Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase

Science

Volumn 284, Issue 5415, 1999, Pages 805-808

  Rae, T D ^a   Schmidt, P J ^b   Pufahl, R A ^a   Culotta, V C ^b   O'Halloran, T V ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b Johns Hopkins University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; COPPER; METAL; METALLOPROTEIN; SCAVENGER; SUPEROXIDE DISMUTASE;

ARTICLE; BINDING AFFINITY; ENZYME ACTIVATION; ENZYME STABILITY; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PURIFICATION; SACCHAROMYCES CEREVISIAE; YEAST;

APOENZYMES; CHELATING AGENTS; COPPER; CYTOPLASM; ENZYME ACTIVATION; FUNGAL PROTEINS; METALLOTHIONEIN; MOLECULAR CHAPERONES; PHENANTHROLINES; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUPEROXIDE DISMUTASE;

EID: 0033617578     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.284.5415.805     Document Type: Article

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35. We thank D. Hamer for yeast strain 19.3C; J. Valentine for the ySOD1-pET3d plasmid; D. Kosman for yeast SOD1 antibody; I. Klotz, J. Widom, and D. Huffman for advice; and J. Strain, A. Torres, and A. Hermreiter for technical assistance. Supported in part by NIH grants GM 54111 (T.V.O.), GM 50016 (V.C.C.). F32 GM19457 (T.D.R.), and F32 DK09305 (R.A.P.); National Institute of Environmental Health Science training grant ES07141 (P.J.S.); the Johns Hopkins University National Institute for Environmental Health Science Center (V.C.C.); and the Amyotrophic Lateral Sclerosis Association (T.V.O.). T.V.O is a member of the Robert H. Lurie Comprehensive Cancer Center.