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105 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  1
2015 Stingele J, Jentsch S. DNA–protein crosslink repair Nature Reviews Molecular Cell Biology. DOI: 10.1038/nrm4015  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2010 Creton S, Jentsch S. SnapShot: The SUMO system. Cell. 143: 848-848.e1. PMID 21111242 DOI: 10.1016/j.cell.2010.11.026  1
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  1
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  1
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  1
2009 Jentsch S, Siepe D. Pin1, a novel switch in the ubiquitin pathway. Cell Cycle (Georgetown, Tex.). 8: 3800-1. PMID 19934659  1
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  1
2009 Bergink S, Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature. 458: 461-7. PMID 19325626 DOI: 10.1038/nature07963  1
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  1
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  1
2008 Haendler B, Jentsch S. The ubiquitin system in health and disease. Preface. Ernst Schering Foundation Symposium Proceedings. V-VI. PMID 19202596  1
2008 Pohl C, Jentsch S. Regulation of apoptosis and cytokinesis by the anti-apoptotic E2/E3 ubiquitin-ligase BRUCE. Ernst Schering Foundation Symposium Proceedings. 115-26. PMID 19198067  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2003 Peltroche-Llacsahuanga H, Schnitzler N, Jentsch S, Platz A, De Hoog S, Schweizer KG, Haase G. Analyses of phagocytosis, evoked oxidative burst, and killing of black yeasts by human neutrophils: a tool for estimating their pathogenicity? Medical Mycology. 41: 7-14. PMID 12627799  1
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  1
2002 Rape M, Jentsch S. Taking a bite: proteasomal protein processing. Nature Cell Biology. 4: E113-6. PMID 11988749 DOI: 10.1038/ncb0502-e113  1
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  1
2002 Jesenberger V, Jentsch S. Deadly encounter: ubiquitin meets apoptosis. Nature Reviews. Molecular Cell Biology. 3: 112-21. PMID 11836513 DOI: 10.1038/nrm731  1
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  1
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  1
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  1
2001 Feng B, Wang X, Hauser M, Kaufmann S, Jentsch S, Haase G, Becker JM, Szaniszlo PJ. Molecular cloning and characterization of WdPKS1, a gene involved in dihydroxynaphthalene melanin biosynthesis and virulence in Wangiella (Exophiala) dermatitidis. Infection and Immunity. 69: 1781-94. PMID 11179356 DOI: 10.1128/IAI.69.3.1781-1794.2001  1
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  1
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  1
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  1
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  1
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  1
1998 Jentsch S, Ulrich HD. Protein breakdown. Ubiquitous déjà vu. Nature. 395: 321, 323. PMID 9759715 DOI: 10.1038/26335  1
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  1
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  1
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  1
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  1
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  1
1998 Hohfeld J, Jentsch S. Corrigendum. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 (The EMBO Journal (1997) 16 (6209-6216)) Embo Journal. 17: 847.  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1994 Kaiser P, Seufert W, Höfferer L, Kofler B, Sachsenmaier C, Herzog H, Jentsch S, Schweiger M, Schneider R. A human ubiquitin-conjugating enzyme homologous to yeast UBC8. The Journal of Biological Chemistry. 269: 8797-802. PMID 8132613  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1992 Jentsch S. The ubiquitin-conjugation system. Annual Review of Genetics. 26: 179-207. PMID 1336336 DOI: 10.1146/annurev.ge.26.120192.001143  1
1992 Seufert W, Jentsch S. In vivo function of the proteasome in the ubiquitin pathway. The Embo Journal. 11: 3077-80. PMID 1322295  1
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  1
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  1
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  1
1991 Jentsch S. A pseudogene for a novel ubiquitin C-terminal hydrolase of S. cerevisiae. Nucleic Acids Research. 19: 1147. PMID 1826949  1
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  1
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  1
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  1
1990 Seufert W, Jentsch S. Nucleotide sequence of two tRNA(Arg)-tRNA(Asp) tandem genes linked to duplicated UBC genes in Saccharomyces cerevisiae. Nucleic Acids Research. 18: 1638. PMID 2183198  1
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  1
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  1
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  1
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  1
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  1
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  1
1983 Jentsch S. Restriction and modification in Bacillus subtilis: sequence specificities of restriction/modification systems BsuM, BsuE, and BsuF. Journal of Bacteriology. 156: 800-8. PMID 6195145  1
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  1
1981 Günthert U, Jentsch S, Freund M. Restriction and modification in Bacillus subtilis: two DNA methyltransferases with BsuRI specificity. II. Catalytic properties, substrate specificity, and mode of action. The Journal of Biological Chemistry. 256: 9346-51. PMID 6267073  1
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  1
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  1
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