Secretory nucleoside diphosphate kinases from both intra- and extracellular pathogenic bacteria are functionally indistinguishable

Microbiology

Volumn 157, Issue 11, 2011, Pages 3024-3035

  Dar, Haider Hussain ^a   Prasad, Deepshikha ^a   Varshney, Grish C ^a   Chakraborti, Pradip K ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; LACTATE DEHYDROGENASE; NUCLEOSIDE DIPHOSPHATE KINASE; PHOSPHOTRANSFERASE;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; CYTOLYSIS; CYTOTOXICITY; ENZYME ACTIVITY; ENZYME RELEASE; MACROPHAGE; MOUSE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SALMONELLA TYPHIMURIUM; VIBRIO CHOLERAE;

ADENOSINE TRIPHOSPHATE; ANIMALS; BACTERIAL PROTEINS; CELL DEATH; CELL LINE; GENE KNOCKOUT TECHNIQUES; L-LACTATE DEHYDROGENASE; MACROPHAGES; MICE; MYCOBACTERIUM TUBERCULOSIS; NUCLEOSIDE-DIPHOSPHATE KINASE; PHOSPHORYLATION; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; VIBRIO CHOLERAE;

MYCOBACTERIUM TUBERCULOSIS; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM; VIBRIO CHOLERAE;

EID: 80155200967     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.049221-0     Document Type: Article

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