Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops

Journal of Bacteriology

Volumn 185, Issue 14, 2003, Pages 4172-4185

  Roberts, Michael M ^a   Coker, Alun R ^b   Fossati, Gianluca ^c   Mascagni, Paolo ^c   Coates, Anthony R M ^a   Wood, Steve P ^b  

^a ST GEORGE'S UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^c Italfarmaco SpA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN;

ARTICLE; BACTERIAL VIRULENCE; CELL PROLIFERATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; GROWTH INHIBITION; HYDROPHILICITY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OSTEOBLAST; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BONE RESORPTION; CHAPERONIN 10; CRYSTALLOGRAPHY, X-RAY; GROEL PROTEIN; GROES PROTEIN; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SOLUTIONS;

ACTINOBACTERIA (CLASS); BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; UNCULTURED ACTINOMYCETE;

EID: 0037924463     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.14.4172-4185.2003     Document Type: Article

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