Search Results - "Schorr, Stefan"

Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery by Fumagalli, Fiorenza, Noack, Julia, Bergmann, Timothy J., Cebollero, Eduardo, Pisoni, Giorgia Brambilla, Fasana, Elisa, Fregno, Ilaria, Galli, Carmela, Loi, Marisa, Soldà, Tatiana, D’Antuono, Rocco, Raimondi, Andrea, Jung, Martin, Melnyk, Armin, Schorr, Stefan, Schreiber, Anne, Simonelli, Luca, Varani, Luca, Wilson-Zbinden, Caroline, Zerbe, Oliver, Hofmann, Kay, Peter, Matthias, Quadroni, Manfredo, Zimmermann, Richard, Molinari, Maurizio

“…The endoplasmic reticulum (ER) is a site of protein biogenesis in eukaryotic cells. Perturbing ER homeostasis activates stress programs collectively called the…”
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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum by Aviram, Naama, Ast, Tslil, Costa, Elizabeth A., Arakel, Eric C., Chuartzman, Silvia G., Jan, Calvin H., Haßdenteufel, Sarah, Dudek, Johanna, Jung, Martin, Schorr, Stefan, Zimmermann, Richard, Schwappach, Blanche, Weissman, Jonathan S., Schuldiner, Maya

“…Experiments in yeast cells show that three proteins—Snd1, Snd2 and Snd3—provide an alternative pathway for targeting of cellular proteins to the endoplasmic…”
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Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import by Nguyen, Duy, Stutz, Regine, Schorr, Stefan, Lang, Sven, Pfeffer, Stefan, Freeze, Hudson H., Förster, Friedrich, Helms, Volkhard, Dudek, Johanna, Zimmermann, Richard

“…In mammalian cells, one-third of all polypeptides are transported into or across the ER membrane via the Sec61 channel. While the Sec61 complex facilitates…”
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Identification of signal peptide features for substrate specificity in human Sec62/Sec63‐dependent ER protein import by Schorr, Stefan, Nguyen, Duy, Haßdenteufel, Sarah, Nagaraj, Nagarjuna, Cavalié, Adolfo, Greiner, Markus, Weissgerber, Petra, Loi, Marisa, Paton, Adrienne W., Paton, James C., Molinari, Maurizio, Förster, Friedrich, Dudek, Johanna, Lang, Sven, Helms, Volkhard, Zimmermann, Richard

“…In mammalian cells, one‐third of all polypeptides are integrated into the membrane or translocated into the lumen of the endoplasmic reticulum (ER) via the…”
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hSnd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells by Haßdenteufel, Sarah, Sicking, Mark, Schorr, Stefan, Aviram, Naama, Fecher‐Trost, Claudia, Schuldiner, Maya, Jung, Martin, Zimmermann, Richard, Lang, Sven

“…Recently, understanding of protein targeting to the endoplasmic reticulum (ER) was expanded by the discovery of multiple pathways that function in parallel to…”
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Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon by Pfeffer, Stefan, Dudek, Johanna, Gogala, Marko, Schorr, Stefan, Linxweiler, Johannes, Lang, Sven, Becker, Thomas, Beckmann, Roland, Zimmermann, Richard, Förster, Friedrich

“…In mammalian cells, proteins are typically translocated across the endoplasmic reticulum (ER) membrane in a co-translational mode by the ER protein translocon,…”
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Quantitative Proteomics and Differential Protein Abundance Analysis after Depletion of Putative mRNA Receptors in the ER Membrane of Human Cells Identifies Novel Aspects of mRNA Targeting to the ER by Bhadra, Pratiti, Schorr, Stefan, Lerner, Monika, Nguyen, Duy, Dudek, Johanna, Förster, Friedrich, Helms, Volkhard, Lang, Sven, Zimmermann, Richard

“…In human cells, one-third of all polypeptides enter the secretory pathway at the endoplasmic reticulum (ER). The specificity and efficiency of this process are…”
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AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum by Klein, Marie-Christine, Zimmermann, Katharina, Schorr, Stefan, Landini, Martina, Klemens, Patrick A. W., Altensell, Jacqueline, Jung, Martin, Krause, Elmar, Nguyen, Duy, Helms, Volkhard, Rettig, Jens, Fecher-Trost, Claudia, Cavalié, Adolfo, Hoth, Markus, Bogeski, Ivan, Neuhaus, H. Ekkehard, Zimmermann, Richard, Lang, Sven, Haferkamp, Ilka

“…To fulfill its role in protein biogenesis, the endoplasmic reticulum (ER) depends on the Hsp70-type molecular chaperone BiP, which requires a constant ATP…”
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BiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ER by Schäuble, Nico, Lang, Sven, Jung, Martin, Cappel, Sabine, Schorr, Stefan, Ulucan, Özlem, Linxweiler, Johannes, Dudek, Johanna, Blum, Robert, Helms, Volkhard, Paton, Adrienne W, Paton, James C, Cavalié, Adolfo, Zimmermann, Richard

“…In mammalian cells, signal peptide‐dependent protein transport into the endoplasmic reticulum (ER) is mediated by a dynamic protein‐conducting channel, the…”
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Absence of BiP Co-chaperone DNAJC3 Causes Diabetes Mellitus and Multisystemic Neurodegeneration by Synofzik, Matthis, Haack, Tobias B., Kopajtich, Robert, Gorza, Matteo, Rapaport, Doron, Greiner, Markus, Schönfeld, Caroline, Freiberg, Clemens, Schorr, Stefan, Holl, Reinhard W., Gonzalez, Michael A., Fritsche, Andreas, Fallier-Becker, Petra, Zimmermann, Richard, Strom, Tim M., Meitinger, Thomas, Züchner, Stephan, Schüle, Rebecca, Schöls, Ludger, Prokisch, Holger

“…Diabetes mellitus and neurodegeneration are common diseases for which shared genetic factors are still only partly known. Here, we show that loss of the BiP…”
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Erratum: Corrigendum: Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery by Fumagalli, Fiorenza, Noack, Julia, Bergmann, Timothy J., Cebollero, Eduardo, Pisoni, Giorgia Brambilla, Fasana, Elisa, Fregno, Ilaria, Galli, Carmela, Loi, Marisa, Soldà, Tatiana, D'Antuono, Rocco, Raimondi, Andrea, Jung, Martin, Melnyk, Armin, Schorr, Stefan, Schreiber, Anne, Simonelli, Luca, Varani, Luca, Wilson-Zbinden, Caroline, Zerbe, Oliver, Hofmann, Kay, Peter, Matthias, Quadroni, Manfredo, Zimmermann, Richard, Molinari, Maurizio

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Integrative functions of the mitochondrial contact site and cristae organizing system by Schorr, Stefan, van der Laan, Martin

“…Mitochondria are complex double-membrane-bound organelles of eukaryotic cells that function as energy-converting powerhouses, metabolic factories and signaling…”
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Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells by Lang, Sven, Benedix, Julia, Fedeles, Sorin V, Schorr, Stefan, Schirra, Claudia, Schäuble, Nico, Jalal, Carolin, Greiner, Markus, Hassdenteufel, Sarah, Tatzelt, Jörg, Kreutzer, Birgit, Edelmann, Ludwig, Krause, Elmar, Rettig, Jens, Somlo, Stefan, Zimmermann, Richard, Dudek, Johanna

“…Co-translational transport of polypeptides into the endoplasmic reticulum (ER) involves the Sec61 channel and additional components such as the ER lumenal…”
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Targeting cell migration and the endoplasmic reticulum stress response with calmodulin antagonists: a clinically tested small molecule phenocopy of SEC62 gene silencing in human tumor cells by Linxweiler, Maximilian, Schorr, Stefan, Schäuble, Nico, Jung, Martin, Linxweiler, Johannes, Langer, Frank, Schäfers, Hans-Joachim, Cavalié, Adolfo, Zimmermann, Richard, Greiner, Markus

“…Tumor cells benefit from their ability to avoid apoptosis and invade other tissues. The endoplasmic reticulum (ER) membrane protein Sec62 is a key player in…”
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hS nd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells by Haßdenteufel, Sarah, Sicking, Mark, Schorr, Stefan, Aviram, Naama, Fecher‐Trost, Claudia, Schuldiner, Maya, Jung, Martin, Zimmermann, Richard, Lang, Sven

“…Recently, understanding of protein targeting to the endoplasmic reticulum ( ER ) was expanded by the discovery of multiple pathways that function in parallel…”
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Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum by Schorr, Stefan, Klein, Marie-Christine, Gamayun, Igor, Melnyk, Armin, Jung, Martin, Schäuble, Nico, Wang, Qian, Hemmis, Birgit, Bochen, Florian, Greiner, Markus, Lampel, Pavel, Urban, Sabine Katharina, Hassdenteufel, Sarah, Dudek, Johanna, Chen, Xing-Zhen, Wagner, Richard, Cavalié, Adolfo, Zimmermann, Richard

“…In mammalian cells, signal peptide-dependent protein transport into the endoplasmic reticulum (ER) is mediated by a dynamic polypeptide-conducting channel, the…”
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Sec62 as a novel gating modulator for protein translocation and ion permeability of the mammalian Sec61 complex (LB196) by Schorr, Stefan, Linxweiler, Maximilian, Greiner, Markus, Jung, Martin, Cavalie, Adolfo, Zimmermann, Richard

“…In mammalian cells the endoplasmic reticulum (ER) plays a key role during the biogenesis of secretory and membrane proteins and acts as a major regulator for…”
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Resource Management on Multicore Systems: The ACTORS Approach by Bini, E, Buttazzo, G, Eker, J, Schorr, S, Guerra, R, Fohler, G, Arzen, Karl-Erik, Romero, V, Scordino, C

“…High-performance embedded systems require the execution of many applications on multicore platforms and are subject to stringent restrictions and constraints…”
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Correction: Corrigendum: Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery by Fumagalli, Fiorenza, Noack, Julia, Bergmann, Timothy J., Cebollero, Eduardo, Pisoni, Giorgia Brambilla, Fasana, Elisa, Fregno, Ilaria, Galli, Carmela, Loi, Marisa, Soldà, Tatiana, D'Antuono, Rocco, Raimondi, Andrea, Jung, Martin, Melnyk, Armin, Schorr, Stefan, Schreiber, Anne, Simonelli, Luca, Varani, Luca, Wilson-Zbinden, Caroline, Zerbe, Oliver, Hofmann, Kay, Peter, Matthias, Quadroni, Manfredo, Zimmermann, Richard, Molinari, Maurizio

“…Nature Cell Biology 18, 1173–1184 (2016); published online 17 October 2016; corrected after print 18 November 2016. In the version of this Article originally…”
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Corrigendum: Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery by Fumagalli, Fiorenza, Noack, Julia, Bergmann, Timothy J, Cebollero, Eduardo, Pisoni, Giorgia Brambilla, Fasana, Elisa, Fregno, Ilaria, Galli, Carmela, Loi, Marisa, Soldà, Tatiana, D'Antuono, Rocco, Raimondi, Andrea, Jung, Martin, Melnyk, Armin, Schorr, Stefan, Schreiber, Anne, Simonelli, Luca, Varani, Luca, Wilson-Zbinden, Caroline, Zerbe, Oliver, Hofmann, Kay, Peter, Matthias, Quadroni, Manfredo, Zimmermann, Richard, Molinari, Maurizio

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