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Thomas Sommer

Max-Delbrück-Center for Molecular Medicine Friedrich-Wilhelms-Universität zu Berlin, Berlin, Prussia, Germany 
Intracellular Proteolysis
"Thomas Sommer"
Cross-listing: Chemistry Tree


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Vincenzo E. A. Russo grad student 1988 FU Berlin (Chemistry Tree)
 (Klonierung und Charakterisierung blaulichtregulierter Gene von Neurospora crassa)
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Christianson JC, Jarosch E, Sommer T. (2023) Mechanisms of substrate processing during ER-associated protein degradation. Nature Reviews. Molecular Cell Biology
Brodsky JL, Engelman DM, Hendershot LM, et al. (2022) Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum. Faculty Reviews. 11: 29
Pfeiffer A, Stephanowitz H, Krause E, et al. (2016) A complex of Htm1 and the oxidoreductase Pdi1 accelerates degradation of misfolded glycoproteins. The Journal of Biological Chemistry
Mehnert M, Sommermeyer F, Berger M, et al. (2015) The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins. Molecular Biology of the Cell. 26: 185-94
Mehnert M, Sommer T, Jarosch E. (2014) Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane. Nature Cell Biology. 16: 77-86
Hampton RY, Sommer T. (2012) Finding the will and the way of ERAD substrate retrotranslocation. Current Opinion in Cell Biology. 24: 460-6
Bagola K, Mehnert M, Jarosch E, et al. (2011) Protein dislocation from the ER. Biochimica Et Biophysica Acta. 1808: 925-36
Mehnert M, Sommer T, Jarosch E. (2010) ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 32: 905-13
Horn SC, Hanna J, Hirsch C, et al. (2009) Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Molecular Cell. 36: 782-93
Clerc S, Hirsch C, Oggier DM, et al. (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. The Journal of Cell Biology. 184: 159-72
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