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Volumn 277, Issue 29, 2002, Pages 26163-26170
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The membrane-peripheral subunits of transhydrogenase from Entamoeba histolytica are functional only when dimerized
a a a |
Author keywords
[No Author keywords available]
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Indexed keywords
BACTERIA;
CATALYSIS;
CRYSTAL STRUCTURE;
DIMERIZATION;
DIMERS;
HYDROGENATION;
POLYPEPTIDES;
PROTOZOA;
X RAY SCATTERING;
BINDING COMPONENTS;
BIOLOGICAL MEMBRANES;
HYBRID PROTEIN;
NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE;
ARTICLE;
CATALYSIS;
CRYSTAL STRUCTURE;
DIMERIZATION;
ENTAMOEBA HISTOLYTICA;
ENZYME ANALYSIS;
ENZYME SUBUNIT;
HYDROGENATION;
NONHUMAN;
PRIORITY JOURNAL;
RADIATION SCATTERING;
ANIMALS;
DIMERIZATION;
ENTAMOEBA HISTOLYTICA;
NAD;
NADP;
NADP TRANSHYDROGENASE;
PROTEIN CONFORMATION;
SCATTERING, RADIATION;
STRUCTURE-ACTIVITY RELATIONSHIP;
BACTERIA (MICROORGANISMS);
ENTAMOEBA;
ENTAMOEBA HISTOLYTICA;
GOSSYPIUM HIRSUTUM;
MAMMALIA;
PROTOZOA;
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EID: 0037135584
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M203514200 Document Type: Article |
Times cited : (9)
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References (42)
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