Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Dönem Avci"'
Autor:
Andrea Zanotti, João P. L. Coelho, Dinah Kaylani, Gurdeep Singh, Marina Tauber, Manuel Hitzenberger, Dönem Avci, Martin Zacharias, Robert B. Russell, Marius K. Lemberg, Matthias J. Feige
Publikováno v:
Science (New York, N.Y.). 378(6623)
Cells need to detect and degrade faulty membrane proteins to maintain homeostasis. In this study, we identify a previously unknown function of the human signal peptidase complex (SPC)—the enzyme that removes endoplasmic reticulum (ER) signal peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebb1342bb70c0289f2e44fda26fe4eca
https://pubmed.ncbi.nlm.nih.gov/36454823
https://pubmed.ncbi.nlm.nih.gov/36454823
Autor:
Hester A. Beard, Christian Lüchtenborg, Marta Barniol-Xicota, Dipali Kale, Britta Brügger, Marius K. Lemberg, Dönem Avci, Ronny Heidasch, Bernd Schröder, Steven H. L. Verhelst, Torben Mentrup
Intramembrane proteolysis regulates important processes such as signaling and transcriptional and posttranslational abundance control of proteins with key functions in metabolic pathways. This includes transcriptional control of mevalonate pathway ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cfbf125666e1a7d4c2ac8c9c5ee55030
https://doi.org/10.1101/2021.07.19.452877
https://doi.org/10.1101/2021.07.19.452877
Autor:
Ronny Heidasch, Karsten Richter, Michelle Neßling, Holger Lorenz, Nicole S. Malchus, Marius K. Lemberg, Dönem Avci
Publikováno v:
The Journal of biological chemistry. 294(8)
The endoplasmic reticulum (ER), as a multifunctional organelle, plays crucial roles in lipid biosynthesis and calcium homeostasis as well as the synthesis and folding of secretory and membrane proteins. Therefore, it is of high importance to maintain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::189f74460303004cf08b6093f56920ce
https://pubmed.ncbi.nlm.nih.gov/30578301
https://pubmed.ncbi.nlm.nih.gov/30578301
Autor:
Dönem Avci, Marius K. Lemberg
Publikováno v:
Trends in Cell Biology. 25:611-622
Protein degradation is a fundamentally important process that allows cells to recognize and remove damaged protein species and to regulate protein abundance according to functional need. A fundamental challenge is to understand how membrane proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07383cb2aef291523a445e24bbb24098
https://doi.org/10.1016/j.tcb.2015.07.003
https://doi.org/10.1016/j.tcb.2015.07.003
Autor:
Bianca Schrul, Dönem Avci, Oliver Schilling, Maya Schuldiner, Akio Fukumori, Elisabeth Kremmer, Marius K. Lemberg, Chia-yi Chen, Michal Breker, Harald Steiner, Martin L. Biniossek, Idan Frumkin, Shai Fuchs
Publikováno v:
Mol. Cell 56, 630-640 (2014)
Molecular cell 56(5), 630-640 (2014). doi:10.1016/j.molcel.2014.10.012
Molecular cell 56(5), 630-640 (2014). doi:10.1016/j.molcel.2014.10.012
Summary Proteolysis by aspartyl intramembrane proteases such as presenilin and signal peptide peptidase (SPP) underlies many cellular processes in health and disease. Saccharomyces cerevisiae encodes a homolog that we named yeast presenilin fold 1 (Y
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a66714995f0d6599f2e25ab6d2987cd3
Autor:
John C. Christianson, Lena-Sophie Dreher, Jasmin Schulz, Emma J. Fenech, Dönem Avci, Thorsten Hoppe, Yuki Hayashi, Norbert Volkmar, Markus A. Queisser, Aljona Gutschmidt
The mammalian ubiquitin ligase Hrd1 is the central component of a complex facilitating degradation of misfolded proteins during the ubiquitin–proteasome-dependent process of ER-associated degradation (ERAD). Hrd1 associates with cofactors to execut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8cea0ffb7b2f0c330ba2e82f080440a
https://doi.org/10.1242/jcs.206847
https://doi.org/10.1242/jcs.206847
Autor:
Dönem Avci, Beate Hehn, Chia-yi Chen, Dieter Langosch, Nicole S. Malchus, Marius K. Lemberg, Walter Stelzer
Publikováno v:
The EMBO Journal. 33:2492-2506
Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of signal peptides at the endoplasmic reticulum (ER), but has also been suggested to play a role in ER-associated degradation (ERAD). Here, we show that SPP forms a complex with the E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57246d751801f7cafd46142eb345310e
https://doi.org/10.15252/embj.201488208
https://doi.org/10.15252/embj.201488208
Autor:
Dönem Avci, Marius K. Lemberg
Publikováno v:
Molecular Cell. 69:161-162
Defective ER-resident membrane proteins need to be ejected into the cytoplasm in order to be degraded by the proteasome, but the exact mechanism remains unclear. In this issue of Molecular Cell, Neal et al. (2018) reveal that the rhomboid pseudoprote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::26963bfc0369d01d1ccc3a23c4d3f440
https://doi.org/10.1016/j.molcel.2017.12.031
https://doi.org/10.1016/j.molcel.2017.12.031
Autor:
Dönem Avci, Oliver Schilling, Oliver Serang, Marius K. Lemberg, Lars Nilse, Patrick Heisterkamp
Publikováno v:
Biochimica et biophysica acta. 1864(10)
We describe in detail the usage of leucine metabolic labelling in yeast in order to monitor quantitative proteome alterations, e.g. upon removal of a protease. Since laboratory yeast strains are typically leucine auxotroph, metabolic labelling with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe97e7bbcde67bd8ef0181377a869952
https://pubmed.ncbi.nlm.nih.gov/27426920
https://pubmed.ncbi.nlm.nih.gov/27426920