Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins

Journal of Molecular Biology

Volumn 342, Issue 2, 2004, Pages 605-617

  Qamra, Rohini ^a   Srinivas, Volety ^b   Mande, Shekhar C ^a  

^a Ctr DNA Fingerprinting Diagnostics   (India)

^b CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

aggregation; chaperonin; M. tuberculosis; oligomer; protein folding

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; BACTERIAL VIRULENCE; GENE DUPLICATION; GENE MUTATION; HETEROZYGOTE; HYPOTHESIS; INHIBITION KINETICS; MOLECULAR BIOLOGY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OLIGOMERIZATION; OPERON; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; REGULATORY MECHANISM; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 4344587654     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.066     Document Type: Article

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