D. J. Creighton

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Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations.

D. J. Creighton, D. S. Hamilton, D. Hamilton, 2001, Archives of biochemistry and biophysics.

Glyoxalase I inhibitors in cancer chemotherapy.

R. Holewinski, J. Eiseman, D. J. Creighton, 2003, Biochemical Society transactions.

Oxalacetate decarboxylase activity in muscle is due to pyruvate kinase.

I. A. Rose, D. J. Creighton, 1976, The Journal of biological chemistry.

Model dehydrogenase reactions. Zinc ion catalyzed reduction of chelating aldehydes by N-propyl-1,4-dihydronicotinamides and borohydride.

J. Hajdu, D. Sigman, D. J. Creighton, 1976, Journal of the American Chemical Society.

Alkylation of nucleic acids by the antitumor agent COMC.

B. Ganem, D. Fabris, D. J. Creighton, 2002, Organic letters.

A new method for rapidly generating inhibitors of glyoxalase I inside tumor cells using S-(N-aryl-N-hydroxycarbamoyl)ethylsulfoxides.

M. Kavarana, J. Eiseman, D. J. Creighton, 1999, Journal of medicinal chemistry.

Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping.

M. Stone, K. R. Phillips, D. J. Creighton, 1998, Biochemistry.

Limiting rates of ligand association to alcohol dehydrogenase.

D. Sigman, D. J. Creighton, M. Frolich, 1978, Archives of biochemistry and biophysics.

Is the thiolate—imidazolium ion pair the catalytically important form of papain?

D. J. Creighton, Morris S. Gessouroun, James M. Heapes, 1980, FEBS letters.

The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I.

C. Fenselau, P. S. Lovett, D. J. Creighton, 1994, Gene.

Substrate specificity of bovine liver formaldehyde dehydrogenase.

T. Pourmotabbed, D. J. Creighton, 1986, The Journal of biological chemistry.

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.

J. Eiseman, E. Joseph, D. J. Creighton, 2005, Bioconjugate chemistry.

Active-site ionizations of papain. An evaluation of the potentiometric difference titration method.

D. J. Creighton, M. Migliorini, 1986, European journal of biochemistry.

Novel bivalent inhibitors with sub-nanomolar affinities towards human glyoxalase I.

Qing Shi, Ming-guang Mo, D. J. Creighton, 2015, Bioorganic & medicinal chemistry letters.

Glutathionyl transferase catalyzed addition of glutathione to COMC: a new hypothesis for antitumor activity.

B. Ganem, D. J. Creighton, Zhebo Ding, 2002, Organic letters.

Solvent isotope effects on the rates of alkylation of thiolamine models of papain

D. J. Creighton, Angela Wandinger, 1980, FEBS letters.

Solvent isotope effects on tautomerization equilibria of papain and model thiolamines

D. J. Creighton, D. Schamp, D. Schamp, 1980, FEBS letters.

Models for metalloenzymes. Zinc ion catalyzed phosphorylation of 1,10-phenanthroline-2-carbinol by adenosine triphosphate.

D. Sigman, D. J. Creighton, G. Wahl, 1972, Biochemistry.

Synthesis and initial characterization of γ-L-glutamyl-L-thiothreonyl-glycine and γ-L-glutamyl-L-allo-thiothreonylglycine as steric probes of the active site of glyoxalase I

D. J. Creighton, Xiao-Lan Xie, 1991 .

Optimization of efficiency in the glyoxalase pathway.

T. Pourmotabbed, M. Guha, D. J. Creighton, 1988, Biochemistry.

Role of hydrophobic interactions in binding S-(N-aryl/alkyl-N-hydroxycarbamoyl)glutathiones to the active site of the antitumor target enzyme glyoxalase I.

M. Kavarana, D. J. Creighton, D. Whalen, 2000, Journal of medicinal chemistry.

Nonstereospecific substrate usage by glyoxalase I.

L. Ong, D. J. Creighton, L. Buettner, 1983, Biochemistry.

Caution: the glycylmethyl and glycylethyl esters of glutathione are substrates for glyoxalase I.

D. J. Creighton, D. Hamilton, 1992, Biochimica et biophysica acta.

7 Stereochemistry of Enzyme -Catalyzed Reactions at Carbon

D. J. Creighton, N. Murthy, 1990 .

Inhibition by active site directed covalent modification of human glyoxalase I.

R. Holewinski, D. J. Creighton, 2014, Bioorganic & medicinal chemistry.

Bivalent transition-state analogue inhibitors of human glyoxalase I.

D. J. Creighton, Zhe-Bin Zheng, 2003, Organic letters.

Hydrophobic binding is not an independent stereochemical determinant in the yeast glyoxalase I reaction.

D. J. Creighton, L. Buettner, A. Weiner, 1980, Biophysical chemistry.

Transition-state structure in the yeast alcohol dehydrogenase reaction: the magnitude of solvent and alpha-secondary hydrogen isotope effects.

J. Klinman, K. Welsh, D. J. Creighton, 1980, Biochemistry.

Model dehydrogenase reactions. Reduction of N-methylacridinium ion by reduced nicotinamide adenine dinucleotide and its derivatives.

J. Hajdu, D. Sigman, G. Mooser, 1973, Journal of the American Chemical Society.

A model for alcohol dehydrogenase. The zinc ion catalyzed reduction of 1,10-phenanthroline-2-carboxaldehyde by N-propyl-1,4-dihydronicotinamide.

D. Sigman, D. J. Creighton, 1971, Journal of the American Chemical Society.

Reaction of COTC with glutathione: structure of the putative glyoxalase I inhibitor.

B. Ganem, D. J. Creighton, D. Hamilton, 2000, Organic letters.

Enzyme chemistry of dithiohemiacetals: synthesis and characterization of S-D-dithiomandeloylglutathione as an alternate substrate for glyoxalase I.

M. Guha, D. J. Creighton, J. Li, 1991, Biochemical and biophysical research communications.

SOLVENT ISOTOPE EFFECTS IN THE YEAST ALCOHOL DEHYDROGENASE REACTION

J. Klinman, K. Welsh, D. J. Creighton, 1977 .

Mechanism of the glutathione transferase-catalyzed conversion of antitumor 2-crotonyloxymethyl-2-cycloalkenones to GSH adducts.

B. Ganem, K. Houk, B. Mannervik, 2003, Journal of the American Chemical Society.

Lentivirus-derived antimicrobial peptides: increased potency by sequence engineering and dimerization.

H. Vogel, R. Montelaro, T. Mietzner, 1999, The Journal of antimicrobial chemotherapy.

Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins

R. Montelaro, T. Mietzner, S. Tencza, 1997, Antimicrobial agents and chemotherapy.

Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts

S. Rahlfs, K. Becker, B. Mannervik, 2005, Biological chemistry.

Pharmacokinetics and antitumor properties in tumor-bearing mice of an enediol analogue inhibitor of glyoxalase I

M. Kavarana, J. Eiseman, D. Sentz, 2000, Cancer Chemotherapy and Pharmacology.

Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.

A D Cameron, B. Mannervik, A. Cameron, 1999, Biochemistry.

Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes.

D. V. Vander Jagt, M. Guha, D. J. Creighton, 1988, Biochemistry.

Diffusion-dependent kinetic properties of glyoxalase I and estimates of the steady-state concentrations of glyoxalase-pathway intermediates in glycolyzing erythrocytes.

D J Creighton, M J Shih, J W Edinger, 1997, European journal of biochemistry.

Evidence for a (Triosephosphate Isomerase-like) "Catalytic Loop" near the Active Site of Glyoxalase I (*)

P. S. Lovett, D. J. Creighton, T. Lu, 1995, The Journal of Biological Chemistry.

Mechanism-based competitive inhibitors of glyoxalase I: intracellular delivery, in vitro antitumor activities, and stabilities in human serum and mouse serum.

E G Kovaleva, E. Kovaleva, M. Kavarana, 1999, Journal of medicinal chemistry.

Studies on the mechanism and stereochemical properties of the oxalacetate decarboxylase activity of pyruvate kinase.

I. A. Rose, D. J. Creighton, 1976, The Journal of biological chemistry.

Molecular basis of the antitumor activities of 2-crotonyloxymethyl-2-cycloalkenones.

B. Ganem, J. Eiseman, E. Joseph, 2003, Journal of Medicinal Chemistry.

Selective inhibition of MCF-7(piGST) breast tumors using glutathione transferase-derived 2-methylene-cycloalkenones.

B. Ganem, J. Eiseman, E. Joseph, 2005, Journal of medicinal chemistry.

S-(N-aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II.

M. Kavarana, D. J. Creighton, D. Hamilton, 1994, Journal of medicinal chemistry.