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Volumn 273, Issue 48, 1999, Pages 31867-31872
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Functional consequences of mutations of conserved, polar amino acids in transmembrane sequences of the Ca2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum
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Author keywords
[No Author keywords available]
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Indexed keywords
CAFFEINE;
CALCIUM CHANNEL;
META CRESOL;
RYANODINE RECEPTOR;
AMINO ACID ANALYSIS;
AMINO ACID SEQUENCE;
ANIMAL CELL;
ANIMAL TISSUE;
ARTICLE;
BINDING AFFINITY;
CALCIUM TRANSPORT;
ENZYME LINKED IMMUNOSORBENT ASSAY;
GENE CONTROL;
GENE EXPRESSION;
GENE MUTATION;
IMMUNOBLOTTING;
MUTAGENESIS;
NONHUMAN;
PRIORITY JOURNAL;
RABBIT;
SARCOPLASMIC RETICULUM;
SKELETAL MUSCLE;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ANIMALS;
CAFFEINE;
CALCIUM;
CELL LINE;
CONSERVED SEQUENCE;
CRESOLS;
HUMANS;
KINETICS;
MACROMOLECULAR SUBSTANCES;
MOLECULAR SEQUENCE DATA;
MUSCLE, SKELETAL;
MUTAGENESIS, SITE-DIRECTED;
POINT MUTATION;
RABBITS;
RECOMBINANT PROTEINS;
RYANODINE;
RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
TRANSFECTION;
VALINE;
ANIMALIA;
ORYCTOLAGUS CUNICULUS;
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EID: 0001531535
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.273.48.31867 Document Type: Article |
Times cited : (54)
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References (21)
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