Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Katrina L. Bogan"'
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e19710 (2011)
NAD(+) is both a co-enzyme for hydride transfer enzymes and a substrate of sirtuins and other NAD(+) consuming enzymes. NAD(+) biosynthesis is required for two different regimens that extend lifespan in yeast. NAD(+) is synthesized from tryptophan an
Externí odkaz:
https://doaj.org/article/7cb4c44855ef40bf95b7543128eb6196
Autor:
Wolfram Tempel, Wael M Rabeh, Katrina L Bogan, Peter Belenky, Marzena Wojcik, Heather F Seidle, Lyudmila Nedyalkova, Tianle Yang, Anthony A Sauve, Hee-Won Park, Charles Brenner
Publikováno v:
PLoS Biology, Vol 5, Iss 10, p e263 (2007)
The eukaryotic nicotinamide riboside kinase (Nrk) pathway, which is induced in response to nerve damage and promotes replicative life span in yeast, converts nicotinamide riboside to nicotinamide adenine dinucleotide (NAD+) by phosphorylation and ade
Externí odkaz:
https://doaj.org/article/6e381eb8f8a6473f955a9c049c6e9369
Autor:
David K. Meyerholz, Joseph Zabner, Paula S. Ludwig, Jeng-Haur Chen, Leah R. Reznikov, Peter J. Taft, Tanner J. Wallen, Philip H. Karp, Paul B. McCray, Sarah E. Ernst, Nicholas D. Gansemer, Michael V. Rector, George A. Nelson, Mahmoud M.Abou Alaiwa, Emma E. Hornick, Randall S. Prather, Eugene H. Chang, Ryan J. Adam, Alejandro A. Pezzulo, David A. Stoltz, Drake C. Bouzek, Lynda S. Ostedgaard, Michael J. Welsh, Tatiana Rokhlina, Melissa Samuel, James D. McMenimen, Katrina L. Bogan, Mark J. Hoegger, Christine L. Wohlford-Lenane, Eric A. Hoffman
Publikováno v:
Journal of Clinical Investigation. 123:2685-2693
Cystic fibrosis (CF) pigs develop disease with features remarkably similar to those in people with CF, including exocrine pancreatic destruction, focal biliary cirrhosis, micro-gallbladder, vas deferens loss, airway disease, and meconium ileus. Where
Autor:
Charles R. Evans, Charles F. Burant, Robert T. Kennedy, Peter Belenky, Katrina L. Bogan, Peng Song, Charles Brenner
Publikováno v:
Journal of Biological Chemistry. 284:34861-34869
Recently, we discovered that nicotinamide riboside and nicotinic acid riboside are biosynthetic precursors of NAD(+), which are utilized through two pathways consisting of distinct enzymes. In addition, we have shown that exogenously supplied nicotin
Autor:
Katrina L. Bogan, Jeffrey S. Smith, Julie M. McClure, Peter Belenky, Frances G. Racette, Charles Brenner
Publikováno v:
Cell. 129:473-484
Summary Although NAD + biosynthesis is required for Sir2 functions and replicative lifespan in yeast, alterations in NAD + precursors have been reported to accelerate aging but not to extend lifespan. In eukaryotes, nicotinamide riboside is a newly d
Publikováno v:
Trends in Biochemical Sciences. 32:12-19
Nicotinamide adenine dinucleotide (NAD(+)) is both a coenzyme for hydride-transfer enzymes and a substrate for NAD(+)-consuming enzymes, which include ADP-ribose transferases, poly(ADP-ribose) polymerases, cADP-ribose synthases and sirtuins. Recent r
Autor:
Katrina L. Bogan, Charles Brenner
Nicotinamide adenine dinucleotide (NAD + ) and its phosphorylated form, nicotinamide adenine dinucleotide phosphate (NADP + ), are hydride-accepting coenzymes that play essential roles in substrate oxidation reactions in metabolism. The reduced forms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fad7fcd01b50e039e37a238dadd8776
https://doi.org/10.1016/b978-0-12-378630-2.00103-1
https://doi.org/10.1016/b978-0-12-378630-2.00103-1
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e19710 (2011)
PLoS ONE
PLoS ONE
NAD(+) is both a co-enzyme for hydride transfer enzymes and a substrate of sirtuins and other NAD(+) consuming enzymes. NAD(+) biosynthesis is required for two different regimens that extend lifespan in yeast. NAD(+) is synthesized from tryptophan an
Autor:
Katrina L. Bogan, Charles Brenner
Publikováno v:
ChemInform. 41
5′-Nucleotidase (EC 3.1.3.5) designates a set of enzymes, which catalyze the hydrolysis of ribonucleoside and deoxyribonucleoside monophosphates into the corresponding nucleosides plus orthophosphate. 5′-Nucleotidases are classified according to