Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Willem J. van Dijk"'
Autor:
Robbert Q. Kim, Paul P. Geurink, Monique P. C. Mulder, Alexander Fish, Reggy Ekkebus, Farid El Oualid, Willem J. van Dijk, Duco van Dalen, Huib Ovaa, Hugo van Ingen, Titia K. Sixma
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a
Externí odkaz:
https://doaj.org/article/822bd4cb8eb04f3199afc82488ed53d3
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
The tumor suppressor BAP1 is activated by ASXL1 to deubiquitinate mono-ubiquitinated H2A at K119 in Polycomb gene repression. Here, the authors show how BAP1’s C-terminal extension auto-recruits it to nucleosomes, where the DEUBAD domain of ASXL1 i
Externí odkaz:
https://doaj.org/article/0ea8dc04cd7544a2834c03123e450572
Publikováno v:
EMBO Reports
During DNA replication, the deubiquitinating enzyme USP1 limits the recruitment of translesion polymerases by removing ubiquitin marks from PCNA to allow specific regulation of the translesion synthesis (TLS) pathway. USP1 activity depends on an allo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e1f0332c9c27125d26a750f484bdee
https://doi.org/10.15252/embr.202051749
https://doi.org/10.15252/embr.202051749
Publikováno v:
The Journal of Biological Chemistry
Background: Linear ubiquitination of NEMO by LUBAC is important for NF-κB activation. Results: HOIP and the “top” of ubiquitin are essential for linear ubiquitination, whereas NEMO ubiquitination additionally requires HOIL-1L. Conclusion: NEMO p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::016da3d898419bd93fe9ea5b54d96b2d
https://doi.org/10.1074/jbc.m113.495846
https://doi.org/10.1074/jbc.m113.495846
Publikováno v:
Journal of structural biology. 195(1)
Ubiquitin conjugation is an important signal in cellular pathways, changing the fate of a target protein, by degradation, relocalisation or complex formation. These signals are balanced by deubiquitinating enzymes (DUBs), which antagonize ubiquitinat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cab6dda9866b263cb5b951b7b465383c
https://pubmed.ncbi.nlm.nih.gov/27183903
https://pubmed.ncbi.nlm.nih.gov/27183903
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
The deubiquitinating enzyme BAP1 is an important tumor suppressor that has drawn attention in the clinic since its loss leads to a variety of cancers. BAP1 is activated by ASXL1 to deubiquitinate mono-ubiquitinated H2A at K119 in Polycomb gene repres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0080e2992fd29546b127133145fa4562
http://europepmc.org/articles/PMC4729829
http://europepmc.org/articles/PMC4729829
Autor:
Sylvie M. Noordermeer, Davide Monteferrario, Bert A. van der Reijden, Willem J. van Dijk, Judith J. Smit, Titia K. Sixma
Publikováno v:
The EMBO Journal. 31:3833-3844
Activation of the NF-κB pathway requires the formation of Met1-linked 'linear' ubiquitin chains on NEMO, which is catalysed by the Linear Ubiquitin Chain Assembly Complex (LUBAC) E3 consisting of HOIP, HOIL-1L and Sharpin. Here, we show that both LU
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e111be2aec4a1c0ae9b06a9c89fcc077
https://doi.org/10.1038/emboj.2012.217
https://doi.org/10.1038/emboj.2012.217
Autor:
Francesca Mattiroli, Wim Vermeulen, Pauline Ikpa, Elisabetta Citterio, Titia K. Sixma, Jurgen A. Marteijn, Willem J. van Dijk, Joseph H.A. Vissers
Publikováno v:
Cell, 150(6), 1182-1195. Cell Press
SummaryUbiquitin-dependent signaling during the DNA damage response (DDR) to double-strand breaks (DSBs) is initiated by two E3 ligases, RNF8 and RNF168, targeting histone H2A and H2AX. RNF8 is the first ligase recruited to the damage site, and RNF16
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a355b98cfd23e3f2fb97c95f1d57ccfd
https://hdl.handle.net/1765/54870
https://hdl.handle.net/1765/54870
Autor:
Mark P.A. Luna-Vargas, Michael Rape, Titia K. Sixma, Alexander Fish, Alex C. Faesen, Willem J. van Dijk
Publikováno v:
EMBO Reports
Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain The ubiquitin-specific protease Usp4 contains an autoinhibitory Ubl domain in its catalytic domain. Inhibition can be relieved by interaction with a non-active USP, such as USP39
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57e56a4de07ed5289950b5b818014be0
https://doi.org/10.1038/embor.2011.33
https://doi.org/10.1038/embor.2011.33
Autor:
Helene Klug, Alexander Fish, Erica S. Johnson, Willem J. van Dijk, Annette Flotho, Jesper V. Olsen, Matthias Mann, Titia K. Sixma, Puck Knipscheer, Andrea Pichler
Publikováno v:
Molecular Cell. 31(3):371-382
Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ae4e90461eb6c5cdd551430c1ba7172