Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 18336-18345

  Banumathy, Gowrishankar ^a   Singh, Varsha ^a   Pavithra, Soundara Raghavan ^a   Tatu, Utpal ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELL CULTURE; GENETIC ENGINEERING; OLIGOMERS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY;

PARASITES; TRANSCRIPTION ACTIVITIES;

GROWTH KINETICS;

GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; OLIGOMER; PROTEIN KINASE; TRANSCRIPTION FACTOR; BENZOQUINONE DERIVATIVE; CYSTEINE PROTEINASE INHIBITOR; ENZYME INHIBITOR; MACROCYCLIC LACTAM; QUINONE DERIVATIVE; SUCROSE;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ERYTHROCYTE; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MALARIA; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; SCHIZONT; SEDIMENTATION; TROPHOZOITE; TWO DIMENSIONAL GEL ELECTROPHORESIS; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; GEL CHROMATOGRAPHY; HEAT; METABOLISM; MOLECULAR GENETICS; PARASITOLOGY; PHOSPHORYLATION; PHYSIOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SERODIAGNOSIS; TIME;

EUKARYOTA; MAMMALIA; PLASMODIUM FALCIPARUM; PROTOZOA;

AMINO ACID SEQUENCE; ANIMALS; BENZOQUINONES; BINDING SITES; CHROMATOGRAPHY, GEL; CYSTEINE PROTEINASE INHIBITORS; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; ERYTHROCYTES; HEAT; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LACTAMS, MACROCYCLIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PLASMODIUM FALCIPARUM; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; QUINONES; SEQUENCE HOMOLOGY, AMINO ACID; SUCROSE; TIME FACTORS;

EID: 0038381514     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211309200     Document Type: Article

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