Directed evolution of PDZ variants to generate high-affinity detection reagents

Protein Engineering, Design and Selection

Volumn 18, Issue 4, 2005, Pages 165-173

  Ferrer, Marc ^a   Maiolo, Jim ^a   Kratz, Patricia ^a   Jackowski, Jessica L ^b,c   Murphy, Dennis J ^c   Delagrave, Simon ^b,c   Inglese, James ^a,d  

^a MERCK RESEARCH LABORATORIES   (United States)

^b BioTech Studio LLC   (United States)

^c USA Center for Molecular Biotechnology   (United States)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Directed evolution; High affinity detection reagents; PDZ variants

Indexed keywords

ANTIBODIES; BIOASSAY; DISEASE CONTROL; DRUG THERAPY; ENZYME INHIBITION; ENZYME KINETICS;

PROTEASE; PROTEOLYSIS; REAGENTS; THERAPEUTIC PRODUCTS;

ENZYMES;

PDZ PROTEIN; PROTEINASE; REAGENT;

AMINO ACID SUBSTITUTION; ARTICLE; DIRECTED MOLECULAR EVOLUTION; ENZYME ACTIVITY; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN VARIANT; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; DIRECTED MOLECULAR EVOLUTION; DRUG DESIGN; HIV PROTEASE; HIV PROTEASE INHIBITORS; HUMANS; INDICATORS AND REAGENTS; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PEPTIDE LIBRARY; PHOSPHOPROTEINS; PROTEIN STRUCTURE, TERTIARY; RABBITS; SODIUM-HYDROGEN ANTIPORTER;

EID: 18844416595     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzi018     Document Type: Article

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