Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities-Reference-Cited by-同舟云学术

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Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities

Published:2006-05 Issue:18 Volume:281 Page:12824-12832
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Choe Youngchool,Leonetti Francesco,Greenbaum Doron C.,Lecaille Fabien,Bogyo Matthew,Brömme Dieter,Ellman Jonathan A.,Craik Charles S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. MEROPS: the peptidase database

2. Papa's got a brand new tag: advances in identification of proteases and their substrates

3. A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B

4. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries

5. Cellular Localization of Membrane-type Serine Protease 1 and Identification of Protease-activated Receptor-2 and Single-chain Urokinase-type Plasminogen Activator as Substrates

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