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Volumn 101, Issue 9, 2004, Pages 2712-2717
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The solution structure of the N-terminal domain of E3L shows a tyrosine confirmation that may explain its reduce affinity to Z-DNA in vitro
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Author keywords
[No Author keywords available]
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Indexed keywords
CARBON 13;
DNA Z;
NITROGEN 15;
UNCLASSIFIED DRUG;
VIRUS PROTEIN;
VIRUS PROTEIN E3L;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING AFFINITY;
DNA BINDING;
DNA VIRUS;
ISOTOPE LABELING;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
POXVIRUS;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
STRUCTURE ANALYSIS;
VACCINIA VIRUS;
VIRUS GENE;
VIRUS GENE E3L;
VIRUS PATHOGENESIS;
AMINO ACID SEQUENCE;
BINDING SITES;
DNA, Z-FORM;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
NUCLEIC ACID CONFORMATION;
PROTEIN CONFORMATION;
RNA-BINDING PROTEINS;
SOLUTIONS;
TYROSINE;
VIRAL PROTEINS;
DNA VIRUSES;
POXVIRIDAE;
VACCINIA;
VACCINIA VIRUS;
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EID: 1542267839
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.0308612100 Document Type: Article |
Times cited : (48)
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References (17)
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