Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Alexander K H Weiss"'
Publikováno v:
PLoS ONE, Vol 14, Iss 8, p e0220434 (2019)
Human fumarylacetoacetate hydrolase (FAH) domain containing protein 1 (FAHD1) is a mitochondrial oxalocatate decarboxylase, the first of its kind identified in eukaryotes. The physiological role of FAHD1 in other eukaryotes is still poorly understood
Externí odkaz:
https://doaj.org/article/18befc3000004e1f98397155a70bf540
Autor:
Andreas Andric, Michael Niederwanger, Eva Albertini, Pidder Jansen-Dürr, Stephen R. Stürzenbaum, Reinhard Dallinger, Veronika Pedrini-Martha, Alexander K. H. Weiss
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-14 (2024)
Abstract Metallothioneins (MTs) are a family of mostly low-molecular weight, cysteine-rich proteins capable of specific metal-ion binding that are involved in metal detoxification and homeostasis, as well as in stress response. In contrast to most ot
Externí odkaz:
https://doaj.org/article/f3acd5f102614a85950013f21c9716b2
Autor:
Anne Heberle, Elia Cappuccio, Andreas Andric, Tatjana Kuen, Anna Simonini, Alexander K. H. Weiss
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-17 (2024)
Abstract This study investigated the impact of overexpressing the mitochondrial enzyme Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) in human osteosarcoma epithelial cells (U2OS) in vitro. While the downregulation or knockdown of
Externí odkaz:
https://doaj.org/article/32e25f26eadc490bb104834b1153c188
Autor:
Markus Mandl, Hans P. Viertler, Maria Zopoglou, Maria C. Mitterberger-Vogt, Juliane Gasser, Florian M. Hatzmann, Tina Rauchenwald, Marit E. Zwierzina, Monika Mattesich, Alexander K. H. Weiss, Lorenza Mottes, Camille Brucker, Petra Waldegger, Gerhard Pierer, Werner Zwerschke
Publikováno v:
Cell death discovery. 8(1)
Misalignment of physiological circadian rhythms promotes obesity which is characterized by white adipose tissue (WAT) expansion. Differentiation of Adipose stem/progenitor cells (ASCs) contributes to WAT increase but the importance of the cellular cl
Publikováno v:
Journal of visualized experiments : JoVE. (180)
Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) is the first identified member of the FAH superfamily in eukaryotes, acting as oxaloacetate decarboxylase in mitochondria. This article presents a series of methods for the extraction
Autor:
Michele Petit, Giorgia Baraldo, Alexander K. H. Weiss, Pidder Jansen-Dürr, Solmaz Etemad, André Schrattenholz
Publikováno v:
Mechanisms of Ageing and Development. 177:22-29
FAHD1, a member of the FAH superfamily of enzymes, was identified in a proteomic screen for mitochondrial proteins with differential expression in young versus senescent human endothelial cells. FAHD1 acts as oxaloacetate decarboxylase, and recent ob
Autor:
Pidder Jansen-Dürr, Hubert Gstach, Bernhard Rupp, Andreas Naschberger, Karin Kreidl, Ilaria Dorigatti, Elia Cappuccio, Max Holzknecht, Alexander K. H. Weiss
Publikováno v:
Journal of visualized experiments : JoVE
Fumarylacetoacetate hydrolase (FAH) domain-containing proteins (FAHD) are identified members of the FAH superfamily in eukaryotes. Enzymes of this superfamily generally display multi-functionality, involving mainly hydrolase and decarboxylase mechani
Autor:
Elisabeth Damisch, Anna Krahbichler, Alexander K. H. Weiss, Elia Cappuccio, Hubert Gstach, Pidder Jansen-Dürr, Max Holzknecht, Eva Albertini, Ilaria Dorigatti
Publikováno v:
Mechanisms of ageing and development
Fumarylacetoacetate hydrolase (FAH) superfamily members are commonly expressed in the prokaryotic kingdom, where they take part in the committing steps of degradation pathways of complex carbon sources. Besides FAH itself, the only described FAH supe
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 8, p e0220434 (2019)
PLoS ONE, Vol 14, Iss 8, p e0220434 (2019)
Human fumarylacetoacetate hydrolase (FAH) domain containing protein 1 (FAHD1) is a mitochondrial oxalocatate decarboxylase, the first of its kind identified in eukaryotes. The physiological role of FAHD1 in other eukaryotes is still poorly understood
Autor:
Pidder Jansen-Dürr, Annabella Pittl, Alexander K. H. Weiss, Hubert Gstach, Klaus Scheffzek, Max Holzknecht, Theresia Dunzendorfer-Matt, Matthew W. Bowler, Elia Cappuccio, Klaus R. Liedl, Johannes R. Loeffler, Solmaz Etemad, Andreas Naschberger
Publikováno v:
Biochem J
Whereas enzymes in the fumarylacetoacetate hydrolase (FAH) superfamily catalyze several distinct chemical reactions, the structural basis for their multi-functionality remains elusive. As a well-studied example, human FAH domain-containing protein 1