Zobrazeno 1 - 10
of 123
pro vyhledávání: '"Henry M, Miziorko"'
Publikováno v:
American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 308:R872-R878
The objective of this study was to determine the potential role of astrocyte-derived ketone bodies in regulating the early changes in caloric intake of diet induced-obese (DIO) versus diet-resistant (DR) rats fed a 31.5% fat high-energy (HE) diet. Af
Autor:
D. Andrew Skaff, William J. McWhorter, Henry M. Miziorko, Gerald J. Wyckoff, Brian V. Geisbrecht
Publikováno v:
Archives of Biochemistry and Biophysics. 566:1-6
Mevalonate diphosphate decarboxylase (MDD; EC 4.1.1.33) catalyzes the irreversible decarboxylation of mevalonate diphosphate in the mevalonate pathway to form isopentenyl diphosphate, which is a precursor in the biosynthesis of many essential polyiso
Autor:
D. A. Skaff, James K. Addo, Andrew Keightley, Henry M. Miziorko, Gerald J. Wyckoff, John VanNice
Publikováno v:
Journal of Bacteriology. 196:1055-1063
Mevalonate (MVA) metabolism provides the isoprenoids used in archaeal lipid biosynthesis. In synthesis of isopentenyl diphosphate, the classical MVA pathway involves decarboxylation of mevalonate diphosphate, while an alternate pathway has been propo
Publikováno v:
Journal of Bacteriology. 195:3854-3862
Enzymes of the isoprenoid biosynthetic pathway in halophilic archaea remain poorly characterized, and parts of the pathway remain cryptic. This situation may be explained, in part, by the difficulty of expressing active, functional recombinant forms
Autor:
Jeffrey C. Murphy, Brian J. Moldover, Ada Solidar, Henry M. Miziorko, Gerald J. Wyckoff, Christa Montgomery
Publikováno v:
The Open Medicinal Chemistry Journal
ChemVassa, a new chemical structure search technology, was developed to allow rapid in silico screening of compounds for hit and hit-to-lead identification in drug development. It functions by using a novel type of molecular descriptor that examines,
Publikováno v:
Biochemistry. 51:5611-5621
Mevalonate diphosphate decarboxylase (MDD) catalyzes the final step of the mevalonate pathway, the Mg{sup 2+}-ATP dependent decarboxylation of mevalonate 5-diphosphate (MVAPP), producing isopentenyl diphosphate (IPP). Synthesis of IPP, an isoprenoid
Autor:
D. Andrew Skaff, Michael L. Barta, William J. McWhorter, Henry M. Miziorko, Kasra X. Ramyar, Brian V. Geisbrecht
Publikováno v:
Biochemistry. 51:4713-4722
Hymeglusin (1233A, F244, L-659-699) is established as a specific β-lactone inhibitor of eukaryotic hydroxymethylglutaryl-CoA synthase (HMGCS). Inhibition results from formation of a thioester adduc...
Autor:
Christa Montgomery, Henry M. Miziorko
Publikováno v:
Archives of Biochemistry and Biophysics. 511:48-55
Human 3-hydroxy-3-methylglutaryl-CoA lyase catalyzes formation of acetyl-CoA and acetoacetate in a reaction that requires divalent cation and is stimulated by sulfhydryl protective reagents. The enzyme is a homodimer and inter-subunit adducts form in
Autor:
Henry M. Miziorko
Publikováno v:
Archives of Biochemistry and Biophysics. 505:131-143
The mevalonate pathway accounts for conversion of acetyl-CoA to isopentenyl 5-diphosphate, the versatile precursor of polyisoprenoid metabolites and natural products. The pathway functions in most eukaryotes, archaea, and some eubacteria. Only recent
Autor:
Timothy J. Herdendorf, Daniel S. Sem, Patchareenart Saparpakorn, Sheng Cai, Henry M. Miziorko, Huili Yao, Andrew L. Olson, Supa Hannongbua
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 75:127-138
Phosphomevalonate kinase (PMK) catalyzes an essential step in the mevalonate pathway, which is the only pathway for synthesis of isoprenoids and steroids in humans. PMK catalyzes transfer of the gamma-phosphate of ATP to mevalonate 5-phosphate (M5P)