Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Merete Høyem"'
Autor:
Chencheng Wang, Shadab Abadpour, Aleksandra Aizenshtadt, Andrea Dalmao-Fernandez, Merete Høyem, Ingrid Wilhelmsen, Justyna Stokowiec, Petter Angell Olsen, Stefan Krauss, Simona Chera, Luiza Ghila, Helge Ræder, Hanne Scholz
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 12 (2024)
Stem cell-derived islets (SC-islets) are not only an unlimited source for cell-based therapy of type 1 diabetes but have also emerged as an attractive material for modeling diabetes and conducting screening for treatment options. Prior to SC-islets b
Externí odkaz:
https://doaj.org/article/4afe0562c8be4495b25a69fa136af8a3
Autor:
Jo Waaler, Stefan Krauss, Anita Wegert, Ruben G.G. Leenders, Ilonka A.T.M. Meerts, Lari Lehtiö, Albert Galera-Prat, Sven T. Sowa, Gunnveig Grødeland, Hanne Scholz, Merete Høyem, Lone Holmen, Petter A. Olsen, Aleksandra Aizenshtadt, Clara Hammarström, Sandra Espada, Enya Amundsen-Isaksen, Shoshy A. Brinch
Supplementary Figure S1. Chemical structures of selected tankyrase inhibitors. Supplementary Figure S2. OM-153 specifically inhibits TNKS1/2 and WNT/β-catenin signaling. Supplementary Figure S3. OM-153 specifically inhibits cell growth of an APC-mut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ae321b85444944ba3b4b1f59b1193c2
https://doi.org/10.1158/2767-9764.22544588.v1
https://doi.org/10.1158/2767-9764.22544588.v1
Autor:
Jo Waaler, Stefan Krauss, Anita Wegert, Ruben G.G. Leenders, Ilonka A.T.M. Meerts, Lari Lehtiö, Albert Galera-Prat, Sven T. Sowa, Gunnveig Grødeland, Hanne Scholz, Merete Høyem, Lone Holmen, Petter A. Olsen, Aleksandra Aizenshtadt, Clara Hammarström, Sandra Espada, Enya Amundsen-Isaksen, Shoshy A. Brinch
The catalytic enzymes tankyrase 1 and 2 (TNKS1/2) alter protein turnover by poly-ADP-ribosylating target proteins, which earmark them for degradation by the ubiquitin–proteasomal system. Prominent targets of the catalytic activity of TNKS1/2 includ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f93c195c48b8a1da60a3074acb0277a
https://doi.org/10.1158/2767-9764.c.6550697
https://doi.org/10.1158/2767-9764.c.6550697
Autor:
Shoshy A. Brinch, Enya Amundsen-Isaksen, Sandra Espada, Clara Hammarström, Aleksandra Aizenshtadt, Petter A. Olsen, Lone Holmen, Merete Høyem, Hanne Scholz, Gunnveig Grødeland, Sven T. Sowa, Albert Galera-Prat, Lari Lehtiö, Ilonka A.T.M. Meerts, Ruben G.G. Leenders, Anita Wegert, Stefan Krauss, Jo Waaler
Publikováno v:
Cancer Research Communications. 2:233-245
The catalytic enzymes tankyrase 1 and 2 (TNKS1/2) alter protein turnover by poly-ADP-ribosylating target proteins, which earmark them for degradation by the ubiquitin–proteasomal system. Prominent targets of the catalytic activity of TNKS1/2 includ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dca9133d4906aa167b66e485e90641cc
https://doi.org/10.1158/2767-9764.crc-22-0027
https://doi.org/10.1158/2767-9764.crc-22-0027
Autor:
Shoshy Alam Brinch, Enya Amundsen-Isaksen, Sandra Espada, Aleksandra Aizenshtadt, Lone Holmen, Clara Hammarström, Merete Høyem, Hanne Scholz, Gunnveig Grødeland, Sven T. Sowa, Albert Galera-Prat, Lari Lehtiö, Ilonka A.T.M. Meerts, Ruben G. G. Leenders, Anita Wegert, Stefan Krauss, Jo Waaler
Publikováno v:
Cancer Research. 82:2651-2651
The catalytic enzymes tankyrase 1 and 2 (TNKS1/2) poly-ADP-ribosylate target proteins, including AXIN proteins, to earmark them for degradation by the ubiquitin-proteasomal system. Hence, inhibition of TNKS1/2 can stabilize AXIN proteins, and consequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a10b3b50b9c287205f70e469b8711f7c
https://doi.org/10.1158/1538-7445.am2022-2651
https://doi.org/10.1158/1538-7445.am2022-2651
Autor:
Afaf Sahraoui, Trine Ranheim, Egil Lien, Jonas Øgaard, Arne Yndestad, Pål Aukrust, Marina Sokolova, Hanne Scholz, Merete Høyem
Publikováno v:
American Journal of Physiology-Endocrinology and Metabolism. 315:E912-E923
Inflammasomes are multiprotein inflammatory platforms that induce caspase-1 activation and subsequently interleukin (IL)-1β and IL-18 processing. The NLRP3 inflammasome is activated by different forms of oxidative stress, and, based on the central r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fc85fdff2dd8ffecc0564c6797bfd6a
https://doi.org/10.1152/ajpendo.00461.2017
https://doi.org/10.1152/ajpendo.00461.2017