A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo

Molecular Microbiology

Volumn 54, Issue 4, 2004, Pages 1036-1050

  Parent, Kristin N ^a   Ranaghan, Matthew J ^a   Teschke, Carolyn M ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN; COAT PROTEIN; MEMBRANE PROTEIN; P22 SCAFFOLDING PROTEIN; PROTEIN SU; TEMPERATURE SENSITIVE FOLDING COAT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE P22; CELL LABELING; COMPLEX FORMATION; IN VIVO STUDY; ISOTOPE LABELING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DEFECT; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN VARIANT; TEMPERATURE SENSITIVITY;

AMINO ACID SUBSTITUTION; BACTERIOPHAGE P22; CAPSID PROTEINS; GROEL PROTEIN; GROES PROTEIN; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN FOLDING; SALMONELLA TYPHIMURIUM; TEMPERATURE;

BACTERIA (MICROORGANISMS);

EID: 8544283776     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04326.x     Document Type: Article

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