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The extended cleavage specificity of human thrombin

The extended cleavage specificity of human thrombin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1333202226

The extended cleavage specificity of human thrombin

About this item

Full title

The extended cleavage specificity of human thrombin

Publisher

United States: Public Library of Science

Journal title

PloS one, 2012-02, Vol.7 (2), p.e31756-e31756

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

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 recognition profile using phage-display technology....

Alternative Titles

Full title

The extended cleavage specificity of human thrombin

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1333202226

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1333202226

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0031756

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