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Volumn 4, Issue 9, 2002, Pages 674-680
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Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
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Author keywords
[No Author keywords available]
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Indexed keywords
ACONITATE HYDRATASE;
ADENOSINE TRIPHOSPHATE;
ENDOPEPTIDASE LA;
MATRIX PROTEIN;
OLIGODEOXYNUCLEOTIDE;
OXYGEN;
UNCLASSIFIED DRUG;
ARTICLE;
CELL VIABILITY;
CONTROLLED STUDY;
ENZYME ACTIVATION;
ENZYME DEGRADATION;
ENZYME INACTIVATION;
ENZYME INHIBITION;
ENZYME SUBSTRATE;
HUMAN;
HUMAN CELL;
HYDROPHOBICITY;
IMMUNITY;
LUNG FIBROBLAST;
MITOCHONDRIAL RESPIRATION;
OXIDATIVE STRESS;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN LOCALIZATION;
PROTEIN MODIFICATION;
PROTEIN STRUCTURE;
ACONITATE HYDRATASE;
ADENOSINE TRIPHOSPHATE;
ANIMALS;
ATP-DEPENDENT PROTEASES;
BASE SEQUENCE;
CATTLE;
CELL LINE;
HEAT-SHOCK PROTEINS;
HUMANS;
HYDROGEN PEROXIDE;
KINETICS;
MITOCHONDRIA;
MITOCHONDRIA, HEART;
OLIGODEOXYRIBONUCLEOTIDES, ANTISENSE;
OXIDATION-REDUCTION;
SERINE ENDOPEPTIDASES;
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EID: 0036713692
PISSN: 14657392
EISSN: None
Source Type: Journal
DOI: 10.1038/ncb836 Document Type: Article |
Times cited : (488)
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References (52)
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