• Publications
  • Influence
GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop
TLDR
Kinetic studies suggest that mobility in the catalytic loop promotes a side reaction that results in cofactor release and GAD65 autoinactivation, and these data reveal the molecular basis for regulation of GABA homeostasis.
Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.
The structure of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides was determined at 3.1-A resolution by the molecular replacement method, using the Rhodopseudomonas viridis RC as
Sorbitol dehydrogenase: structure, function and ligand design.
TLDR
The available structural and biochemical information of SDH are currently being utilized in a structure-based approach to develop drugs for the treatment or prevention of the complications of diabetes.
Structure of human factor D. A complement system protein at 2.0 A resolution.
TLDR
Factor D is the first complement serine protease whose three-dimensional structure has been determined, and there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serinine proteases.
Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.
TLDR
The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
Correlation of paramagnetic states and molecular structure in bacterial photosynthetic reaction centers: the symmetry of the primary electron donor in Rhodopseudomonas viridis and Rhodobacter
TLDR
The large reduction of the zero field splitting parameters relative to monomeric bacteriochlorophyll triplet in vitro suggests significant participation of asymmetrical charge transfer electronic configurations in the special pair triplet state of both organisms.
...
...