The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity

FEBS Journal

Volumn 283, Issue 7, 2016, Pages 1286-1299

  Vashist, Atul ^a,b   Prithvi Raj, D ^a   Gupta, Umesh Datta ^b   Bhat, Rajiv ^c   Tyagi, Jaya Sivaswami ^a  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

^b NATIONAL JALMA INSTITUTE OF LEPROSY AND OTHER MYCOBACTERIAL DISEASES   (India)

^c JAWAHARLAL NEHRU UNIVERSITY   (India)

Author keywords

biophysical characterization; DevR DosR; dormancy regulon; M. tuberculosis; signal transduction

Indexed keywords

DEVR PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG; BACTERIAL DNA; BACTERIAL PROTEIN; DOSR PROTEIN, MYCOBACTERIUM TUBERCULOSIS; PROTEIN BINDING; PROTEIN KINASE;

ALPHA HELIX; ARTICLE; AUTOREGULATION; BACTERIAL STRAIN; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYPOXIA; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REGULON; ANAEROBIC GROWTH; CHEMISTRY; CIRCULAR DICHROISM; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MUTATION; PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; WESTERN BLOTTING;

ANAEROBIOSIS; BACTERIAL PROTEINS; BLOTTING, WESTERN; CIRCULAR DICHROISM; DNA, BACTERIAL; GENE EXPRESSION REGULATION, BACTERIAL; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE;

EID: 84975686870     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13664     Document Type: Article

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