The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains

Proceedings of the National Academy of Sciences of the United States of America

Volumn 95, Issue 26, 1998, Pages 15253-15258

  Lopez Buesa, Pascual ^a,b   Pfund, Christine ^a   Craig, Elizabeth A ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

^b UNIVERSIDAD DE ZARAGOZA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 70; HYBRID PROTEIN; PROTEIN DNAK;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BINDING SITES; CYTOSOL; FUNGAL PROTEINS; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE;

EID: 0032417527     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.95.26.15253     Document Type: Article

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