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Denaturation and reactivation of dimeric human glutathione reductase: an assay for folding inhibitors

Nordhoff, A. and Tziatzios, C. and van den Broek, J. A. and Schott, M. K. and Kalbitzer, Hans Robert and Becker, K. and Schubert, D. and Schirmer, R. H. (1997) Denaturation and reactivation of dimeric human glutathione reductase: an assay for folding inhibitors. European journal of biochemistry (=the FEBS journal) 245 (2), pp. 273-282.

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Abstract

Human glutathione reductase (GR; which catalyzes the reaction NADPH + GSSG + H+ --> 2 GSH + NADP+) is an obligatory FAD-containing homodimer of known geometry. Native human GR, a potential target of antimalarial and cytostatic agents, cannot be dissociated by dilution or by means of subunit-interface mimetics, similarly to well-studied viral dimeric proteins. However, ab initio folding and/or ...

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Item Type:Article
Date:1997
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
9151953PubMed ID
Classification:
NotationType
DimerizationMESH
Enzyme Inhibitors/pharmacologyMESH
Glutathione Reductase/pharmacologyMESH
GuanidineMESH
Guanidines/pharmacologyMESH
HumansMESH
Magnetic Resonance SpectroscopyMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Peptide Fragments/pharmacologyMESH
Protein Conformation/drug effectsMESH
Protein DenaturationMESH
Protein FoldingMESH
Time FactorsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:16
Last Modified:13 Sep 2010 08:16
Item ID:16549
Owner Only: item control page
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