Thermostable hexameric form of Eis (Rv2416c) protein of M. tuberculosis plays an important role for enhanced intracellular survival within macrophages

PLoS ONE

Volumn 6, Issue 11, 2011, Pages

  Ganaie, Arsheed A ^a   Lella, Ravi K ^b   Solanki, Rahul ^a   Sharma, Charu ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

^b CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; AMINOGLYCOSIDE; BACTERIAL PROTEIN; GUANIDINE; MONOMER; PROTEIN EIS; UNCLASSIFIED DRUG; UREA; ACETYL COENZYME A; AMINOGLYCOSIDE ACETYLTRANSFERASE; BACTERIAL ANTIGEN; DODECYL SULFATE SODIUM; EIS PROTEIN, MYCOBACTERIUM TUBERCULOSIS;

ARTICLE; BACTERIAL GENE; BACTERIAL SURVIVAL; CONTROLLED STUDY; EIS GENE; ENZYME ACTIVITY; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; INTRACELLULAR SPACE; MACROPHAGE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; THERMOSTABILITY; CHEMISTRY; DRUG EFFECT; GENETICS; METABOLISM; MICROBIAL VIABILITY; MICROBIOLOGY; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; PROTEIN UNFOLDING; SPECTROFLUOROMETRY; TEMPERATURE; TUMOR CELL LINE;

MYCOBACTERIUM TUBERCULOSIS;

ACETYL COENZYME A; ACETYLTRANSFERASES; ANTIGENS, BACTERIAL; BACTERIAL PROTEINS; CELL LINE, TUMOR; GUANIDINE; HUMANS; INTRACELLULAR SPACE; MACROPHAGES; MICROBIAL VIABILITY; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN UNFOLDING; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; UREA;

EID: 81155134455     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027590     Document Type: Article

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