Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Andrea Pichler"'
Autor:
Lukas Clemens Böckelmann, Titiksha Basu, Albert Gründer, Wei Wang, Jan Breucker, Sandra Kaiser, Andrea Pichler, Heike Luise Pahl
Publikováno v:
Haematologica, Vol 106, Iss 4 (2020)
Externí odkaz:
https://doaj.org/article/9cb5c5ce01d84a959d4140043ef76ff7
Autor:
Luigi Tortola, Roberto Nitsch, Mathieu J.M. Bertrand, Melanie Kogler, Younes Redouane, Ivona Kozieradzki, Iris Uribesalgo, Lilian M. Fennell, Mads Daugaard, Helene Klug, Gerald Wirnsberger, Reiner Wimmer, Thomas Perlot, Renu Sarao, Shuan Rao, Toshikatsu Hanada, Nozomi Takahashi, Elisabeth Kernbauer, Duygu Demiröz, Michaela Lang, Giulio Superti-Furga, Thomas Decker, Andrea Pichler, Fumiyo Ikeda, Guido Kroemer, Peter Vandenabeele, Poul H. Sorensen, Josef M. Penninger
Publikováno v:
Cell Reports, Vol 15, Iss 7, Pp 1481-1492 (2016)
Summary: The HECT domain E3 ligase HACE1 has been identified as a tumor suppressor in multiple cancers. Here, we report that HACE1 is a central gatekeeper of TNFR1-induced cell fate. Genetic inactivation of HACE1 inhibits TNF-stimulated NF-κB activa
Externí odkaz:
https://doaj.org/article/e091f3229be44c319bc3164c0e592945
Autor:
Senthilkumar Ramamoorthy, Esen Dogan, Pierre Cauchy, Andrea Pichler, Thomas Clapes, Eirini Trompouki, Gustavo Antonio Urrutia, Soeren Boller, Rudolf Grosschedl, Jorma J. Palvimo, Kyungjin Boo, Maria-Elena Torres-Padilla, Haribaskar Ramachandran
Publikováno v:
Genes Dev
Genes and Development
Genes Dev. 35, 1142-1160 (2021)
Genes and Development
Genes Dev. 35, 1142-1160 (2021)
The establishment of cell fates involves alterations of transcription factor repertoires and repurposing of transcription factors by post-translational modifications. In embryonic stem cells (ESCs), the chromatin organizers SATB2 and SATB1 balance pl
Autor:
Daniel Salas-Lloret, Coen van der Meulen, Easa Nagamalleswari, Ekaterina Gracheva, Arnoud H. de Ru, H. Anne Marie Otte, Peter A. van Veelen, Andrea Pichler, Joachim Goedhart, Alfred C.O. Vertegaal, Román González-Prieto
Ubiquitin and ubiquitin-like conjugation cascades consist of dedicated E1, E2 and E3 enzymes with E3s providing substrate specificity. Mass spectrometry-based approaches have enabled the identification of more than 60,000 acceptor sites for ubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::283c34e7480f2e8f6e614780d8c38ea8
https://doi.org/10.1101/2022.06.22.497173
https://doi.org/10.1101/2022.06.22.497173
Autor:
Wei Wang, Jan Breucker, Heike L. Pahl, Lukas Clemens Böckelmann, Albert Gründer, Andrea Pichler, Titiksha Basu, Sandra Kaiser
Publikováno v:
Haematologica
Autor:
Easa Nagamalleswari, Karishma Bakshi, Jan Breucker, Michaela Gschweitl, Román González-Prieto, Nathalie Eisenhardt, Chronis Fatouros, Viduth K Chaugule, Alfred C.O. Vertegaal, Andrea Pichler
UBC9 sumoylation (S*UBC9) in mammals contributes to SUMO target discrimination, biochemically1. Here, we present biological insights by characterizing a sumoylation mimetic UBC9-fusion (mCS~UBC9) in comparison to its wild-type (mCUBC9). We observe th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31d82ac52df161f86e4363d62f78e3e2
https://doi.org/10.1101/2022.04.11.487628
https://doi.org/10.1101/2022.04.11.487628
Autor:
Karishma Bakshi, Easa Nagamalleswari, Jan Breucker, Nathalie Eisenhardt, Richa Tiwari, Román González-Prieto, Chronis Fatouros, Viduth K Chaugule, Heekyoung Lee, Dragana Ilic, Fredrik Trulsson, Gerhard Mittler, Alfred C.O. Vertegaal, Andrea Pichler
We identified EME1, the regulatory subunit of the structure-specific endonuclease complex EME1-MUS81, as substrate for the sumoylated UBC9 and demonstrated synergistic functions in promoting Camptothecin (CPT)-induced nucleolar ribosomal DNA (rDNA) r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd4bd9d28727ccb58244b1b8b03bcd61
https://doi.org/10.1101/2022.04.11.487769
https://doi.org/10.1101/2022.04.11.487769
Publikováno v:
Methods in Enzymology
Methods in Enzymology-Ubiquitin and Ubiquitin-like Protein Modifiers
Ubiquitin and Ubiquitin-like Protein Modifiers
Methods in Enzymology-Ubiquitin and Ubiquitin-like Protein Modifiers
Ubiquitin and Ubiquitin-like Protein Modifiers
The small ubiquitin-related modifier (SUMO) is a protein of ~10kDa that is covalently conjugated to its substrate proteins in anenzymatic processcalledsumoylation. Thisposttranslational modificationis an essential regulatory mechanism that plays cruc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::459cbe109f8ccd9a528c63f5ae8b81bb
https://doi.org/10.1016/bs.mie.2018.12.025
https://doi.org/10.1016/bs.mie.2018.12.025
Autor:
Jan Breucker, Andrea Pichler
Publikováno v:
Post-Translational Modification of Proteins ISBN: 9781493990535
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5599350e2dc2c900e8b6f6fe6a3cee54
https://doi.org/10.1007/978-1-4939-9055-9_14
https://doi.org/10.1007/978-1-4939-9055-9_14
Autor:
Andrea Pichler
Publikováno v:
The EMBO journal. 37(12)
Modification of chromosomal proteins by conjugation to SUMO is a key step to cope with DNA damage and to maintain the integrity of the genome. The recruitment of SUMO E3 ligases to chromatin may represent one layer of control on protein sumoylation.