Assemblies of DegP underlie its dual chaperone and protease function

FEMS Microbiology Letters

Volumn 296, Issue 2, 2009, Pages 143-148

  Subrini, Orso ^a   Betton, Jean Michel ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

Chaperone; Periplasm; Protein degradation; Protein folding; Stress

Indexed keywords

BACTERIAL PROTEIN; CELL PROTEIN; CHAPERONE; DEGP PROTEIN; HEAT SHOCK PROTEIN; HTRA PROTEIN; OLIGOMER; PERIPLASMIC PROTEIN; PROTEINASE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; QUALITY CONTROL; SHORT SURVEY; STRUCTURE ANALYSIS;

ESCHERICHIA COLI;

EID: 67649205489     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2009.01658.x     Document Type: Short Survey

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