Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Karolin Eifler"'
Autor:
Prabhavathi Talloji, Lilian Nehlin, Bruno Hüttel, Nikola Winter, Martin Černý, Hana Dufková, Bulut Hamali, Katarzyna Hanczaryk, Jan Novák, Monika Hermanns, Nicole Drexler, Karolin Eifler, Nikolaus Schlaich, Břetislav Brzobohatý, Andreas Bachmair
Publikováno v:
BMC Plant Biology, Vol 22, Iss 1, Pp 1-17 (2022)
Abstract Background Many regulatory circuits in plants contain steps of targeted proteolysis, with the ubiquitin proteasome system (UPS) as the mediator of these proteolytic events. In order to decrease ubiquitin-dependent proteolysis, we inducibly e
Externí odkaz:
https://doaj.org/article/1a145092771f4ed8bc85202fd630f9f3
Autor:
Karolin Eifler, Sabine A. G. Cuijpers, Edwin Willemstein, Jonne A. Raaijmakers, Dris El Atmioui, Huib Ovaa, René H. Medema, Alfred C. O. Vertegaal
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Signal transduction by small ubiquitin-like modifier (SUMO) is important for cell cycle progression. Here the authors show that SUMOylation regulates the APC/C complex, a master orchestrator of metaphase to anaphase transition, with consequences for
Externí odkaz:
https://doaj.org/article/5797f95b8c1741f1b90f2f7c055ba779
Autor:
Prabhavathi Talloji, Lilian Nehlin, Bruno Hüttel, Nikola Winter, Martin Černý, Hana Dufková, Bulut Hamali, Katarzyna Hanczaryk, Jan Novák, Monika Hermanns, Nicole Drexler, Karolin Eifler, Nikolaus Schlaich, Břetislav Brzobohatý, Andreas Bachmair
Publikováno v:
BMC plant biology 22, 183 (2022). doi:10.1186/s12870-022-03536-6
BMC plant biology 22, 183 (2022). doi:10.1186/s12870-022-03536-6
Published by BioMed Central, London
Published by BioMed Central, London
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d97778905d5bfed2a58ec5054e12bb62
https://pubmed.ncbi.nlm.nih.gov/35395773
https://pubmed.ncbi.nlm.nih.gov/35395773
Autor:
Sabine A.G. Cuijpers, Edwin Willemstein, René H. Medema, Jonne A. Raaijmakers, Dris El Atmioui, Karolin Eifler, Alfred C.O. Vertegaal, Huib Ovaa
Publikováno v:
Nature Communications
Nature Communications, 9
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Nature Communications, 9
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Signal transduction by small ubiquitin-like modifier (SUMO) regulates a myriad of nuclear processes. Here we report on the role of SUMO in mitosis in human cell lines. Knocking down the SUMO conjugation machinery results in a delay in mitosis and def
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31ff01cdcf16a4d10d91acc7047bf1bc
http://europepmc.org/articles/PMC5856775
http://europepmc.org/articles/PMC5856775
Publikováno v:
Advances in experimental medicine and biology. 963
Like in most other areas of cellular metabolism, the functions of the ubiquitin-like modifier SUMO in the maintenance of genome stability are manifold and varied. Perturbations of global sumoylation causes a wide spectrum of phenotypes associated wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::97c95a71308b53cdfb8c3f3aad3f2804
https://pubmed.ncbi.nlm.nih.gov/28197906
https://pubmed.ncbi.nlm.nih.gov/28197906
Publikováno v:
SUMO Regulation of Cellular Processes ISBN: 9783319500430
Like in most other areas of cellular metabolism, the functions of the ubiquitin-like modifier SUMO in the maintenance of genome stability are manifold and varied. Perturbations of global sumoylation causes a wide spectrum of phenotypes associated wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52fe49b6ec0b8606d217f4dcbdf04d5c
https://doi.org/10.1007/978-3-319-50044-7_4
https://doi.org/10.1007/978-3-319-50044-7_4
Autor:
Karolin Eifler, Alfred C.O. Vertegaal
Publikováno v:
Trends in Biochemical Sciences, 40(12), 779-793
Protein conjugation with Small ubiquitin-like modifier (SUMOylation) has critical roles during cell cycle progression. Many important cell cycle regulators, including many oncogenes and tumor suppressors, are functionally regulated via SUMOylation. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::919f29287249a2b6ddaf07040e9473a4
https://hdl.handle.net/1887/105634
https://hdl.handle.net/1887/105634
Publikováno v:
Journal of Biological Chemistry, 290(25), 15526-15537
Ring finger protein 4 (RNF4) is a SUMO-targeted ubiquitin E3 ligase with a pivotal function in the DNA damage response (DDR). SUMO interaction motifs (SIMs) in the N-terminal part of RNF4 tightly bind to SUMO polymers, and RNF4 can ubiquitinate these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e94246adb8d190296e99a520c9d4b73
https://hdl.handle.net/1887/103004
https://hdl.handle.net/1887/103004
Autor:
Konstantin, Tomanov, Anja, Zeschmann, Rebecca, Hermkes, Karolin, Eifler, Ionida, Ziba, Michele, Grieco, Maria, Novatchkova, Kay, Hofmann, Holger, Hesse, Andreas, Bachmair
The Arabidopsis thaliana genes PROTEIN INHIBITOR OF ACTIVATED STAT LIKE1 (PIAL1) and PIAL2 encode proteins with SP-RING domains, which occur in many ligases of the small ubiquitin-related modifier (SUMO) conjugation pathway. We show that PIAL1 and PI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::061f8d86395e5df5df244f09a520130d
https://europepmc.org/articles/PMC4277223/
https://europepmc.org/articles/PMC4277223/
Autor:
Ivo A. Hendriks, Joost Schimmel, René H. Medema, Sabine A.G. Cuijpers, Karolin Eifler, Christian D. Kelstrup, Chiara Francavilla, Alfred C.O. Vertegaal, Jesper V. Olsen, Matty Verlaan-de Vries, Jón Otti Sigurðsson
Publikováno v:
Molecular Cell, 53(6), 1053-1066
Loss of small ubiquitin-like modification (SUMOylation) in mice causes genomic instability due to the missegregation of chromosomes. Currently, little is known about the identity of relevant SUMO target proteins that are involved in this process and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a8cd21b624f09c5c6195447de70534e
https://hdl.handle.net/1887/104856
https://hdl.handle.net/1887/104856