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Volumn 44, Issue 5, 2001, Pages 271-282
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Amino acid substitution analyses of the DNA contact region, two amphipathic α-helices and a recognition-helix-like helix outside the dimeric β-barrel of Epstein-Barr virus nuclear antigen 1
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Author keywords
Dimerization DNA binding domain; EBNA 1; EBV; Point mutation; Recognition helix; Sequence homology to papilloma virus E2
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Indexed keywords
AMINO ACID;
CELL NUCLEUS ANTIGEN;
VIRUS PROTEIN;
ALPHA HELIX;
AMINO ACID ANALYSIS;
AMINO ACID SUBSTITUTION;
ARTICLE;
CONTROLLED STUDY;
DIMERIZATION;
DNA BINDING;
ELECTRICITY;
EPSTEIN BARR VIRUS;
LATENT PERIOD;
MOLECULAR RECOGNITION;
NONHUMAN;
PAPILLOMA VIRUS;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
REDUCTION;
VIRUS MUTATION;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
CONSERVED SEQUENCE;
DIMERIZATION;
DNA, VIRAL;
DNA-BINDING PROTEINS;
ELECTROSTATICS;
EPSTEIN-BARR VIRUS NUCLEAR ANTIGENS;
GLYCINE;
HERPESVIRUS 4, HUMAN;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
POINT MUTATION;
PROTEIN BINDING;
PROTEIN STRUCTURE, SECONDARY;
RECOMBINANT FUSION PROTEINS;
REPLICATION ORIGIN;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
STRUCTURE-ACTIVITY RELATIONSHIP;
HUMAN HERPESVIRUS 4;
PAPILLOMAVIRUS;
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EID: 0035742902
PISSN: 03005526
EISSN: None
Source Type: Journal
DOI: 10.1159/000050058 Document Type: Article |
Times cited : (7)
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References (52)
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