Year |
Citation |
Score |
2020 |
Wilfling F, Lee CW, Erdmann PS, Zheng Y, Sherpa D, Jentsch S, Pfander B, Schulman BA, Baumeister W. A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits. Molecular Cell. PMID 33207182 DOI: 10.1016/j.molcel.2020.10.030 |
0.711 |
|
2020 |
den Brave F, Cairo LV, Jagadeesan C, Ruger-Herreros C, Mogk A, Bukau B, Jentsch S. Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions. Cell Reports. 31: 107680. PMID 32492414 DOI: 10.1016/J.Celrep.2020.107680 |
0.435 |
|
2020 |
Lee CW, Wilfling F, Ronchi P, Allegretti M, Mosalaganti S, Jentsch S, Beck M, Pfander B. Selective autophagy degrades nuclear pore complexes. Nature Cell Biology. 22: 159-166. PMID 32029894 DOI: 10.1038/S41556-019-0459-2 |
0.725 |
|
2019 |
Heckmann I, Kern MJ, Pfander B, Jentsch S. A SUMO-dependent pathway controls elongating RNA Polymerase II upon UV-induced damage. Scientific Reports. 9: 17914. PMID 31784551 DOI: 10.1038/S41598-019-54027-Y |
0.396 |
|
2019 |
Höpfler M, Kern MJ, Straub T, Prytuliak R, Habermann BH, Pfander B, Jentsch S. Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance. The Embo Journal. PMID 31015336 DOI: 10.15252/Embj.2018100368 |
0.432 |
|
2017 |
Paasch F, den Brave F, Psakhye I, Pfander B, Jentsch S. Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. The Journal of Biological Chemistry. PMID 29183993 DOI: 10.1074/Jbc.M117.817833 |
0.4 |
|
2017 |
Lu K, den Brave F, Jentsch S. Pathway choice between proteasomal and autophagic degradation. Autophagy. 0. PMID 28813181 DOI: 10.1080/15548627.2017.1358851 |
0.427 |
|
2017 |
Karaduman R, Chanarat S, Pfander B, Jentsch S. Error-Prone Splicing Controlled by the Ubiquitin Relative Hub1. Molecular Cell. PMID 28712727 DOI: 10.1016/J.Molcel.2017.06.021 |
0.741 |
|
2017 |
Lademann CA, Renkawitz J, Pfander B, Jentsch S. The INO80 Complex Removes H2A.Z to Promote Presynaptic Filament Formation during Homologous Recombination. Cell Reports. 19: 1294-1303. PMID 28514650 DOI: 10.1016/J.Celrep.2017.04.051 |
0.355 |
|
2017 |
Lu K, den Brave F, Jentsch S. Receptor oligomerization guides pathway choice between proteasomal and autophagic degradation. Nature Cell Biology. PMID 28504708 DOI: 10.1038/Ncb3531 |
0.397 |
|
2016 |
Psakhye I, Jentsch S. Identification of Substrates of Protein-Group SUMOylation. Methods in Molecular Biology (Clifton, N.J.). 1475: 219-31. PMID 27631809 DOI: 10.1007/978-1-4939-6358-4_16 |
0.406 |
|
2015 |
Stingele J, Jentsch S. DNA-protein crosslink repair. Nature Reviews. Molecular Cell Biology. 16: 455-60. PMID 26130008 DOI: 10.1038/Nrm4015 |
0.418 |
|
2015 |
Stingele J, Habermann B, Jentsch S. DNA-protein crosslink repair: proteases as DNA repair enzymes. Trends in Biochemical Sciences. 40: 67-71. PMID 25496645 DOI: 10.1016/J.Tibs.2014.10.012 |
0.487 |
|
2014 |
Lu K, Psakhye I, Jentsch S. A new class of ubiquitin-Atg8 receptors involved in selective autophagy and polyQ protein clearance. Autophagy. 10: 2381-2. PMID 25470352 DOI: 10.4161/15548627.2014.981919 |
0.405 |
|
2014 |
Lu K, Psakhye I, Jentsch S. Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell. 158: 549-63. PMID 25042851 DOI: 10.1016/J.Cell.2014.05.048 |
0.446 |
|
2014 |
Stingele J, Schwarz MS, Bloemeke N, Wolf PG, Jentsch S. A DNA-dependent protease involved in DNA-protein crosslink repair. Cell. 158: 327-38. PMID 24998930 DOI: 10.1016/J.Cell.2014.04.053 |
0.466 |
|
2014 |
Ammon T, Mishra SK, Kowalska K, Popowicz GM, Holak TA, Jentsch S. The conserved ubiquitin-like protein Hub1 plays a critical role in splicing in human cells. Journal of Molecular Cell Biology. 6: 312-23. PMID 24872507 DOI: 10.1093/Jmcb/Mju026 |
0.428 |
|
2014 |
Renkawitz J, Lademann CA, Jentsch S. Mechanisms and principles of homology search during recombination. Nature Reviews. Molecular Cell Biology. 15: 369-83. PMID 24824069 DOI: 10.1038/Nrm3805 |
0.316 |
|
2014 |
Gonzalez-Huici V, Szakal B, Urulangodi M, Psakhye I, Castellucci F, Menolfi D, Rajakumara E, Fumasoni M, Bermejo R, Jentsch S, Branzei D. DNA bending facilitates the error-free DNA damage tolerance pathway and upholds genome integrity. The Embo Journal. 33: 327-40. PMID 24473148 DOI: 10.1002/Embj.201387425 |
0.442 |
|
2013 |
Jentsch S, Psakhye I. Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annual Review of Genetics. 47: 167-86. PMID 24016193 DOI: 10.1146/Annurev-Genet-111212-133453 |
0.443 |
|
2013 |
Renkawitz J, Lademann CA, Jentsch S. γH2AX spreading linked to homology search. Cell Cycle (Georgetown, Tex.). 12: 2526-7. PMID 23907159 DOI: 10.4161/Cc.25836 |
0.373 |
|
2013 |
Bergink S, Ammon T, Kern M, Schermelleh L, Leonhardt H, Jentsch S. Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction. Nature Cell Biology. 15: 526-32. PMID 23624404 DOI: 10.1038/Ncb2729 |
0.502 |
|
2013 |
Renkawitz J, Lademann CA, Kalocsay M, Jentsch S. Monitoring homology search during DNA double-strand break repair in vivo. Molecular Cell. 50: 261-72. PMID 23523370 DOI: 10.1016/J.Molcel.2013.02.020 |
0.377 |
|
2013 |
Karras GI, Fumasoni M, Sienski G, Vanoli F, Branzei D, Jentsch S. Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway. Molecular Cell. 49: 536-46. PMID 23260657 DOI: 10.1016/J.Molcel.2012.11.016 |
0.757 |
|
2012 |
Psakhye I, Jentsch S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell. 151: 807-20. PMID 23122649 DOI: 10.1016/J.Cell.2012.10.021 |
0.503 |
|
2011 |
Eichinger CS, Jentsch S. 9-1-1: PCNA's specialized cousin. Trends in Biochemical Sciences. 36: 563-8. PMID 21978893 DOI: 10.1016/J.Tibs.2011.08.002 |
0.443 |
|
2011 |
Mishra SK, Ammon T, Popowicz GM, Krajewski M, Nagel RJ, Ares M, Holak TA, Jentsch S. Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing. Nature. 474: 173-8. PMID 21614000 DOI: 10.1038/Nature10143 |
0.391 |
|
2011 |
Jentsch S. Travels with ubiquitin: from protein degradation to DNA repair. Embo Molecular Medicine. 3: 72-4. PMID 21268282 DOI: 10.1002/Emmm.201000116 |
0.387 |
|
2011 |
Van der Veen AG, Schorpp K, Schlieker C, Buti L, Damon JR, Spooner E, Ploegh HL, Jentsch S. Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proceedings of the National Academy of Sciences of the United States of America. 108: 1763-70. PMID 21209336 DOI: 10.1073/Pnas.1014402108 |
0.462 |
|
2010 |
Jentsch S, Müller S. Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways. Sub-Cellular Biochemistry. 54: 184-94. PMID 21222283 DOI: 10.1007/978-1-4419-6676-6_15 |
0.494 |
|
2010 |
Creton S, Jentsch S. SnapShot: The SUMO system. Cell. 143: 848-848.e1. PMID 21111242 DOI: 10.1016/J.Cell.2010.11.026 |
0.478 |
|
2010 |
Parnas O, Zipin-Roitman A, Pfander B, Liefshitz B, Mazor Y, Ben-Aroya S, Jentsch S, Kupiec M. Elg1, an alternative subunit of the RFC clamp loader, preferentially interacts with SUMOylated PCNA. The Embo Journal. 29: 2611-22. PMID 20571511 DOI: 10.1038/Emboj.2010.128 |
0.422 |
|
2010 |
Eichinger CS, Jentsch S. Synaptonemal complex formation and meiotic checkpoint signaling are linked to the lateral element protein Red1. Proceedings of the National Academy of Sciences of the United States of America. 107: 11370-5. PMID 20534433 DOI: 10.1073/Pnas.1004248107 |
0.389 |
|
2010 |
Karras GI, Jentsch S. The RAD6 DNA damage tolerance pathway operates uncoupled from the replication fork and is functional beyond S phase. Cell. 141: 255-67. PMID 20403322 DOI: 10.1016/J.Cell.2010.02.028 |
0.755 |
|
2009 |
Jentsch S, Siepe D. Pin1, a novel switch in the ubiquitin pathway. Cell Cycle (Georgetown, Tex.). 8: 3800-1. PMID 19934659 DOI: 10.4161/Cc.8.23.9971 |
0.306 |
|
2009 |
Siepe D, Jentsch S. Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Nature Cell Biology. 11: 967-72. PMID 19597489 DOI: 10.1038/Ncb1908 |
0.412 |
|
2009 |
Bergink S, Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature. 458: 461-7. PMID 19325626 DOI: 10.1038/Nature07963 |
0.469 |
|
2009 |
Kalocsay M, Hiller NJ, Jentsch S. Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Molecular Cell. 33: 335-43. PMID 19217407 DOI: 10.1016/J.Molcel.2009.01.016 |
0.403 |
|
2009 |
Pohl C, Jentsch S. Midbody ring disposal by autophagy is a post-abscission event of cytokinesis. Nature Cell Biology. 11: 65-70. PMID 19079246 DOI: 10.1038/Ncb1813 |
0.344 |
|
2008 |
Pohl C, Jentsch S. Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. Cell. 132: 832-45. PMID 18329369 DOI: 10.1016/J.Cell.2008.01.012 |
0.367 |
|
2007 |
Braun S, Jentsch S. SM-protein-controlled ER-associated degradation discriminates between different SNAREs. Embo Reports. 8: 1176-82. PMID 18007658 DOI: 10.1038/Sj.Embor.7401105 |
0.429 |
|
2007 |
Torres-Rosell J, Sunjevaric I, De Piccoli G, Sacher M, Eckert-Boulet N, Reid R, Jentsch S, Rothstein R, Aragón L, Lisby M. The Smc5-Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus. Nature Cell Biology. 9: 923-31. PMID 17643116 DOI: 10.1038/Ncb1619 |
0.427 |
|
2007 |
Moldovan GL, Pfander B, Jentsch S. PCNA, the maestro of the replication fork. Cell. 129: 665-79. PMID 17512402 DOI: 10.1016/J.Cell.2007.05.003 |
0.386 |
|
2007 |
Jentsch S, Rumpf S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends in Biochemical Sciences. 32: 6-11. PMID 17142044 DOI: 10.1016/J.Tibs.2006.11.005 |
0.45 |
|
2006 |
Arakawa H, Moldovan GL, Saribasak H, Saribasak NN, Jentsch S, Buerstedde JM. A role for PCNA ubiquitination in immunoglobulin hypermutation. Plos Biology. 4: e366. PMID 17105346 DOI: 10.1371/Journal.Pbio.0040366 |
0.447 |
|
2006 |
Sacher M, Pfander B, Hoege C, Jentsch S. Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nature Cell Biology. 8: 1284-90. PMID 17013376 DOI: 10.1038/Ncb1488 |
0.5 |
|
2006 |
Moldovan GL, Pfander B, Jentsch S. PCNA controls establishment of sister chromatid cohesion during S phase. Molecular Cell. 23: 723-32. PMID 16934511 DOI: 10.1016/J.Molcel.2006.07.007 |
0.429 |
|
2006 |
Piwko W, Jentsch S. Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site. Nature Structural & Molecular Biology. 13: 691-7. PMID 16845392 DOI: 10.1038/Nsmb1122 |
0.469 |
|
2006 |
Rumpf S, Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Molecular Cell. 21: 261-9. PMID 16427015 DOI: 10.1016/J.Molcel.2005.12.014 |
0.438 |
|
2005 |
Sacher M, Pfander B, Jentsch S. Identification of SUMO-protein conjugates. Methods in Enzymology. 399: 392-404. PMID 16338371 DOI: 10.1016/S0076-6879(05)99027-7 |
0.477 |
|
2005 |
Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature. 436: 428-33. PMID 15931174 DOI: 10.1038/Nature03665 |
0.48 |
|
2005 |
Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Körner R, Olsen JV, Jentsch S, Melchior F, Sixma TK. SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nature Structural & Molecular Biology. 12: 264-9. PMID 15723079 DOI: 10.1038/Nsmb903 |
0.305 |
|
2005 |
Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell. 120: 73-84. PMID 15652483 DOI: 10.1016/J.Cell.2004.11.013 |
0.7 |
|
2004 |
Rape M, Jentsch S. Productive RUPture: activation of transcription factors by proteasomal processing. Biochimica Et Biophysica Acta. 1695: 209-13. PMID 15571816 DOI: 10.1016/J.Bbamcr.2004.09.022 |
0.678 |
|
2004 |
Baumeister W, Bachmair A, Chau V, Cohen R, Coffino P, Demartino G, Deshaies R, Dohmen J, Emr S, Finley D, Hampton R, Hill C, Hochstrasser M, Huber R, Jackson P, ... Jentsch S, et al. Varshavsky's contributions. Science (New York, N.Y.). 306: 1290-2. PMID 15550643 DOI: 10.1126/Science.306.5700.1290 |
0.68 |
|
2004 |
Lotz K, Pyrowolakis G, Jentsch S. BRUCE, a giant E2/E3 ubiquitin ligase and inhibitor of apoptosis protein of the trans-Golgi network, is required for normal placenta development and mouse survival. Molecular and Cellular Biology. 24: 9339-50. PMID 15485903 DOI: 10.1128/Mcb.24.21.9339-9350.2004 |
0.376 |
|
2004 |
Bartke T, Pohl C, Pyrowolakis G, Jentsch S. Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. Molecular Cell. 14: 801-11. PMID 15200957 DOI: 10.1016/J.Molcel.2004.05.018 |
0.398 |
|
2003 |
Lüders J, Pyrowolakis G, Jentsch S. The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP. Embo Reports. 4: 1169-74. PMID 14608371 DOI: 10.1038/Sj.Embor.7400025 |
0.413 |
|
2002 |
Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419: 135-41. PMID 12226657 DOI: 10.1038/Nature00991 |
0.49 |
|
2002 |
Rape M, Jentsch S. Taking a bite: proteasomal protein processing. Nature Cell Biology. 4: E113-6. PMID 11988749 DOI: 10.1038/Ncb0502-E113 |
0.674 |
|
2002 |
Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates. The Embo Journal. 21: 615-21. PMID 11847109 DOI: 10.1093/Emboj/21.4.615 |
0.694 |
|
2002 |
Jesenberger V, Jentsch S. Deadly encounter: ubiquitin meets apoptosis. Nature Reviews. Molecular Cell Biology. 3: 112-21. PMID 11836513 DOI: 10.1038/Nrm731 |
0.409 |
|
2001 |
Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell. 107: 667-77. PMID 11733065 DOI: 10.1016/S0092-8674(01)00595-5 |
0.676 |
|
2001 |
Hoppe T, Rape M, Jentsch S. Membrane-bound transcription factors: regulated release by RIP or RUP. Current Opinion in Cell Biology. 13: 344-8. PMID 11343906 DOI: 10.1016/S0955-0674(00)00218-0 |
0.634 |
|
2001 |
Müller S, Hoege C, Pyrowolakis G, Jentsch S. SUMO, ubiquitin's mysterious cousin. Nature Reviews. Molecular Cell Biology. 2: 202-10. PMID 11265250 DOI: 10.1038/35056591 |
0.431 |
|
2000 |
Hoppe T, Matuschewski K, Rape M, Schlenker S, Ulrich HD, Jentsch S. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell. 102: 577-86. PMID 11007476 DOI: 10.1016/S0092-8674(00)00080-5 |
0.748 |
|
2000 |
Jentsch S, Pyrowolakis G. Ubiquitin and its kin: how close are the family ties? Trends in Cell Biology. 10: 335-42. PMID 10884686 DOI: 10.1016/S0962-8924(00)01785-2 |
0.502 |
|
2000 |
Ulrich HD, Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. The Embo Journal. 19: 3388-97. PMID 10880451 DOI: 10.1093/Emboj/19.13.3388 |
0.703 |
|
1999 |
Liakopoulos D, Büsgen T, Brychzy A, Jentsch S, Pause A. Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function. Proceedings of the National Academy of Sciences of the United States of America. 96: 5510-5. PMID 10318914 DOI: 10.1073/Pnas.96.10.5510 |
0.371 |
|
1999 |
Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 96: 635-44. PMID 10089879 DOI: 10.1016/S0092-8674(00)80574-7 |
0.723 |
|
1998 |
Jentsch S, Ulrich HD. Protein breakdown. Ubiquitous déjà vu. Nature. 395: 321, 323. PMID 9759715 DOI: 10.1038/26335 |
0.647 |
|
1998 |
Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, Vierstra R, Johnston S, Hampton R, Haber J, Mccusker J, Silver P, Frontali L, Thorsness P, Varshavsky A, Byers B, ... ... Jentsch S, et al. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends in Biochemical Sciences. 23: 244-5. PMID 9697412 DOI: 10.1016/S0968-0004(98)01222-5 |
0.688 |
|
1998 |
Hauser HP, Bardroff M, Pyrowolakis G, Jentsch S. A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. The Journal of Cell Biology. 141: 1415-22. PMID 9628897 DOI: 10.1083/Jcb.141.6.1415 |
0.443 |
|
1998 |
Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. The Embo Journal. 17: 3251-7. PMID 9628862 DOI: 10.1093/Emboj/17.12.3251 |
0.637 |
|
1998 |
Liakopoulos D, Doenges G, Matuschewski K, Jentsch S. A novel protein modification pathway related to the ubiquitin system. The Embo Journal. 17: 2208-14. PMID 9545234 DOI: 10.1093/Emboj/17.8.2208 |
0.481 |
|
1998 |
Schwarz SE, Matuschewski K, Liakopoulos D, Scheffner M, Jentsch S. The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme. Proceedings of the National Academy of Sciences of the United States of America. 95: 560-4. PMID 9435231 DOI: 10.1073/Pnas.95.2.560 |
0.421 |
|
1997 |
Höhfeld J, Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. The Embo Journal. 16: 6209-16. PMID 9321400 DOI: 10.1093/Emboj/16.20.6209 |
0.404 |
|
1996 |
Smith SE, Koegl M, Jentsch S. Role of the ubiquitin/proteasome system in regulated protein degradation in Saccharomyces cerevisiae. Biological Chemistry. 377: 437-46. PMID 8922277 |
0.407 |
|
1996 |
Hateboer G, Hijmans EM, Nooij JB, Schlenker S, Jentsch S, Bernards R. mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. The Journal of Biological Chemistry. 271: 25906-11. PMID 8824223 DOI: 10.1074/Jbc.271.42.25906 |
0.415 |
|
1996 |
Jentsch S. When proteins receive deadly messages at birth. Science (New York, N.Y.). 271: 955-6. PMID 8584931 DOI: 10.1126/Science.271.5251.955 |
0.351 |
|
1996 |
Matuschewski K, Hauser HP, Treier M, Jentsch S. Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions. The Journal of Biological Chemistry. 271: 2789-94. PMID 8576256 DOI: 10.1074/Jbc.271.5.2789 |
0.369 |
|
1995 |
Barral Y, Jentsch S, Mann C. G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes & Development. 9: 399-409. PMID 7883165 DOI: 10.1101/Gad.9.4.399 |
0.361 |
|
1995 |
Seufert W, Futcher B, Jentsch S. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature. 373: 78-81. PMID 7800043 DOI: 10.1038/373078A0 |
0.397 |
|
1995 |
Jentsch S, Schlenker S. Selective protein degradation: a journey's end within the proteasome. Cell. 82: 881-4. PMID 7553848 DOI: 10.1016/0092-8674(95)90021-7 |
0.385 |
|
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 |
0.423 |
|
1993 |
Zhen M, Heinlein R, Jones D, Jentsch S, Candido EP. The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating enzyme involved in selective protein degradation. Molecular and Cellular Biology. 13: 1371-7. PMID 8441382 DOI: 10.1128/Mcb.13.3.1371 |
0.405 |
|
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 |
0.445 |
|
1993 |
Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell. 74: 357-69. PMID 8393731 DOI: 10.1016/0092-8674(93)90426-Q |
0.635 |
|
1993 |
Jungmann J, Reins HA, Schobert C, Jentsch S. Resistance to cadmium mediated by ubiquitin-dependent proteolysis. Nature. 361: 369-71. PMID 8381213 DOI: 10.1038/361369A0 |
0.458 |
|
1993 |
Jungmann J, Reins HA, Lee J, Romeo A, Hassett R, Kosman D, Jentsch S. MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. The Embo Journal. 12: 5051-6. PMID 8262047 DOI: 10.1002/J.1460-2075.1993.Tb06198.X |
0.355 |
|
1992 |
Jentsch S. Ubiquitin-dependent protein degradation: a cellular perspective. Trends in Cell Biology. 2: 98-103. PMID 14732013 DOI: 10.1016/0962-8924(92)90013-D |
0.501 |
|
1992 |
Jentsch S. The ubiquitin-conjugation system. Annual Review of Genetics. 26: 179-207. PMID 1336336 DOI: 10.1146/Annurev.Ge.26.120192.001143 |
0.476 |
|
1992 |
Seufert W, Jentsch S. In vivo function of the proteasome in the ubiquitin pathway. The Embo Journal. 11: 3077-80. PMID 1322295 DOI: 10.1002/J.1460-2075.1992.Tb05379.X |
0.481 |
|
1992 |
Treier M, Seufert W, Jentsch S. Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme involved in selective protein degradation. The Embo Journal. 11: 367-72. PMID 1310935 DOI: 10.1002/J.1460-2075.1992.Tb05059.X |
0.489 |
|
1991 |
McGrath JP, Jentsch S, Varshavsky A. UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme. The Embo Journal. 10: 227-36. PMID 1989885 DOI: 10.1002/J.1460-2075.1991.Tb07940.X |
0.636 |
|
1991 |
Seufert W, Jentsch S. Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biologica Hungarica. 42: 27-37. PMID 1844315 |
0.352 |
|
1991 |
Jentsch S, Seufert W, Hauser HP. Genetic analysis of the ubiquitin system. Biochimica Et Biophysica Acta. 1089: 127-39. PMID 1647207 DOI: 10.1016/0167-4781(91)90001-3 |
0.362 |
|
1990 |
Seufert W, McGrath JP, Jentsch S. UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation. The Embo Journal. 9: 4535-41. PMID 2265617 DOI: 10.1002/J.1460-2075.1990.Tb07905.X |
0.466 |
|
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 |
0.461 |
|
1990 |
Seufert W, Jentsch S. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. The Embo Journal. 9: 543-50. PMID 2154373 DOI: 10.1002/J.1460-2075.1990.Tb08141.X |
0.475 |
|
1988 |
Goebl MG, Yochem J, Jentsch S, McGrath JP, Varshavsky A, Byers B. The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme. Science (New York, N.Y.). 241: 1331-5. PMID 2842867 DOI: 10.1126/Science.2842867 |
0.624 |
|
1987 |
Jentsch S, McGrath JP, Varshavsky A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature. 329: 131-4. PMID 3306404 DOI: 10.1038/329131A0 |
0.659 |
|
1985 |
Noyer-Weidner M, Jentsch S, Kupsch J, Bergbauer M, Trautner TA. DNA methyltransferase genes of Bacillus subtilis phages: structural relatedness and gene expression. Gene. 35: 143-50. PMID 3928442 DOI: 10.1016/0378-1119(85)90166-0 |
0.649 |
|
1984 |
Buhk HJ, Behrens B, Tailor R, Wilke K, Prada JJ, Günthert U, Noyer-Weidner M, Jentsch S, Trautner TA. Restriction and modification in Bacillus subtilis: nucleotide sequence, functional organization and product of the DNA methyltransferase gene of bacteriophage SPR. Gene. 29: 51-61. PMID 6092231 DOI: 10.1016/0378-1119(84)90165-3 |
0.641 |
|
1983 |
Noyer-Weidner M, Jentsch S, Pawlek B, Günthert U, Trautner TA. Restriction and modification in Bacillus subtilis: DNA methylation potential of the related bacteriophages Z, SPR, SP beta, phi 3T, and rho 11. Journal of Virology. 46: 446-53. PMID 6302313 DOI: 10.1128/Jvi.46.2.446-453.1983 |
0.615 |
|
1981 |
Jentsch S, Günthert U, Trautner TA. DNA methyltransferases affecting the sequence 5'CCGG. Nucleic Acids Research. 9: 2753-9. PMID 6269059 DOI: 10.1093/Nar/9.12.2753 |
0.638 |
|
1981 |
Noyer-Weidner M, Pawlek B, Jentsch S, Günthert U, Trautner TA. Restriction and modification in Bacillus subtilis: gene coding for a BsuR-specific modification methyltransferase in the temperate bacteriophage phi 3T. Journal of Virology. 38: 1077-80. PMID 6264152 DOI: 10.1128/Jvi.38.3.1077-1080.1981 |
0.632 |
|
1980 |
Trautner TA, Pawlek B, Günthert U, Canosi U, Jentsch S, Freund M. Restriction and modification in Bacillus subtilis: identification of a gene in the temperate phage SP beta coding for a BsuR specific modification methyltransferase. Molecular & General Genetics : Mgg. 180: 361-7. PMID 6258025 DOI: 10.1007/Bf00425849 |
0.643 |
|
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