Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Andreas Kniss"'
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 15, p 5369 (2020)
In this review, we focus on the ubiquitination process within the endoplasmic reticulum associated protein degradation (ERAD) pathway. Approximately one third of all synthesized proteins in a cell are channeled into the endoplasmic reticulum (ER) lum
Externí odkaz:
https://doaj.org/article/fa70d4d84dd8480ba1c9388917ae72cc
Autor:
Vladimir V Rogov, Alexandra Stolz, Arvind C Ravichandran, Diana O Rios‐Szwed, Hironori Suzuki, Andreas Kniss, Frank Löhr, Soichi Wakatsuki, Volker Dötsch, Ivan Dikic, Renwick CJ Dobson, David G McEwan
Publikováno v:
EMBO reports. 19
Autor:
Andreas Kniss, Vladimir V. Rogov, Sina Kazemi, Volker Dötsch, Peter Güntert, Thomas Sommer, Maren Berger, Ernst Jarosch, Frank Löhr
Publikováno v:
Journal of biomolecular NMR. 72(1-2)
Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoprote
Autor:
Sina Kazemi, Philipp E. Spindler, Vladimir V. Rogov, Thomas F. Prisner, Peter Güntert, Koraljka Husnjak, Thomas Sommer, Volker Dötsch, Ivan Dikic, Lukas Pluska, Andreas Kniss, Denise Schuetz
Publikováno v:
Structure (London, England : 1993). 26(2)
Ubiquitination is the most versatile posttranslational modification. The information is encoded by linkage type as well as chain length, which are translated by ubiquitin binding domains into specific signaling events. Chain topology determines the c
Autor:
Manuel S. Rodriguez, Andreas Kniss, Andreas Stengl, Stefan Müller, Volker Dötsch, Svenja Wiechmann, Christian Behrends, Anne Gärtner, Andreas Ernst, Vladimir V. Rogov
Publikováno v:
The Journal of biological chemistry. 292(37)
Posttranslational modifications by small ubiquitin-like modifiers (SUMOs) regulate many cellular processes, including genome integrity, gene expression, and ribosome biogenesis. The E2-conjugating enzyme Ubc9 catalyzes the conjugation of SUMOs to ϵ-
Autor:
Volker Dötsch, Terje Johansen, Åsa Birna Birgisdottir, Vladimir V. Rogov, Andreas Kniss, Jessica Huber, Vladimir Kirkin
LC3/GABARAP proteins (LC3/GABARAPs) are mammalian orthologues of yeast Atg8, small ubiquitin (Ub)-like proteins (UBLs) whose covalent attachment to lipid membranes is crucial for the growth and closure of the double membrane vesicle called the autoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8403fe4afcc8ca34e83a386983e32ad4
https://doi.org/10.1016/bs.mie.2016.10.023
https://doi.org/10.1016/bs.mie.2016.10.023
Autor:
Soichi Wakatsuki, Volker Dötsch, Andreas Kniss, Philipp Wild, David G. McEwan, Frank Löhr, Masato Kawasaki, Ryuichi Kato, Ivan Dikic, Alexis Rozenknop, Hironori Suzuki, Peter Güntert, Evgenij Fiskin, Vladimir V. Rogov
Publikováno v:
Biochemical Journal
Selective autophagy is mediated by the interaction of autophagy modifiers and autophagy receptors that also bind to ubiquitinated cargo. Optineurin is an autophagy receptor that plays a role in the clearance of cytosolic Salmonella. The interaction b
Autor:
Alexander Law, Soichi Wakatsuki, Frank Löhr, Vladimir V. Rogov, Alexandra Stolz, Andreas Kniss, Diana O. Rios-Szwed, David G. McEwan, Volker Dötsch, Arvind C. Ravicahandran, Ivan Dikic, Hironori Suzuki, Renwick C. J. Dobson
Through the canonical LC3 interaction motif (LIR), [W/F/Y]-X1-X2-[I/L/V], protein complexes are recruited to autophagosomes to perform their functions as either autophagy adaptors or receptors. How these adaptors/receptors selectively interact with e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4243d4381337ffad011c263985153831
Autor:
Andreas Kniss, Thomas Sommer, Peter Güntert, Vladimir V. Rogov, Katrin Bagola, Maximilian von Delbrück, Lukas Pluska, Volker Dötsch, Frank Löhr
Publikováno v:
Molecular Cell.
Ubiquitin conjugation is an essential process modulating protein function in eukaryotic cells. Surprisingly, little is known about how the progressive assembly of ubiquitin chains is managed by the responsible enzymes. Only recently has ubiquitin bin