Charles E. Grimshaw

Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme.

MECHANISM OF HUMAN ALDEHYDE REDUCTASE : CHARACTERIZATION OF THE ACTIVE SITE POCKET

Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis.

HUMAN ALDOSE REDUCTASE : RATE CONSTANTS FOR A MECHANISM INCLUDING INTERCONVERSION OF TERNARY COMPLEXES BY RECOMBINANT WILD-TYPE ENZYME

Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts.

HUMAN ALDOSE REDUCTASE : PK OF TYROSINE 48 REVEALS THE PREFERRED IONIZATION STATE FOR CATALYSIS AND INHIBITION

A Source of Response Regulator Autophosphatase Activity: The Critical Role of a Residue Adjacent to the Spo0F Autophosphorylation Active Site†

Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase.

Human aldose reductase: subtle effects revealed by rapid kinetic studies of the C298A mutant enzyme.

The Sorbinil Trap: A Predicted Dead-End Complex Confirms the Mechanism of Aldose Reductase Inhibition†