Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Anita Wegert"'
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:
Eddy Damen, Albert Galera-Prat, Piotr Nieczypor, Jo Waaler, Sudarshan Murthy, Sven T. Sowa, Sjoerd Aertssen, Ruben Gerardus George Leenders, Max Lycke, Marc Nazaré, Shoshy Alam Brinch, Stefan Krauss, Lari Lehtiö, Anita Wegert
Publikováno v:
Journal of Medicinal Chemistry
Tankyrases 1 and 2 are central biotargets in the WNT/β-catenin signaling and Hippo signaling pathways. We have previously developed tankyrase inhibitors bearing a 1,2,4-triazole moiety and binding predominantly to the adenosine binding site of the t
Autor:
Christoph Schächtele, Jan E. Ehlert, Ruben Gerardus George Leenders, Daniel Müller, Daniel Feger, Danny C. Lenstra, Jasmin Mecinović, Federica Trivarelli, Remco Zijlmans, Gerhard Müller, Bart van Bree, Anita Wegert, Marc van de Sande, Eddy Damen, Carolin Heidemann-Dinger, Michael H.G. Kubbutat
Publikováno v:
Bioorganic & Medicinal Chemistry Letters, 29, 2516-2524
Bioorganic & Medicinal Chemistry Letters, 29, 17, pp. 2516-2524
Bioorganic & Medicinal Chemistry Letters, 29, 17, pp. 2516-2524
Detailed structure activity relationship of two series of quinazoline EHMT1/EHMT2 inhibitors (UNC0224 and UNC0638) have been elaborated. New and active alternatives are presented for the ubiquitous substitution patterns found in literature for the li
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
Autor:
Ruben G. G. Leenders, Shoshy Alam Brinch, Sven T. Sowa, Enya Amundsen-Isaksen, Albert Galera-Prat, Sudarshan Murthy, Sjoerd Aertssen, Johannes N. Smits, Piotr Nieczypor, Eddy Damen, Anita Wegert, Marc Nazaré, Lari Lehtiö, Jo Waaler, Stefan Krauss
Publikováno v:
Journal of Medicinal Chemistry
Tankyrase 1 and 2 (TNKS1/2) catalyze post-translational modification by poly-ADP-ribosylation of a plethora of target proteins. In this function, TNKS1/2 also impact the WNT/β-catenin and Hippo signaling pathways that are involved in numerous human
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8427ede283b6e2e612e0c012c6a2929
http://hdl.handle.net/10852/92113
http://hdl.handle.net/10852/92113
Autor:
Richard H. Blaauw, Arthur J. Altunc, Jasmin Mecinović, Anita Wegert, Giordano Proietti, Danny C. Lenstra, Abbas H. K. Al Temimi, Yali Wang, Hong Guo, Ping Qian, Paul B. White, Helene I. V. Amatdjais-Groenen, Ruben S. Teeuwen, Vu Uyen Tran, Wansheng Ren
Publikováno v:
Temimi, A H K A, Tran, V, Teeuwen, R S, Altunc, A J, Amatdjais-Groenen, H I V, White, P B, Lenstra, D C, Proietti, G, Wang, Y, Wegert, A, Blaauw, R H, Qian, P, Ren, W, Guo, H & Mecinović, J 2020, ' Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis ', Scientific Reports, vol. 10, 3671 . https://doi.org/10.1038/s41598-020-60337-3
Scientific Reports, 10, 1-11
Scientific Reports
Scientific Reports, 10, 1, pp. 1-11
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports, 10, 1-11
Scientific Reports
Scientific Reports, 10, 1, pp. 1-11
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Methylation of lysine residues in histone proteins is catalyzed by S-adenosylmethionine (SAM)-dependent histone lysine methyltransferases (KMTs), a genuinely important class of epigenetic enzymes of biomedical interest. Here we report synthetic, mass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01f96f16f756f157284a26be88463219
https://findresearcher.sdu.dk:8443/ws/files/169051680/s41598_020_60337_3.pdf
https://findresearcher.sdu.dk:8443/ws/files/169051680/s41598_020_60337_3.pdf
Autor:
Anita Wegert, Jasmin Mecinović, Richard H. Blaauw, Abbas H. K. Al Temimi, Paul B. White, Floris P. J. T. Rutjes, Nicole G. A. van der Linden, Marcus J M Mulders
Publikováno v:
Chemical Communications
Al Temimi, A H K, White, P B, Mulders, M J M, van der Linden, N G A, Blaauw, R H, Wegert, A, Rutjes, F P J T & Mecinović, J 2020, ' Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases ', Chemical Communications, vol. 56, no. 20, pp. 3039-3042 . https://doi.org/10.1039/c9cc09098c
Chemical Communications, 56, 20, pp. 3039-3042
Chemical Communications, 56, 3039-3042
Al Temimi, A H K, White, P B, Mulders, M J M, van der Linden, N G A, Blaauw, R H, Wegert, A, Rutjes, F P J T & Mecinović, J 2020, ' Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases ', Chemical Communications, vol. 56, no. 20, pp. 3039-3042 . https://doi.org/10.1039/c9cc09098c
Chemical Communications, 56, 20, pp. 3039-3042
Chemical Communications, 56, 3039-3042
We report synthesis and enzymatic assays on human histone lysine methyltransferase catalysed methylation of histones that possess lysine and its geometrically constrained analogues containing rigid (E)-alkene (KE), (Z)-alkene (KZ) and alkyne (Kyne) m
Autor:
Renaud Bouzanne des Mazery, Dirk Schepmann, Bernhard Wünsch, Kun-Yuan Lin, Clemens Wagner, Peter Molenveld, Roy P. M. Storcken, Anita Wegert, Dieter Metze, Geert Jan Sterk, Marjon G. Bolster, Michael Soeberdt, Reshma Autar, Chih-Ching Lai, Sonja Ständer, Tai-Yu Huang, Sebastianus N. H. Aerts, Christoph Abels, Giovanni Tangherlini, Tobias Lotts, Bastian Frehland, Ulrich Knie, Frank R. van Holst
Publikováno v:
Journal of Medicinal Chemistry. 60:2526-2551
In order to develop novel κ agonists restricted to the periphery, a diastereo- and enantioselective synthesis of (4aR,5S,8aS)-configured decahydroquinoxalines 5-8 was developed. Physicochemical and pharmacological properties were fine-tuned by struc