Aptamer-mediated inhibition of mycobacterium tuberculosis polyphosphate kinase 2

Biochemistry

Volumn 50, Issue 15, 2011, Pages 3261-3271

  Shum, Ka To ^a   Lui, Eric Lik Hang ^a   Wong, Sybil Cheuk Ki ^a   Yeung, Pok ^a   Sam, Laiju ^a   Wang, Ying ^b   Watt, Rory M ^b   Tanner, Julian A ^a  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

APTAMERS; CATALYTIC ACTIVITY; CIRCULAR DICHROISM; DEPENDENT PROCESS; DISSOCIATION CONSTANT; DNA APTAMERS; G-QUADRUPLEXES; GEL-FILTRATION CHROMATOGRAPHY; INHIBITION KINETICS; INORGANIC POLYPHOSPHATE; INTRACELLULAR METABOLISM; ISOTHERMAL TITRATION CALORIMETRY; MECHANISTIC ANALYSIS; MYCOBACTERIUM TUBERCULOSIS; OCTAMERS; PATHOGENIC ORGANISMS; POLYPHOSPHATES; PROTEIN FAMILY; SECONDARY STRUCTURES; VIBRIO CHOLERAE;

CATALYST ACTIVITY; DICHROISM; DISSOCIATION; ENZYMES; GEL PERMEATION CHROMATOGRAPHY; NUCLEIC ACIDS; PHOSPHORYLATION;

ENZYME INHIBITION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; APTAMER; DNA; GUANINE QUADRUPLEX; OCTAMER TRANSCRIPTION FACTOR; POLYPHOSPHATE; POLYPHOSPHATE KINASE 2; PROTEIN KINASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERIUM ISOLATE; BINDING AFFINITY; CATALYSIS; CHEMICAL ANALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENTROPY; ENZYME ACTIVITY; ENZYME INHIBITION; GEL FILTRATION CHROMATOGRAPHY; IC 50; ISOTHERMAL TITRATION CALORIMETRY; MEDIATOR; MUTATIONAL ANALYSIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; VIBRIO CHOLERAE;

APTAMERS, NUCLEOTIDE; BASE SEQUENCE; CLONING, MOLECULAR; ENZYME INHIBITORS; G-QUADRUPLEXES; KINETICS; MODELS, MOLECULAR; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PHOSPHOTRANSFERASES (PHOSPHATE GROUP ACCEPTOR); PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); LARIBACTER HONGKONGENSIS; MYCOBACTERIUM TUBERCULOSIS; VIBRIO CHOLERAE;

EID: 79953866877     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2001455     Document Type: Article

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