Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Anne-Marie B. Lauridsen"'
Autor:
Isabelle Jourdain, Rasmus Hartmann-Petersen, Amanda B Abildgaard, Anne-Marie B. Lauridsen, Caroline Kampmeyer, Signe M. Schenstrøm, Antonina Karakostova
Exocytosis involves fusion of secretory vesicles with the plasma membrane, thereby delivering membrane proteins to the cell surface and releasing material into the extracellular space. The tethering of the secretory vesicles before membrane fusion is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fa118ba213c9bf728a45eb5d9ec949b
https://europepmc.org/articles/PMC5602385/
https://europepmc.org/articles/PMC5602385/
Autor:
Rasmus Hartmann-Petersen, Yasushi Saeki, Michael Seeger, Keiji Tanaka, Anne-Marie B. Lauridsen, Klavs B. Hendil, Franziska Kriegenburg
Publikováno v:
Cell. 135:355-365
SummaryIt has been suggested that degradation of polyubiquitylated proteins is coupled to dissociation of 26S proteasomes. In contrast, using several independent types of experiments, we find that mammalian proteasomes can degrade polyubiquitylated p
Autor:
Esben G. Poulsen, Anne-Marie B. Lauridsen, Michael Lees, Cornelia Steinhauer, Lars Ellgaard, Rasmus Hartmann-Petersen
Publikováno v:
Poulsen, E G, Steinhauer, C, Lees, M, Lauridsen, A-M, Ellgaard, L & Hartmann-Petersen, R 2012, ' HUWE1 and TRIP12 Collaborate in Degradation of Ubiquitin-Fusion Proteins and Misframed Ubiquitin ', P L o S One, vol. 7, no. 11 . https://doi.org/10.1371/journal.pone.0050548
PLoS ONE, Vol 7, Iss 11, p e50548 (2012)
PLoS ONE
PLoS ONE, Vol 7, Iss 11, p e50548 (2012)
PLoS ONE
In eukaryotic cells an uncleavable ubiquitin moiety conjugated to the N-terminus of a protein signals the degradation of the fusion protein via the proteasome-dependent ubiquitin fusion degradation (UFD) pathway. In yeast the molecular mechanism of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2905f14c557ded4ff3c1f8ae7cd9ce41
https://curis.ku.dk/portal/da/publications/huwe1-and-trip12-collaborate-in-degradation-of-ubiquitinfusion-proteins-and-misframed-ubiquitin(efa9e7ce-56d8-44f7-b984-36905bde2f84).html
https://curis.ku.dk/portal/da/publications/huwe1-and-trip12-collaborate-in-degradation-of-ubiquitinfusion-proteins-and-misframed-ubiquitin(efa9e7ce-56d8-44f7-b984-36905bde2f84).html
Autor:
Camilla Steen Jensen, Colin Gordon, Anne-Marie B. Lauridsen, Rasmus Hartmann-Petersen, Franziska Kriegenburg, Katrine M. Andersen
Publikováno v:
Antioxidantsredox signaling. 14(9)
The 26S proteasome is a large proteolytic particle present in the cytosol and nucleus of eukaryotic cells. Most intracellular proteins, including those affected by oxidative damage, are degraded by the proteasome. The human thioredoxin, Txnl1, is kno
Autor:
Rasmus Hartmann-Petersen, Keiji Tanaka, Shigeo Murata, Anne-Marie B. Lauridsen, Klavs B. Hendil, Franziska Kriegenburg, Anders H. Johnsen
Publikováno v:
Journal of molecular biology. 394(2)
26S proteasomes consist of cylindrical 20S proteasomes with 19S regulatory complexes attached to the ends. Treatment with high concentrations of salt causes the regulatory complexes to separate into two sub-complexes, the base, which is in contact wi
Autor:
Anders H. Johnsen, Poul Kristensen, Klavs B. Hendil, Karen Dissing, Anne-Marie B. Lauridsen, Rasmus Hartmann-Petersen, Jakob Ploug Jørgensen
Publikováno v:
Journal of molecular biology. 360(5)
We have identified Adrm1 as a novel component of the regulatory ATPase complex of the 26 S proteasome: Adrm1 was precipitated with an antibody to proteasomes and vice versa. Adrm1 co-migrated with proteasomes on gel-filtration chromatography and non-
Autor:
Katrine M. Andersen, Camilla Jensen, Franziska Kriegenburg, Anne-Marie B. Lauridsen, Colin Gordon, Rasmus Hartmann-Petersen
Publikováno v:
Antioxidants & Redox Signaling; May2011, Vol. 14 Issue 9, p1601-1608, 8p