Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Julia Birk"'
Autor:
Beáta Lizák, Julia Birk, Melinda Zana, Gergely Kosztyi, Denise V. Kratschmar, Alex Odermatt, Richard Zimmermann, Miklós Geiszt, Christian Appenzeller-Herzog, Gábor Bánhegyi
Publikováno v:
BMC Biology, Vol 18, Iss 1, Pp 1-16 (2020)
Abstract Background The lumen of the endoplasmic reticulum (ER) acts as a cellular Ca2+ store and a site for oxidative protein folding, which is controlled by the reduced glutathione (GSH) and glutathione-disulfide (GSSG) redox pair. Although depleti
Externí odkaz:
https://doaj.org/article/6e96e7b7282a4f3fb5aef956daf86129
Publikováno v:
Bio-Protocol, Vol 11, Iss 13 (2021)
The production of reactive oxygen species (ROS) and endoplasmic reticulum (ER) stress are tightly linked. The generation of ROS can be both the cause and a consequence of ER stress pathways, and an increasing number of human diseases are characterize
Externí odkaz:
https://doaj.org/article/4235bb70727d4292a6a9dd5db553295a
Autor:
Denise V Kratschmar, Diego Calabrese, Jo Walsh, Adam Lister, Julia Birk, Christian Appenzeller-Herzog, Pierre Moulin, Chris E Goldring, Alex Odermatt
Publikováno v:
PLoS ONE, Vol 7, Iss 5, p e36774 (2012)
Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) is a key transcription factor regulating a plethora of detoxifying enzymes and antioxidant genes involved in drug metabolism and defence against oxidative stress. The glucocorticoid receptor (GR) is
Externí odkaz:
https://doaj.org/article/934a5509ebc54bb3b681fafd05d3e56b
Autor:
Karen E. Chapman, Michael Weingartner, Petra Klusonova, Denise V. Kratschmar, Gareth G. Lavery, Julia Birk, Alex Odermatt, Simon Stücheli
Publikováno v:
British Journal of Pharmacology
BACKGROUND AND PURPOSE 11β-Hydroxysteroid dehydrogenase 1 (11β-HSD1) regulates tissue-specific glucocorticoid metabolism and its impaired expression and activity are associated with major diseases. Pharmacological inhibition of 11β-HSD1 is conside
Publikováno v:
Bio Protoc
The production of reactive oxygen species (ROS) and endoplasmic reticulum (ER) stress are tightly linked. The generation of ROS can be both the cause and a consequence of ER stress pathways, and an increasing number of human diseases are characterize
Autor:
Melinda Zana, Richard Zimmermann, Julia Birk, Beáta Lizák, Denise V. Kratschmar, Miklós Geiszt, Christian Appenzeller-Herzog, Gergely Kosztyi, Gábor Bánhegyi, Alex Odermatt
Publikováno v:
BMC Biology
BMC Biology, Vol 18, Iss 1, Pp 1-16 (2020)
BMC Biology, Vol 18, Iss 1, Pp 1-16 (2020)
Background The lumen of the endoplasmic reticulum (ER) acts as a cellular Ca2+ store and a site for oxidative protein folding, which is controlled by the reduced glutathione (GSH) and glutathione-disulfide (GSSG) redox pair. Although depletion of lum
Publikováno v:
The FEBS Journal. 285:3993-4004
Hexose-6-phosphate dehydrogenase (H6PD) is thought to be the major source of NADPH within the endoplasmic reticulum (ER), determining 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) reaction direction to convert inert 11-oxo- to potent 11β-hydroxygl
Publikováno v:
The FASEB Journal
Hexose-6-phosphate dehydrogenase (H6PD) produces reduced NADPH in the endoplasmic reticulum (ER) lumen. NADPH constitutes a cofactor for many reducing enzymes, and its inability to traverse biologic membranes makes in situ synthesis of NADPH in the E
Autor:
Denise V. Kratschmar, Hideaki Yamaguchi, Sharavan Kanagaratnam, Alex Odermatt, Julia Birk, Andreas W. Sailer, Klaus Seuwen, Katharina Beck
Publikováno v:
The Journal of steroid biochemistry and molecular biology. 190
Oxysterols are cholesterol metabolites derived through either autoxidation or enzymatic processes. They consist of a large family of bioactive lipids that have been associated with the progression of multiple pathologies. In order to unravel (patho-)
Autor:
Neila Belguith, Faiza Fakhfakh, Alex Odermatt, Bochra Ben Rhouma, Christoph P. Sager, Maria Tsachaki, Roger T. Engeli, Leila Keskes, Julia Birk
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 155:147-154
Mutations in the HSD17B3 gene resulting in 17β-hydroxysteroid dehydrogenase type 3 (17β-HSD3) deficiency cause 46, XY Disorders of Sex Development (46, XY DSD). Approximately 40 different mutations in HSD17B3 have been reported; only few mutant enz