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Volumn 276, Issue 3, 2001, Pages 2234-2242
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The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINE TRIPHOSPHATASE;
ADENOSINE TRIPHOSPHATE;
ADENOSINE TRIPHOSPHATE DERIVATIVE;
COPPER ION;
PROTEIN SUBUNIT;
UNCLASSIFIED DRUG;
WILSON DISEASE PROTEIN;
ADENOSINE PHOSPHATE;
CARRIER PROTEIN;
CATION TRANSPORT PROTEIN;
COPPER;
LYSINE;
PRIMER DNA;
RECOMBINANT PROTEIN;
AMINO ACID SEQUENCE;
ARTICLE;
BINDING SITE;
CONFORMATIONAL TRANSITION;
CONTROLLED STUDY;
GENE MUTATION;
HYDROLYSIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTEIN PROTEIN INTERACTION;
WILSON DISEASE;
CHEMISTRY;
METABOLISM;
MOLECULAR GENETICS;
NUCLEOTIDE SEQUENCE;
PROTEIN BINDING;
SEQUENCE HOMOLOGY;
SPECTROFLUOROMETRY;
ADENOSINE MONOPHOSPHATE;
ADENOSINE TRIPHOSPHATASES;
ADENOSINE TRIPHOSPHATE;
AMINO ACID SEQUENCE;
BASE SEQUENCE;
CARRIER PROTEINS;
CATION TRANSPORT PROTEINS;
COPPER;
DNA PRIMERS;
LYSINE;
MOLECULAR SEQUENCE DATA;
PROTEIN BINDING;
RECOMBINANT PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
SPECTROMETRY, FLUORESCENCE;
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EID: 0035910261
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M003238200 Document Type: Article |
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Times cited : (138)
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References (41)
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