Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Maximilian J. Kern"'
Autor:
Maria Körner, Susanne R Meyer, Gabriella Marincola, Maximilian J Kern, Clemens Grimm, Christina Schuelein-Voelk, Utz Fischer, Kay Hofmann, Alexander Buchberger
Publikováno v:
eLife, Vol 12 (2023)
The ATPase p97 (also known as VCP, Cdc48) has crucial functions in a variety of important cellular processes such as protein quality control, organellar homeostasis, and DNA damage repair, and its de-regulation is linked to neuromuscular diseases and
Externí odkaz:
https://doaj.org/article/088885aee7b845c49c72985154a87b7b
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
SCIENTIFIC REPORTS
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
SCIENTIFIC REPORTS
RNA polymerase II (RNAPII) is the workhorse of eukaryotic transcription and produces messenger RNAs and small nuclear RNAs. Stalling of RNAPII caused by transcription obstacles such as DNA damage threatens functional gene expression and is linked to
Autor:
Bianca Habermann, Roman Prytuliak, Markus Höpfler, Stefan Jentsch, Boris Pfander, Tobias Straub, Maximilian J. Kern
Publikováno v:
EMBO Journal
EMBO Journal, EMBO Press, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
The EMBO Journal
EMBO Journal, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
EMBO Journal, EMBO Press, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
The EMBO Journal
EMBO Journal, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
International audience; Chromatin is a highly regulated environment, and protein association with chromatin is often controlled by post-translational modifications and the corresponding enzymatic machinery. Specifically, SUMO-targeted ubiquitin ligas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::737e644ecb2af4e4e9ed05accc7266fd
https://hal.archives-ouvertes.fr/hal-02369006/file/Hoepfler_EMBJ-38-e100368.pdf
https://hal.archives-ouvertes.fr/hal-02369006/file/Hoepfler_EMBJ-38-e100368.pdf
Autor:
Steven Bergink, Stefan Jentsch, Maximilian J. Kern, Lothar Schermelleh, Tim Ammon, Heinrich Leonhardt
Publikováno v:
Nature Cell Biology, 15(5), 526-+. Nature Publishing Group
Cdc48 (also known as p97), a conserved chaperone-like ATPase, plays a strategic role in the ubiquitin system(1-3). Empowered by ATP-driven conformational changes(4), Cdc48 acts as a segregase by dislodging ubiquitylated proteins from their environmen
Autor:
Maximilian J. Kern, James Titchmarsh, Annekathrin von Hacht, Stuart L. Warriner, Lenz R. Steimer, James C.A. Bardwell, Sheena E. Radford, Linda Foit, Gareth J. Morgan
Publikováno v:
Molecular Cell. 36:861-871
Identifying mutations that stabilize proteins is challenging because most substitutions are destabilizing. In addition to being of immense practical utility, the ability to evolve protein stability in vivo may indicate how evolution has formed today'
Publikováno v:
Biochemical and biophysical research communications. 380(2)
The chaperone-related p97 protein plays a central role in various cellular processes involving the ubiquitin-proteasome system. The diverse functions of p97 are controlled by a large number of cofactors that recruit specific substrates or influence t