Literature DB >> 12437093

Phage display substrate: a blind method for determining protease specificity.

David Deperthes1.   

Abstract

Phage display substrate enables rapid determination of protease specificity by exposing vast numbers of recombinant peptides to a given protease. Peptides released through specific cleavage are amplified in an expression system. Phage display substrate has been widely exploited and developed further. The number of proteases (from various sources) characterized by this approach testifies to its power. To conserve their advantage over chemical methods, however, phage libraries must be constructed accordingly. The current phenomenal progress in genomics steadily increases the number of protease to be studied. Phage display substrate should prove a powerful method to exploit this wealth of new knowledge.

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Year:  2002        PMID: 12437093     DOI: 10.1515/BC.2002.119

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  14 in total

1.  Protease specificity determination by using cellular libraries of peptide substrates (CLiPS).

Authors:  Kevin T Boulware; Patrick S Daugherty
Journal:  Proc Natl Acad Sci U S A       Date:  2006-05-03       Impact factor: 11.205

2.  Substrate specificity of human kallikreins 1 and 6 determined by phage display.

Authors:  Hai-Xin Li; Bum-Yeol Hwang; Gurunathan Laxmikanthan; Sachiko I Blaber; Michael Blaber; Pavel A Golubkov; Pengyu Ren; Brent L Iverson; George Georgiou
Journal:  Protein Sci       Date:  2008-04       Impact factor: 6.725

Review 3.  New insights into the functional mechanisms and clinical applications of the kallikrein-related peptidase family.

Authors:  Nashmil Emami; Eleftherios P Diamandis
Journal:  Mol Oncol       Date:  2007-09-15       Impact factor: 6.603

Review 4.  Progress in phage display: evolution of the technique and its application.

Authors:  Tomaz Bratkovic
Journal:  Cell Mol Life Sci       Date:  2010-03       Impact factor: 9.261

5.  A bacteriophage-based platform for rapid trace detection of proteases.

Authors:  Petr Capek; Killeen S Kirkconnell; Tobin J Dickerson
Journal:  J Am Chem Soc       Date:  2010-09-29       Impact factor: 15.419

Review 6.  Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases.

Authors:  Franco Faucher; John M Bennett; Matthew Bogyo; Scott Lovell
Journal:  Cell Chem Biol       Date:  2020-07-28       Impact factor: 8.116

7.  Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines.

Authors:  Abeer Jabaiah; Patrick S Daugherty
Journal:  Chem Biol       Date:  2011-03-25

Review 8.  New perspective for phage display as an efficient and versatile technology of functional proteomics.

Authors:  Wei Li; Nora B Caberoy
Journal:  Appl Microbiol Biotechnol       Date:  2009-10-14       Impact factor: 4.813

9.  Factor Xa active site substrate specificity with substrate phage display and computational molecular modeling.

Authors:  Hung-Ju Hsu; Keng-Chang Tsai; Yi-Kun Sun; Hung-Ju Chang; Yi-Jen Huang; Hui-Ming Yu; Chun-Hung Lin; Shi-Shan Mao; An-Suei Yang
Journal:  J Biol Chem       Date:  2008-02-22       Impact factor: 5.157

10.  Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics.

Authors:  Abeer M Jabaiah; Jennifer A Getz; Witold A Witkowski; Jeanne A Hardy; Patrick S Daugherty
Journal:  Biol Chem       Date:  2012-09       Impact factor: 3.915

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