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Volumn 92, Issue 2, 2001, Pages 81-87
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ADP-ribosyltransferases: Plastic tools for inactivating protein and small molecular weight targets
a b a b |
Author keywords
ADP ribosylation; Amino acid sequence alignment; Bacterial toxins; Protein design; Sequence homology; Structure prediction
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Indexed keywords
CATALYSIS;
CRYSTALLIZATION;
ENZYMES;
TOXIC MATERIALS;
METABOLIC REGULATORS;
BIOTECHNOLOGY;
BACTERIAL TOXIN;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;
AMINO ACID SEQUENCE;
CATALYSIS;
CONFERENCE PAPER;
CRYSTALLIZATION;
DISULFIDE BOND;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME INACTIVATION;
ENZYME MECHANISM;
ENZYME METABOLISM;
ENZYME REGULATION;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
LIGAND BINDING;
MOLECULAR WEIGHT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN DOMAIN;
PROTEIN FOLDING;
REDUCTION;
SEQUENCE HOMOLOGY;
AMINO ACID SEQUENCE;
ANIMALS;
BIOTECHNOLOGY;
DRUG DESIGN;
HUMANS;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
POLY(ADP-RIBOSE) POLYMERASES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
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EID: 0035909796
PISSN: 01681656
EISSN: None
Source Type: Journal
DOI: 10.1016/S0168-1656(01)00356-X Document Type: Review |
Times cited : (27)
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References (34)
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