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Volumn 277, Issue 31, 2002, Pages 27953-27959
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Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINETRIPHOSPHATE;
CATALYST ACTIVITY;
CELLS;
COPPER;
BINDING SITES;
BIOCHEMISTRY;
ADENOSINE TRIPHOSPHATASE;
ATOX1 PROTEIN;
CHAPERONE;
COMPLEMENTARY DNA;
COPPER;
HYBRID PROTEIN;
METALLOPROTEIN;
UNCLASSIFIED DRUG;
WILSON DISEASE PROTEIN;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING SITE;
CATALYSIS;
COPPER METABOLISM;
DOWN REGULATION;
GENE EXPRESSION;
HUMAN;
METAL BINDING;
MOLECULAR CLONING;
PRIORITY JOURNAL;
PROTEIN PROTEIN INTERACTION;
PROTEIN PURIFICATION;
WILSON DISEASE;
ADENOSINE TRIPHOSPHATASES;
APOPROTEINS;
BINDING SITES;
CATALYSIS;
CATION TRANSPORT PROTEINS;
CLONING, MOLECULAR;
COPPER;
HEPATOLENTICULAR DEGENERATION;
HUMANS;
KINETICS;
LIVER;
MOLECULAR CHAPERONES;
MUTATION;
RECOMBINANT FUSION PROTEINS;
RECOMBINANT PROTEINS;
MAMMALIA;
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EID: 0037008692
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M203845200 Document Type: Article |
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Times cited : (149)
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References (22)
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