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Volumn 281, Issue 28, 2006, Pages 19273-19279
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Engineering of a single conserved amino acid residue of herpes simplex virus type 1 thymidine kinase allows a predominant shift from pyrimidine to purine nucleoside phosphorylation
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Author keywords
[No Author keywords available]
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Indexed keywords
CRYSTAL STRUCTURE;
ENZYMES;
LIGAMENTS;
MUTAGENESIS;
SUBSTRATES;
VIRUSES;
AMINO ACID MUTATION;
KINASE ACTIVITY;
PYRIMIDINE NUCLEOSIDE ANALOGUE BINDING;
THYMIDINE (DTHD) KINASE (TK);
AMINO ACIDS;
ALANINE;
GANCICLOVIR;
MUTANT PROTEIN;
NITROGEN;
NUCLEOSIDE ANALOG;
PHENYLALANINE;
PURINE;
PYRIMIDINE;
THYMIDINE KINASE;
THYMIDINE TRIPHOSPHATE;
TYROSINE;
ARTICLE;
CATALYSIS;
CHEMICAL STRUCTURE;
CRYSTAL STRUCTURE;
HERPES SIMPLEX VIRUS 1;
KINETICS;
MUTATION;
NEGATIVE FEEDBACK;
NUCLEOTIDE SEQUENCE;
PHOSPHORYLATION;
PRIORITY JOURNAL;
PROTEIN ENGINEERING;
SITE DIRECTED MUTAGENESIS;
STEREOSPECIFICITY;
ANTIVIRAL AGENTS;
BINDING SITES;
HERPESVIRUS 1, HUMAN;
KINETICS;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PHOSPHORYLATION;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
PURINE NUCLEOSIDES;
PYRIMIDINE NUCLEOSIDES;
THYMIDINE KINASE;
HUMAN HERPESVIRUS 1;
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EID: 33745834321
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M600414200 Document Type: Article |
Times cited : (31)
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References (16)
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