Zobrazeno 1 - 10
of 73
pro vyhledávání: '"R Jürgen, Dohmen"'
Publikováno v:
Biomolecules, Vol 13, Iss 1, p 11 (2022)
Whereas assembly of the 20S proteasome core particle (CP) in prokaryotes apparently occurs spontaneously, the efficiency of this process in eukaryotes relies on the dedicated assembly chaperones Ump1, Pba1-Pba2, and Pba3-Pba4. For mammals, it was rep
Externí odkaz:
https://doaj.org/article/404e9b0a0e0a454bb73a25f39960d0fa
Autor:
Annie M. Sriramachandran, Katrin Meyer-Teschendorf, Stefan Pabst, Helle D. Ulrich, Niels H. Gehring, Kay Hofmann, Gerrit J. K. Praefcke, R. Jürgen Dohmen
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The cellular functions of poly-SUMO chains of different compositions are not fully understood. Here, the authors characterize Arkadia/RNF111 as a SUMO-targeted ubiquitin ligase that recognizes proteins with hybrid SUMO1-capped SUMO2/3 chains and targ
Externí odkaz:
https://doaj.org/article/d0762ab2824541ce8ce0b7085be1b113
Publikováno v:
Biomolecules, Vol 12, Iss 2, p 253 (2022)
Biogenesis of the eukaryotic 20S proteasome core particle (PC) is a complex process assisted by specific chaperones absent from the active complex. The first identified chaperone, Ump1, was found in a precursor complex (PC) called 15S PC. Yeast cells
Externí odkaz:
https://doaj.org/article/f1883ccb5d984a56a53abb6f496166d8
Autor:
Frederik Faden, Thomas Ramezani, Stefan Mielke, Isabel Almudi, Knud Nairz, Marceli S. Froehlich, Jörg Höckendorff, Wolfgang Brandt, Wolfgang Hoehenwarter, R. Jürgen Dohmen, Arp Schnittger, Nico Dissmeyer
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
Switching target protein accumulation and activity by portable conditional degrons is potentially useful for both basic research and bioengineering. Here the authors present a versatile system to tune protein levels in live animals and plants using a
Externí odkaz:
https://doaj.org/article/10f345e55eab42f3a056bfd9d5b7d2a2
Autor:
R. Jürgen Dohmen
Publikováno v:
Microbial Cell, Vol 2, Iss 10, Pp 356-359 (2015)
Externí odkaz:
https://doaj.org/article/4e0860bc66ad4ef98663da74d3b03639
Publikováno v:
Microbial Cell, Vol 2, Iss 6, Pp 197-207 (2015)
Ornithine decarboxylase (ODC), a ubiquitin-independent substrate of the proteasome, is a homodimeric protein with a rate-limiting function in polyamine biosynthesis. Polyamines regulate ODC levels by a feedback mechanism mediated by ODC antizyme (OAZ
Externí odkaz:
https://doaj.org/article/c895188ded024be5a2d2fe30ab0b50d0
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 21; Pages: 12972
Polyamines are essential biogenic poly-cations with important roles in many cellular processes and diseases such as cancer. A rate-limiting step early in the biosynthesis of polyamines is the conversion of ornithine to putrescine by the homodimeric e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14ba1c6524d76ca33225d3b38ce80dd0
Autor:
Anke M.J. Peters, Tim Niehues, Ulrich Salzer, Min Ae Lee-Kirsch, Jan de Laffolie, Brigitte Strahm, Nadja Lucas, R. Jürgen Dohmen, Ayami Yoshimi, Benjamin Becker, Paula C. Ramos, Andrea Meinhardt, Carsten Speckmann, Tomás Cunha, Stephan Ehl, Miriam Erlacher
Publikováno v:
Journal of clinical immunology, 41(7):16641667
Journal of Clinical Immunology
Journal of Clinical Immunology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cfc3c1cd5912bdd4ef59cd209a3312f
https://repository.publisso.de/resource/frl:6446043
https://repository.publisso.de/resource/frl:6446043
Autor:
Bebiana Sá-Moura, Ana Marisa Simões, Joana Fraga, Humberto Fernandes, Isabel A. Abreu, Hugo M. Botelho, Cláudio M. Gomes, António J. Marques, R. Jürgen Dohmen, Paula C. Ramos, Sandra Macedo-Ribeiro
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 7, Iss 8 (2013)
Protein degradation is essential for maintaining cellular homeostasis. The proteasome is the centralenzyme responsible for non-lysosomal protein degradation in eukaryotic cells. Although proteasome assembly is not yet completelyunderstood, a number o
Externí odkaz:
https://doaj.org/article/0ef0dca3b6c44117b9015a89ce3415b8
Publikováno v:
Methods in enzymology. 618
Covalent modification of proteins with the small ubiquitin-related modifier (SUMO) is found in all eukaryotes and is involved in many important processes. SUMO attachment may change interaction properties, subcellular localization, or stability of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d3fc82e80114fe3a7b23a618a948c537
https://pubmed.ncbi.nlm.nih.gov/30850052
https://pubmed.ncbi.nlm.nih.gov/30850052