Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis

Biochemical Journal

Volumn 418, Issue 2, 2009, Pages 369-378

  Lack, Nathan A ^a   Kawamura, Akane ^b   Fullam, Elizabeth ^a   Laurieri, Nicola ^a   Beard, Stacey ^a   Russell, Angela J ^a   Evangelopoulos, Dimitrios ^a,c   Westwood, Isaac ^a   Sim, Edith ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b SUMMIT PLC   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

2 hydroxy 6 oxo 6 phenylhexa 2,4 dienoic acid hydrolase (HsaD); Arylamine N acetyltransferase (NAT); Cholesterol; Heat stability; Mycobacterium tuberculosis; Survival

Indexed keywords

2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACID HYDROLASE (HSAD); ARYLAMINE N-ACETYLTRANSFERASE (NAT); HEAT STABILITY; MYCOBACTERIUM TUBERCULOSIS; SURVIVAL;

ACIDS; CHOLESTEROL; GENES; METABOLISM; PROTEINS;

STABILITY;

2 HYDROXY 6 OXO 6 PHENYLHEXA 2,4 DIENOIC ACID HYDROLASE; ACID HYDROLASE; ACYL COENZYME A; ARYLAMINE ACETYLTRANSFERASE; HYDRALAZINE; PROPIONYL COENZYME A; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CHOLESTEROL; COENZYME A; HSAD PROTEIN, MYCOBACTERIUM TUBERCULOSIS; HYDROLASE; RECOMBINANT PROTEIN;

ARTICLE; BACTERIAL SURVIVAL; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; BIOLOGICAL MODEL; CHEMISTRY; GENETICS; INTRACELLULAR SPACE; ISOLATION AND PURIFICATION; METABOLISM; MICROBIAL VIABILITY; PHYSIOLOGY; PROTEIN PROCESSING; PROTEIN STABILITY; TEMPERATURE;

MYCOBACTERIUM TUBERCULOSIS;

ARYLAMINE N-ACETYLTRANSFERASE; BACTERIAL PROTEINS; CHOLESTEROL; COENZYME A; HYDROLASES; INTRACELLULAR SPACE; METABOLIC NETWORKS AND PATHWAYS; MICROBIAL VIABILITY; MODELS, BIOLOGICAL; MYCOBACTERIUM TUBERCULOSIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; RECOMBINANT PROTEINS; TEMPERATURE;

EID: 61449103732     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20082011     Document Type: Article

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