Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state

FASEB Journal

Volumn 30, Issue 1, 2016, Pages 405-416

  Olshina, Maya A ^a   Baumann, Hella ^b   Willison, Keith R ^b   Baum, Jake ^b  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Apicomplexa; Gliding motility; In vitro translation; Malaria; Rabbit reticulocyte lysate

Indexed keywords

ACTIN; BETA ACTIN; CHAPERONIN CONTAINING TCP1; G ACTIN; PLASMODIUM FALCIPARUM ACTIN 1; PROTOZOAL DNA; PROTOZOAL PROTEIN; PROTOZOAL RNA; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; CHAPERONIN;

ACTIN POLYMERIZATION; ANIMAL CELL; ARTICLE; AUTORADIOGRAPHY; CELL LYSATE; COMPUTER MODEL; CONTROLLED STUDY; DENSITOMETRY; DNA TEMPLATE; EUKARYOTIC CELL; GENE EXPRESSION SYSTEM; GENETIC VARIABILITY; HETEROLOGOUS EXPRESSION; HUMAN; IN VITRO STUDY; KINETICS; NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROKARYOTIC CELL; PROTEIN EXPRESSION; PROTEIN FOLDING; QUANTITATIVE ANALYSIS; RABBIT; RETICULOCYTE; RNA TRANSCRIPTION; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; CHEMISTRY; METABOLISM;

ACTINS; CHAPERONINS; PLASMODIUM FALCIPARUM; PROTEIN FOLDING; PROTOZOAN PROTEINS;

EID: 84974831770     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.15-276618     Document Type: Article

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