Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Verena Wenzl"'
Publikováno v:
Microorganisms, Vol 11, Iss 4, p 830 (2023)
Combination therapies appear to be beneficial for preventing bacterial resistance to antibacterial approaches. The aim of this study was to define and determine an optimal effective concentration combination (OPECC) for binary application of antibact
Externí odkaz:
https://doaj.org/article/b02ebaa30d634ff5bd6436e70ff60f3a
Autor:
Bernd Mayer, Cristina M. Furdui, Barbara S. Lang, Leslie B. Poole, M. Verena Wenzl, Gustav Oberdorfer, Karl Gruber, Antonius C.F. Gorren
Publikováno v:
Journal of Biological Chemistry. 287:38124-38134
Aldehyde dehydrogenase-2 (ALDH2) catalyzes the bioactivation of nitroglycerin (glyceryl trinitrate, GTN) in blood vessels, resulting in vasodilation by nitric oxide (NO) or a related species. Because the mechanism of this reaction is still unclear we
Autor:
Bernd Mayer, Matteo Beretta, Antonius C.F. Gorren, Doris Koesling, M. Verena Wenzl, Robert Weis, Michael Russwurm, Kurt Schmidt
Publikováno v:
The Journal of Biological Chemistry
The East Asian variant of mitochondrial aldehyde dehydrogenase (ALDH2) exhibits significantly reduced dehydrogenase, esterase, and nitroglycerin (GTN) denitrating activities. The small molecule Alda-1 was reported to partly restore low acetaldehyde d
Autor:
Karl Gruber, Antonius C.F. Gorren, Doris Koesling, Matteo Beretta, Pravas Kumar Baral, Andreas Zeller, Michael Russwurm, Kurt Schmidt, Bernd Mayer, M. Verena Wenzl
Publikováno v:
The Journal of Biological Chemistry
Mitochondrial aldehyde dehydrogenase-2 (ALDH2) plays an essential role in nitroglycerin (GTN) bioactivation, resulting in formation of NO or a related activator of soluble guanylate cyclase. ALDH2 denitrates GTN to 1,2-glyceryl dinitrate and nitrite
Publikováno v:
Cardiovascular Research. 79:304-312
Aims Nitroglycerin (GTN) acts through release of a nitric oxide (NO)-related activator of soluble guanylate cyclase in vascular smooth muscle. Besides enzymatic GTN bioactivation catalysed by aldehyde dehydrogenase, non-enzymatic reaction of GTN with
Autor:
Barbara S, Lang, Antonius C F, Gorren, Gustav, Oberdorfer, M Verena, Wenzl, Cristina M, Furdui, Leslie B, Poole, Bernd, Mayer, Karl, Gruber
Publikováno v:
The Journal of Biological Chemistry
Background: Aldehyde dehydrogenase-2 (ALDH2) catalyzes bioactivation of glyceryl trinitrate (GTN) resulting in vasodilation. The exact mechanism is still unclear. Results: Structures of ALDH2 in complex with GTN and of a thionitrate intermediate were
Autor:
Martina Griesberger, M. Verena Wenzl, Matteo Beretta, Alexander Kollau, Doris Koesling, Gerald Wölkart, Antonius C.F. Gorren, Bernd Mayer, Michael Russwurm, Kurt Schmidt
Publikováno v:
Molecular pharmacology. 79(3)
Mitochondrial aldehyde dehydrogenase (ALDH2) contributes to vascular bioactivation of the antianginal drugs nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN), resulting in cGMP-mediated vasodilation. Although continuous treatment with GTN r
Autor:
Matteo Beretta, Bernd Mayer, M. Verena Wenzl, Robert Weis, Doris Koesling, Antonius C.F. Gorren, Michael Russwurm, Kurt Schmidt
Publikováno v:
BMC Pharmacology
Background The East Asian variant of mitochondrial aldehyde dehydrogenase (ALDH2) exhibits significantly reduced dehydrogenase, esterase and nitroglycerin (GTN) reductase activities [1]. The small molecule Alda-1 was reported to partly restore low ac
Autor:
Doris Koesling, Matteo Beretta, Andreas Zeller, Bernd Mayer, Heike Stessel, M. Verena Wenzl, Michael Russwurm, Kurt Schmidt
Publikováno v:
Molecular pharmacology. 76(5)
Nitroxyl (HNO) may be formed endogenously by uncoupled nitric-oxide (NO) synthases, enzymatic reduction of NO or as product of vascular nitroglycerin bioactivation. The established HNO donor Angeli's salt (trioxodinitrate, AS) causes cGMP-dependent v
Autor:
Bernd Mayer, Matteo Beretta, Gerald Wölkart, Heike Stessl, Michaela Verena Wenzl, Kurt Schmidt
Publikováno v:
Nitric Oxide. 19:61-62