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Volumn 21, Issue 8, 2002, Pages 2045-2053
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The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif
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Author keywords
Affinity cleavage; DNA repair; Endonuclease; Site directed mutagenesis; XPF ERCC1
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Indexed keywords
AMINO ACID;
ARCHAEAL RNA;
ENDONUCLEASE;
RNA HELICASE;
AMINO ACID SEQUENCE;
ARTICLE;
CATALYSIS;
DNA BINDING;
DNA CROSS LINKING;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME SUBSTRATE;
ENZYME SUBUNIT;
EXCISION REPAIR;
GENE LOCUS;
GENETIC CONSERVATION;
HOMOLOGOUS RECOMBINATION;
METAL BINDING;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
POINT MUTATION;
PRIORITY JOURNAL;
PROTEIN FUNCTION;
PROTEIN MOTIF;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
ANIMALS;
BINDING SITES;
CHROMOSOME MAPPING;
CONSERVED SEQUENCE;
DNA REPAIR;
DNA-BINDING PROTEINS;
ENDONUCLEASES;
FERROUS COMPOUNDS;
HUMANS;
METALS;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS;
PROTEINS;
RECOMBINANT FUSION PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
TRANSCRIPTION FACTORS;
ARCHAEA;
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EID: 0037090816
PISSN: 02614189
EISSN: None
Source Type: Journal
DOI: 10.1093/emboj/21.8.2045 Document Type: Article |
Times cited : (165)
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References (55)
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