Dr. John William Burgner M.D.
Anesthesiologist
2401 W University Ave Muncie IN, 47303About
Dr. John Burgner is an anesthesiologist practicing in Muncie, IN. Dr. Burgner ensures the safety of patients who are about to undergo surgery. Anestesiologists specialize in general anesthesia, which will (put the patient to sleep), sedation, which will calm the patient or make him or her unaware of the situation, and regional anesthesia, which just numbs a specific part of the body. As an anesthesiologist, Dr. Burgner also might help manage pain after an operation.
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Expert Publications
Data provided by the National Library of Medicine- Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis.
- Enterococcus faecalis 3-hydroxy-3-methylglutaryl coenzyme A synthase, an enzyme of isopentenyl diphosphate biosynthesis.
- Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase.
- CARBOXYMETHYLATION OF SPERM WHALE METMYOGLOBIN.
- Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold.
- Enterococcus faecalis phosphomevalonate kinase.
- Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.
- X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA.
- pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides.
- Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling.
- Transport of nonmetabolizable opines by Agrobacterium tumefaciens.
- Identification of the structural motif responsible for trimeric assembly of the C-terminal regulatory domains of polycystin channels PKD2L1 and PKD2.
- Bimodal substrate inhibition of lactate dehydrogenase. Factors affecting the enzyme in vivo.
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