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Volumn 361, Issue 1, 2002, Pages 119-123
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Monomers of the catalytic domain of human neuropathy target esterase are active in the presence of phospholipid
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Author keywords
Interfacial activation; Membrane; Radiation inactivation; Secondary structure prediction
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Indexed keywords
BACTERIA;
DETERGENTS;
DIALYSIS;
OLIGOMERS;
PH EFFECTS;
PHOSPHOLIPIDS;
POLYPEPTIDES;
LIPOSOMES;
MONOMERS;
ESTERASE;
GLUTARALDEHYDE;
LIPOSOME;
MONOMER;
PHOSPHOLIPID;
POLYPEPTIDE;
PROTEIN NEST;
PROTEINASE K;
RECOMBINANT PROTEIN;
SERINE;
UNCLASSIFIED DRUG;
ALGORITHM;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
DENATURATION;
DIALYSIS;
ENZYME ACTIVITY;
ENZYME INACTIVATION;
HUMAN;
MOLECULAR INTERACTION;
NEUROPATHY;
OLIGOMERIZATION;
PH;
PHOSPHOLIPID METABOLISM;
PREDICTION;
PRIORITY JOURNAL;
PROTEIN CROSS LINKING;
PROTEIN DOMAIN;
PROTEIN PURIFICATION;
QUANTITATIVE ASSAY;
SOLUBILIZATION;
STRUCTURE ANALYSIS;
CARBOXYLIC ESTER HYDROLASES;
CATALYTIC DOMAIN;
CHOLIC ACIDS;
CROSS-LINKING REAGENTS;
DETERGENTS;
ENZYME INHIBITORS;
ESCHERICHIA COLI;
GLUTARAL;
HUMANS;
HYDROGEN-ION CONCENTRATION;
KINETICS;
LIPOSOMES;
PHOSPHOLIPIDS;
PROTEIN DENATURATION;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
BACTERIA (MICROORGANISMS);
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EID: 0036180175
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3610119 Document Type: Article |
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Times cited : (19)
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References (15)
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