Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ilonka A.T.M. Meerts"'
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
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