Dr. Gregory A. Grant D.P.M.
Podiatrist (Foot and Ankle Specialist) | Foot & Ankle Surgery
1959 NE Pacific St Seattle WA, 98195About
Dr. Gregory Grant is a podiatrist practicing in Seattle, WA. Dr. Grant is a medical doctor specializing in the treatment of the foot , ankle and related parts of the leg. As a podiatrist, Dr. Grant diagnoses and treats conditions of the feet. The feet are key body parts that give a person stability, absorb shock, allow for walking and standing and are necessary for overall well-being. So, the feet need expert care. Podiatrists can specialize in surgery, wound care, sports medicine, diabetic care and pediatrics.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.
- De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal.
- Identification of PTH-amino acids by HPLC.
- Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
- Pancreatic islets and insulinoma cells express a novel isoform of group VIA phospholipase A2 (iPLA2 beta) that participates in glucose-stimulated insulin secretion and is not produced by alternate splicing of the iPLA2 beta transcript.
- Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.
- Multiconformational states in phosphoglycerate dehydrogenase.
- Methods for analyzing cooperativity in phosphoglycerate dehydrogenase.
- Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits.
- D-3-Phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes.
- Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.
- Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
- The ACT domain: a small molecule binding domain and its role as a common regulatory element.
- The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase.
- A novel mechanism for substrate inhibition in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase.
Dr. Gregory A. Grant D.P.M.'s Practice location
UW Medicine Headache Clinic
1959 NE Pacific St -Seattle, WA 98195Get Direction
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