The activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain

mBio

Volumn 4, Issue 4, 2013, Pages

  Ricci, Dante P ^a,b   Schwalm, Jaclyn ^a   Gonzales Cope, Michelle ^a   Silhavy, Thomas J ^a  

^a PRINCETON UNIVERSITY   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHAPERONE; OUTER MEMBRANE PROTEIN; PEPTIDYLPROLYL ISOMERASE PIN1; PEPTIDYLPROLYL ISOMERASE PIN2; PROTEIN BAMA616; PROTEIN BAMB8; PROTEIN SURA; PROTEIN SURA10; PROTEIN SURA13; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BAMA616 GENE; BAMB8 GENE; BIOGENESIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GAIN OF FUNCTION MUTATION; GENE MUTATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROLINE ISOMERASE DOMAIN; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; SURA GENE; SURA10 GENE; SURA13 GENE; TRANSLATION REGULATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA; SALMONELLA; SHIGELLA;

EID: 84883435364     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00540-13     Document Type: Article

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