Cell biology, Endoplasmic reticulum, Ubiquitin, Biochemistry and ERAD pathway are his primary areas of study. His research on Cell biology often connects related areas such as Cell adhesion. His work on Endoplasmic Reticulum Degradation Pathway and Secretory pathway as part of general Endoplasmic reticulum study is frequently linked to ER degradation, bridging the gap between disciplines.
His research in Ubiquitin intersects with topics in Tyrosine, Cadherin and Binding protein. Thomas Sommer usually deals with ERAD pathway and limits it to topics linked to Cytoplasm and Chaperone and Transport protein. As a part of the same scientific family, Thomas Sommer mostly works in the field of Endoplasmic-reticulum-associated protein degradation, focusing on Fungal protein and, on occasion, SEC Translocation Channels and Unfolded protein response.
His primary areas of study are Cell biology, Ubiquitin, Biochemistry, Endoplasmic reticulum and Endoplasmic-reticulum-associated protein degradation. His research investigates the link between Cell biology and topics such as Cytosol that cross with problems in Homeostasis. His Ubiquitin research includes themes of Lysine and Proteolysis, Enzyme.
His study looks at the relationship between Endoplasmic reticulum and fields such as Sec61, as well as how they intersect with chemical problems. The study incorporates disciplines such as Plasma protein binding, Ubiquitin binding and Fungal protein in addition to Endoplasmic-reticulum-associated protein degradation. His studies in Protein degradation integrate themes in fields like Unfolded protein response, Secretory protein and Yeast.
The scientist’s investigation covers issues in Cell biology, Ubiquitin, Endoplasmic-reticulum-associated protein degradation, Protein degradation and Biochemistry. Thomas Sommer regularly ties together related areas like Molecular biology in his Cell biology studies. His studies deal with areas such as Biophysics, Lysine and Enzyme as well as Ubiquitin.
Thomas Sommer has included themes like Plasma protein binding and Ubiquitin binding in his Endoplasmic-reticulum-associated protein degradation study. His Protein degradation study integrates concerns from other disciplines, such as Proteasome, Endoplasmic reticulum, Yeast and Protein folding. His work deals with themes such as Secretory protein, Chaperone and Glycan, which intersect with Endoplasmic reticulum.
Thomas Sommer mainly focuses on Cell biology, Biochemistry, Ubiquitin, Protein degradation and Endoplasmic reticulum. His Cell biology study combines topics in areas such as Integral membrane protein and JUNQ and IPOD. He interconnects Aggresome, STIM1, Endoplasmic-reticulum-associated protein degradation, Sec61 and Peripheral membrane protein in the investigation of issues within JUNQ and IPOD.
The Ubiquitin study combines topics in areas such as Molecular biology, DNA ligase, Lysine and Proteolysis. His work in Protein degradation addresses issues such as Proteasome, which are connected to fields such as Native state, Protein folding, Function, C-terminus and Biophysics. His work carried out in the field of Endoplasmic reticulum brings together such families of science as Membrane contact site, Growth medium, Protein quality, Glycan and Protein Homeostasis.
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ERAD: the long road to destruction
Birgit Meusser;Christian Hirsch;Ernst Jarosch;Thomas Sommer.
Nature Cell Biology (2005)
Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
Yasuyuki Fujita;Gerd Krause;Martin Scheffner;Dietmar Zechner.
Nature Cell Biology (2002)
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
Richard K. Plemper;Sigrun Böhmler;Javier Bordallo;Thomas Sommer.
Nature (1997)
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
Ernst Jarosch;Christof Taxis;Corinna Volkwein;Javier Bordallo.
Nature Cell Biology (2002)
Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.
Alexander Buchberger;Bernd Bukau;Thomas Sommer.
Molecular Cell (2010)
A regulatory link between ER-associated protein degradation and the unfolded-protein response.
Ruth Friedlander;Ernst Jarosch;Jörg Urban;Corinna Volkwein.
Nature Cell Biology (2000)
Role of Cue1p in ubiquitination and degradation at the ER surface.
Thomas Biederer;Corinna Volkwein;Thomas Sommer.
Science (1997)
Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
Ping Chen;Phoebe Johnson;Thomas Sommer;Stefan Jentsch.
Cell (1993)
The ubiquitylation machinery of the endoplasmic reticulum
Christian Hirsch;Robert Gauss;Sabine C. Horn;Oliver Neuber;Oliver Neuber.
Nature (2009)
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
Thomas Sommer;Stefan Jentsch.
Nature (1993)
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