Year |
Citation |
Score |
2023 |
Christianson JC, Jarosch E, Sommer T. Mechanisms of substrate processing during ER-associated protein degradation. Nature Reviews. Molecular Cell Biology. PMID 37528230 DOI: 10.1038/s41580-023-00633-8 |
0.409 |
|
2022 |
Brodsky JL, Engelman DM, Hendershot LM, Piana-Agostinetti S, Sommer T. Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum. Faculty Reviews. 11: 29. PMID 36267301 DOI: 10.12703/r-01-0000018 |
0.338 |
|
2016 |
Pfeiffer A, Stephanowitz H, Krause E, Volkwein C, Hirsch C, Jarosch E, Sommer T. A complex of Htm1 and the oxidoreductase Pdi1 accelerates degradation of misfolded glycoproteins. The Journal of Biological Chemistry. PMID 27053108 DOI: 10.1074/jbc.M115.703256 |
0.337 |
|
2015 |
Mehnert M, Sommermeyer F, Berger M, Kumar Lakshmipathy S, Gauss R, Aebi M, Jarosch E, Sommer T. The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins. Molecular Biology of the Cell. 26: 185-94. PMID 25428985 DOI: 10.1091/Mbc.E14-07-1202 |
0.399 |
|
2014 |
Mehnert M, Sommer T, Jarosch E. Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane. Nature Cell Biology. 16: 77-86. PMID 24292014 DOI: 10.1038/ncb2882 |
0.383 |
|
2012 |
Hampton RY, Sommer T. Finding the will and the way of ERAD substrate retrotranslocation. Current Opinion in Cell Biology. 24: 460-6. PMID 22854296 DOI: 10.1016/J.Ceb.2012.05.010 |
0.394 |
|
2011 |
Bagola K, Mehnert M, Jarosch E, Sommer T. Protein dislocation from the ER. Biochimica Et Biophysica Acta. 1808: 925-36. PMID 20599420 DOI: 10.1016/j.bbamem.2010.06.025 |
0.376 |
|
2010 |
Mehnert M, Sommer T, Jarosch E. 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. PMID 20806269 DOI: 10.1002/bies.201000046 |
0.421 |
|
2009 |
Horn SC, Hanna J, Hirsch C, Volkwein C, Schütz A, Heinemann U, Sommer T, Jarosch E. Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Molecular Cell. 36: 782-93. PMID 20005842 DOI: 10.1016/j.molcel.2009.10.015 |
0.369 |
|
2009 |
Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. The Journal of Cell Biology. 184: 159-72. PMID 19124653 DOI: 10.1083/Jcb.200809198 |
0.324 |
|
2006 |
Gauss R, Sommer T, Jarosch E. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. The Embo Journal. 25: 1827-35. PMID 16619026 DOI: 10.1038/sj.emboj.7601088 |
0.405 |
|
2005 |
Neuber O, Jarosch E, Volkwein C, Walter J, Sommer T. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nature Cell Biology. 7: 993-8. PMID 16179953 DOI: 10.1038/ncb1298 |
0.412 |
|
2005 |
Meusser B, Hirsch C, Jarosch E, Sommer T. ERAD: the long road to destruction. Nature Cell Biology. 7: 766-72. PMID 16056268 DOI: 10.1038/ncb0805-766 |
0.327 |
|
2004 |
Hirsch C, Jarosch E, Sommer T, Wolf DH. Endoplasmic reticulum-associated protein degradation--one model fits all? Biochimica Et Biophysica Acta. 1695: 215-23. PMID 15571817 DOI: 10.1016/J.Bbamcr.2004.10.006 |
0.365 |
|
2004 |
Meusser B, Sommer T. Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation. Molecular Cell. 14: 247-58. PMID 15099523 DOI: 10.1016/S1097-2765(04)00212-6 |
0.306 |
|
2003 |
Jarosch E, Lenk U, Sommer T. Endoplasmic reticulum-associated protein degradation. International Review of Cytology. 223: 39-81. PMID 12641210 DOI: 10.1016/S0074-7696(05)23002-4 |
0.384 |
|
2002 |
Stade K, Vogel F, Schwienhorst I, Meusser B, Volkwein C, Nentwig B, Dohmen RJ, Sommer T. A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast. The Journal of Biological Chemistry. 277: 49554-61. PMID 12393908 DOI: 10.1074/jbc.M207991200 |
0.316 |
|
2002 |
Jarosch E, Geiss-Friedlander R, Meusser B, Walter J, Sommer T. Protein dislocation from the endoplasmic reticulum--pulling out the suspect. Traffic (Copenhagen, Denmark). 3: 530-6. PMID 12121416 DOI: 10.1034/j.1600-0854.2002.30803.x |
0.339 |
|
2002 |
Lenk U, Yu H, Walter J, Gelman MS, Hartmann E, Kopito RR, Sommer T. A role for mammalian Ubc6 homologues in ER-associated protein degradation. Journal of Cell Science. 115: 3007-14. PMID 12082160 |
0.434 |
|
2002 |
Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, Wolf DH, Sommer T. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nature Cell Biology. 4: 134-9. PMID 11813000 DOI: 10.1038/Ncb746 |
0.388 |
|
2001 |
Walter J, Urban J, Volkwein C, Sommer T. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. The Embo Journal. 20: 3124-31. PMID 11406589 DOI: 10.1093/emboj/20.12.3124 |
0.429 |
|
2000 |
Lenk U, Sommer T. Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization. The Journal of Biological Chemistry. 275: 39403-10. PMID 10991948 DOI: 10.1074/jbc.M006949200 |
0.342 |
|
2000 |
Friedlander R, Jarosch E, Urban J, Volkwein C, Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nature Cell Biology. 2: 379-84. PMID 10878801 DOI: 10.1038/35017001 |
0.334 |
|
1997 |
Sommer T, Wolf DH. Endoplasmic reticulum degradation: reverse protein flow of no return. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 11: 1227-33. PMID 9409541 DOI: 10.1096/Fasebj.11.14.9409541 |
0.428 |
|
1997 |
Biederer T, Volkwein C, Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science (New York, N.Y.). 278: 1806-9. PMID 9388185 DOI: 10.1126/science.278.5344.1806 |
0.554 |
|
1997 |
Plemper RK, Böhmler S, Bordallo J, Sommer T, Wolf DH. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388: 891-5. PMID 9278052 DOI: 10.1038/42276 |
0.32 |
|
1996 |
Biederer T, Volkwein C, Sommer T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. The Embo Journal. 15: 2069-76. PMID 8641272 DOI: 10.1002/J.1460-2075.1996.Tb00560.X |
0.553 |
|
1994 |
Hartmann E, Sommer T, Prehn S, Görlich D, Jentsch S, Rapoport TA. Evolutionary conservation of components of the protein translocation complex. Nature. 367: 654-7. PMID 8107851 DOI: 10.1038/367654A0 |
0.304 |
|
1993 |
Sommer T, Jentsch S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature. 365: 176-9. PMID 8396728 DOI: 10.1038/365176A0 |
0.41 |
|
1992 |
Sommer T, Seufert W. Genetic analysis of ubiquitin-dependent protein degradation. Experientia. 48: 172-8. PMID 1740189 DOI: 10.1007/BF01923510 |
0.343 |
|
1990 |
Jentsch S, Seufert W, Sommer T, Reins HA. Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells. Trends in Biochemical Sciences. 15: 195-8. PMID 2193438 DOI: 10.1016/0968-0004(90)90161-4 |
0.358 |
|
1989 |
Sommer T, Chambers JA, Eberle J, Lauter FR, Russo VE. Fast light-regulated genes of Neurospora crassa. Nucleic Acids Research. 17: 5713-23. PMID 2527354 DOI: 10.1093/Nar/17.14.5713 |
0.388 |
|
1987 |
Sommer T, Degli-Innocenti F, Russo VE. Role of nitrogen in the photoinduction of protoperithecia and carotenoids in Neurospora crassa. Planta. 170: 205-8. PMID 24232879 DOI: 10.1007/Bf00397889 |
0.321 |
|
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