Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Elia Cappuccio"'
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:
Ahmad Salti, Solmaz Etemad, Marta Suarez Cubero, Eva Albertini, Beata Kovacs-Szalka, Max Holzknecht, Elia Cappuccio, Maria Cavinato, Frank Edenhofer, Pidder Jansen Dürr
Publikováno v:
Cells, Vol 10, Iss 8, p 2040 (2021)
Mitochondria play a key role in metabolic transitions involved in the reprogramming of somatic cells into induced pluripotent stem cells (iPSCs), but the underlying molecular mechanisms remain largely unexplored. To obtain new insight into the mechan
Externí odkaz:
https://doaj.org/article/82cf94bd3d604eb8bfae83ffb54d86d5
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86a6edf5cf140c037bcbc2bca3826e41
http://europepmc.org/articles/PMC7115867
http://europepmc.org/articles/PMC7115867
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda42565b03a1b40a7a0335c362f4115
https://doi.org/10.1016/j.mad.2020.111284
https://doi.org/10.1016/j.mad.2020.111284
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6951815dac59cfdd0f224fcf9bec41b0
https://pubmed.ncbi.nlm.nih.gov/30348641
https://pubmed.ncbi.nlm.nih.gov/30348641