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Volumn 286, Issue 26, 2011, Pages 23054-23062
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Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency
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Author keywords
[No Author keywords available]
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Indexed keywords
ACHILLES' HEEL;
ADENYLYLATION;
DNA LIGASES;
DNA LIGATION;
DNA REPLICATIONS;
GENOMIC STABILITY;
ION-DEPENDENCE;
KINETIC MECHANISM;
MAMMALIAN DNA;
PHOSPHODIESTER BONDS;
PRE-STEADY STATE;
RATE LIMITING;
RATE-LIMITING STEPS;
REACTION COORDINATES;
REACTION MECHANISM;
REACTION STEPS;
SATURATING CONCENTRATION;
SINGLE-STRAND BREAKS;
STEADY STATE;
THERMODYNAMIC FRAMEWORK;
CATALYSIS;
ENZYMES;
KINETICS;
MAGNESIUM;
MAMMALS;
METAL IONS;
REACTION KINETICS;
DNA;
ADENOSINE TRIPHOSPHATE;
MAGNESIUM ION;
POLYDEOXYRIBONUCLEOTIDE SYNTHASE;
POLYDEOXYRIBONUCLEOTIDE SYNTHASE 1;
SINGLE STRANDED DNA;
UNCLASSIFIED DRUG;
ADENYLATION;
ARTICLE;
BINDING AFFINITY;
BINDING KINETICS;
CHEMICAL BOND;
CONCENTRATION (PARAMETERS);
CONTROLLED STUDY;
DNA REPAIR;
DNA REPLICATION;
DNA STRAND BREAKAGE;
ENZYME BINDING;
ENZYME MECHANISM;
ENZYME SPECIFICITY;
GENOMIC INSTABILITY;
HUMAN;
HUMAN CELL;
PRIORITY JOURNAL;
STEADY STATE;
THERMODYNAMICS;
ADENOSINE TRIPHOSPHATE;
CATALYSIS;
DNA;
DNA BREAKS;
DNA LIGASES;
DNA REPAIR;
DNA REPLICATION;
HUMANS;
KINETICS;
MAGNESIUM;
MAMMALIA;
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EID: 79959536186
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M111.248831 Document Type: Article |
Times cited : (33)
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References (29)
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