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Volumn 123, Issue 48, 2001, Pages 11960-11969
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Diphtheria toxin catalyzed hydrolysis of NAD+: Molecular dynamics study of enzyme-bound substrate, transition state, and inhibitor
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Author keywords
[No Author keywords available]
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Indexed keywords
CONFORMATIONAL STRESS;
ACTIVATION ENERGY;
CRYSTAL STRUCTURE;
ENZYME INHIBITION;
HYDROGEN BONDS;
HYDROLYSIS;
ISOMERIZATION;
MOLECULAR DYNAMICS;
PROTEINS;
SUBSTRATES;
BIOCATALYSTS;
AMIDE;
CARBONYL DERIVATIVE;
CARBOXYLIC ACID DERIVATIVE;
DIPHTHERIA TOXIN;
ENZYME;
ENZYME INHIBITOR;
GLUTAMIC ACID;
HYDROXYL GROUP;
NICOTINAMIDE;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
RIBOSE;
ARTICLE;
CALCULATION;
CATALYSIS;
CHEMICAL BOND;
CHEMICAL REACTION KINETICS;
CONFORMATIONAL TRANSITION;
ENERGY;
ENZYME ACTIVE SITE;
ENZYME INHIBITOR COMPLEX;
ENZYME SUBSTRATE COMPLEX;
HYDROLYSIS;
MOLECULAR DYNAMICS;
MOLECULAR STABILITY;
QUANTUM CHEMISTRY;
REACTION ANALYSIS;
TIME;
TRANS ISOMER;
CATALYSIS;
DIPHTHERIA TOXIN;
HYDROLYSIS;
KINETICS;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
NAD;
NAD+ NUCLEOSIDASE;
OLIGORIBONUCLEOTIDES;
PROTEIN CONFORMATION;
QUANTUM THEORY;
THERMODYNAMICS;
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EID: 0035814372
PISSN: 00027863
EISSN: None
Source Type: Journal
DOI: 10.1021/ja0113807 Document Type: Article |
Times cited : (10)
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References (44)
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