amino acids Analysis Arginine Aspartic acid Binding Sites Biology Cleavage Coagulation Computational Biology - methods Conserved sequence Display devices Enzymes Escherichia coli - metabolism Humans Insertion Ischemia Kinases Kinetics Medicine Molecular Sequence Data Mutation Peptide Library Peptides Phages Proline Proteases Protein Conformation Protein Structure, Tertiary Proteins Recognition Recombinant Proteins - chemistry Sensitivity and Specificity Sequence Homology, Amino Acid Sequences Substrate Specificity Substrates Thioredoxin Thioredoxins - chemistry Thrombin Thrombin - chemistry Thrombin - genetics Thrombin - physiology Traumatic brain injury
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