Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

Nature Structural and Molecular Biology

Volumn 18, Issue 3, 2011, Pages 262-269

  Quan, Shu ^a,b   Koldewey, Philipp ^a,b   Tapley, Tim ^a,b   Kirsch, Nadine ^a,b   Ruane, Karen M ^c   Pfizenmaier, Jennifer ^a,b   Shi, Rong ^c   Hofmann, Stephan ^a,b   Foit, Linda ^a,b   Ren, Guoping ^a,b   Jakob, Ursula ^b   Xu, Zhaohui ^b,d   Cygler, Miroslaw ^c,e   Bardwell, James C A ^a,b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c MCGILL UNIVERSITY   (Canada)

^d UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^e NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PERIPLASMIC PROTEIN; PROTEIN CPXP; PROTEIN IM7; PROTEIN SPY; TANNIN; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; ESCHERICHIA COLI; GENETIC SELECTION; IN VITRO STUDY; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PERIPLASMIC PROTEINS; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; TANNINS; UP-REGULATION;

ESCHERICHIA COLI;

EID: 79952363991     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2016     Document Type: Article

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