Dr. James D Reid M.D.
Surgeon
849 82nd Pkwy Myrtle Beach SC, 29572About
Dr. James Reid is a general surgeon practicing in Myrtle Beach, SC. Dr. Reid specializes in abdominal contents including the esophagus, stomach, liver, gallbladder, pancreas and often thyroid glands. General surgeons are able to deal with almost any surgical or critical care emergency, also involving the skin or soft tissue trauma. Dr. Reid provides quality surgical service for gravely ill or injured patients and is able to respond quickly due to knowledge of various surgical procedures.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803.
- Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.
- The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring.
- Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation.
- Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.
- Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis.
- Direct measurement of metal-ion chelation in the active site of the AAA+ ATPase magnesium chelatase.
- Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.
- A case of adalimumab-induced pneumonitis in a 45-year-old man with Crohn's disease.
- Burkholderia gladioli - a predictor of poor outcome in cystic fibrosis patients who receive lung transplants? A case of locally invasive rhinosinusitis and persistent bacteremia in a 36-year-old lung transplant recipient with cystic fibrosis.
- Nonequilibrium isotope exchange reveals a catalytically significant enzyme-phosphate complex in the ATP hydrolysis pathway of the AAA(+) ATPase magnesium chelatase.
- The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.
- Characterization of the magnesium chelatase from Thermosynechococcus elongatus.
- Five glutamic acid residues in the C-terminal domain of the ChlD subunit play a major role in conferring Mg(2+) cooperativity upon magnesium chelatase.
- The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.
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