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Donald J. Creighton
Researcher at University of Maryland, Baltimore County
Publications - 48
Citations - 1653
Donald J. Creighton is an academic researcher from University of Maryland, Baltimore County. The author has contributed to research in topics: Lactoylglutathione lyase & Glutathione. The author has an hindex of 24, co-authored 48 publications receiving 1595 citations. Previous affiliations of Donald J. Creighton include University of Maryland, College Park & University of Pittsburgh.
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Journal ArticleDOI
Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.
Alexander D. Cameron,Marianne Ridderström,B. Olin,Malcolm J. Kavarana,Donald J. Creighton,Bengt Mannervik +5 more
TL;DR: The structures of human glyoxalase I in complexes with S-benzylglutathione and NBC-GSH have been determined and the carboxyl of Glu 172 is proposed to be displaced from the inner coordination sphere of the metal ion during substrate binding, allowing this group to facilitate proton transfer between the adjacent carbon atoms of the substrate.
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Optimization of efficiency in the glyoxalase pathway.
TL;DR: The model exhibits the following properties under conditions where substrate concentrations are small in comparison to the Km values for the glyoxalase enzymes: the overall rate of conversion of methylglyoxal to D-lactate is primarily limited by the rate of formation of the diastereotopic thiohemiacetals.
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Active monomeric and dimeric forms of pseudomonas putida glyoxalase i : evidence for 3d domain swapping
TL;DR: Glyoxalase I appears to be a novel example of a single protein able to exist in two alternative domain-swapped forms and the only example to date in which 3D domain swapping can be regulated by a small organic ligand.
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N-(2-hydroxypropyl)methacrylamide copolymers of a glutathione (GSH)-activated glyoxalase i inhibitor and DNA alkylating agent: synthesis, reaction kinetics with GSH, and in vitro antitumor activities.
TL;DR: The incorporation of anticancer prodrugs into polyacrylamide conjugates has been shown to improve tumor targeting via the so-called "enhanced permeability and retention" effect, and this prodrug strategy should be applicable to a range of different GSH-based antitumor agents.