ࡱ> jli`=:jbjb.jdd/ ///8/<0\1@jz0~0~0~0~0~0.00 T?V?V?V?V?V?V?,ARC?i0~0~000?8?~0~0?8?8?8?04 ~0~0T?8?tLJ0T?8?8?8?n0 53/:88?8?@01@8?D8?D8?8?D#&&Original Peer-Reviewed Articles (*contributed equally; **shared corresponding authorship) Rumpf, S. and Jentsch S. (2006). Functional division of substrate-processing co-factors of the ubiquitin-selective Cdc48 chaperone. Mol. Cell 21, 261-269. Pfander, B., Moldovan, G.-L., Sacher, M., Hoege, C., and Jentsch, S. (2005). SUMO-modified PCNA recruits Srs2 to prevent recombination during S-phase. Nature 436, 428-433 (advance online publication, 1 June 2005) Pichler*, A., Knipscheer*, P., Oberhofer, E., van Dijk, W.J., Krner, R., Olsen, J.V., Jentsch, S., Melchior, F., and Sixma, T.K. (2005). SUMO modification of the ubiquitin conjugating enzyme E2-25K. Nat. Struct. Mol. Biol. 12, 264-269 (advance online publication, 20 February 2005) Richly, H.*, Rape, M.*, Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005). A series of ubiquitin-binding factors connects CDC48/p97 to substrate multi-ubiquitylation and proteasomal targeting. Cell 120, 73-84. Bartke, T., Pohl, C., Pyrowolakis, G., and Jentsch, S. (2004). Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. Mol. Cell 14, 801-811. Lotz*, K., Pyrowolakis*, G., and Jentsch, S. (2004). BRUCE, a giant E2/E3 ubiquitin-ligase and IAP of the trans-Golgi network, is required for normal placenta development and mouse survival. Mol. Cell. Biol. 24, 9339-9350. Lders, J., Pyrowolakis, G., and Jentsch, S. (2003). The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP. EMBO Rep. 4, 1169-1174. Hoege, C., Pfander, B., Moldovan, G.-L., Pyrowolakis, G., and Jentsch, S. (2002). RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141. Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002). Role of the CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621. Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., and Jentsch, S. (2001). Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48UFD1/NPL4, a ubiquitin-selective chaperone. Cell 107, 667-677. Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H. D., and Jentsch, S. (2000). Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 557-586. Ulrich, H. D. and Jentsch, S. (2000). Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19, 3388-3397. Koegl, M., Hoppe, T., Schlenker, S, Ulrich, H. D., Mayer, T. U., and Jentsch, S. (1999). A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644. Liakopoulos, D.*, Bsgen, T.*, Brychzy, A., Jentsch, S.**, and Pause, A.** (1999). Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau (VHL) tumor suppressor function. Proc. Natl. Acad. Sci. USA 96, 5510-5515. Hauser, H.-P., Bardroff, M., Pyrowolakis, G., and Jentsch, S. (1998). A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J. Cell Biol. 141, 1415-1422. Liakopoulos, D., Doenges, G., Matuschewski, K., and Jentsch, S. (1998). A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208-2214. Mayer, T. U., Braun, T., and Jentsch, S. (1998). Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J. 17, 3251-3257. Schwarz, S. E.*, Matuschewski, K*., Liakopoulos, D.*, Scheffner, M.**, and Jentsch, S.** (1998). The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme. Proc. Natl. Acad. Sci. USA 95, 560-564. Hhfeld, J. and Jentsch, S. (1997). GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216. Hateboer, G., Hijmans, E. M., Nooij, J. B. D., Schlenker, S., Jentsch, S., and Bernards, R. (1996). mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. J. Biol. Chem. 271, 25906-25911. Matuschewski, K., Hauser, H.-P., Treier, M., and Jentsch, S. (1996). Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions. J. Biol. Chem. 271, 2789-2794. Barral, Y., Jentsch, S., and Mann, C. (1995). G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9, 399-409. Seufert, W., Futcher, B., and Jentsch, S. (1995). Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 373, 78-81. Hartmann, E., Sommer, T., Prehn, S., Grlich, D., Jentsch, S., and Rapoport, T. A. (1994). Evolutionary conservation of components of the protein translocation complex. Nature 367, 654-657. Kaiser, P., Seufert, W., Hfferer, L., Kofler, B., Sachsenmair, C., Herzog, H., Jentsch, S., Schweiger, W., and Schneider, R. (1994). A human ubiquitin-conjugating enzyme homologous to yeast UBC8. J. Biol. Chem. 269, 8797-8802. Chen, P., Johnson, P., Sommer, T., Jentsch, S., and Hochstrasser, M. (1993). Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor. Cell 74, 357-369. Jungmann, J., Reins, H.-A., Lee, J., Romeo, A., Hassett, R., Kosman, D., and Jentsch, S. (1993). MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. EMBO J. 12, 5051-5056. Jungmann, J., Reins, H.-A., Schobert, C., and Jentsch, S. (1993). Resistance to cadmium mediated by ubiquitin-dependent protein degradation. Nature 361, 369-371. Sommer, T. and Jentsch, S. (1993). A protein translocation defect linked to ubiquitin-conjugation at the endoplasmic reticulum. Nature 365, 176-179. Zhen, M., Heinlein, R., Jones, D., Jentsch, S., and Candido, E. P. M. (1993). The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating enzyme involved in selective protein degradation. Mol. Cell. Biol. 13, 1371-1377. Seufert, W. and Jentsch, S. (1992). In vivo function of the proteasome in the ubiquitin pathway. EMBO J. 11, 3077-3080. Treier, M., Seufert, W., and Jentsch, S. (1992). Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme involved in protein degradation. EMBO J. 11, 367-372. McGrath, J. P., Jentsch, S., and Varshavsky, A. (1991). UBA1, an essential yeast gene encoding ubiquitin-activating enzyme. EMBO J. 10, 227-236. Jentsch S. (1991). A pseudogene for a novel ubiquitin C-terminal hydrolase of S. cerevisiae. Nucleic Acids Res.19, 1147. Seufert W, Jentsch S. (1990). Nucleotide sequence of two tRNA(Arg)-tRNA(Asp) tandem genes linked to duplicated UBC genes in Saccharomyces cerevisiae. Nucleic Acids Res. 18, 1638. Seufert, W. and Jentsch, S. (1990). Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9, 543-550. Seufert, W., McGrath, J. P., and Jentsch, S. (1990). UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation. EMBO J. 9, 4535-4541. Goebl, M. G., Yochem, J., Jentsch, S., McGrath, J. P., Varshavsky, A., and Byers, B. (1988). The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme. Science 241, 1331-1335. Jentsch, S., McGrath, J. P., and Varshavsky, A. (1987). The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-134. Noyer-Weidner, M., Jentsch, S., Kupsch, J., Bergbauer, M., and Trautner, T. A. (1985). DNA methyltransferase genes of Bacillus subtilis phage: Structural relatedness and gene expression. Gene 35, 143-150. Buhk, H.-J., Behrens, B., Tailor, R., Wilke, K., Prada, J. J., Gnthert, U., Noyer-Weidner, M., Jentsch, S., and Trautner, T. A. (1984). Restriction and modification in Bacillus subtilis: Nucleotide sequence, functional organisation and product of the DNA methyltransferase gene of bacteriophage SPR. Gene 29, 51-61. Noyer-Weidner, M., Jentsch, S., Pawlek, B., Gnthert, U., and Trautner, T. A. (1983). Restriction and modification in Bacillus subtilis: The DNA methylation potential of the related bacteriophage Z, SPR, SPb, f3T and r11. J. Virol. 46, 446-453. Jentsch, S. (1983). Restriction and modification in Bacillus subtilis: Sequence specificities of restriction/modification systems BsuM, BsuE and BsuF. J. Bacteriol. 156, 800-808. Gnthert, U., Jentsch, S., and Freund, M. (1981). Restriction and modification in Bacillus subtilis: Two DNA methyltransferases with BsuRI specificity. II. Catalytic properties, substrate specificity, and mode of action. J. Biol. Chem. 256, 9340-9351. Jentsch, S., Gnthert, U., and Trautner, T. A. (1981). DNA methyltransferases affecting the sequence 5'CCGG. Nucleic Acids Research 9, 2753-2759. Noyer-Weidner, M., Pawlek, B., Jentsch, S., Gnthert, U., and Trautner, T. A. (1981). Restriction and modification in Bacillus subtilis: Gene coding for a BsuR specific modification methytransferase in the temperate bacteriophage f3T. J. Virol. 38, 1077-1080. Trautner, T. A., Pawlek, B., Gnthert, U., Canosi, U., and Jentsch, S. (1980). Restriction and modification in Bacillus subtilis: Identification of a gene in the temperate phage SPb coding for a BsuR specific modification methyltransferase. Mol. Gen. Genet. 180, 361-367. Review Articles and Chapters Sacher, M., Pfander, B., and Jentsch, S. (2005). Identification of SUMO-protein conjugates. In: The Ubiquitin System; Methods Enzymology 399, 392-404. Rape, M., and Jentsch, S. (2002). Taking a bite: proteasomal protein processing. Nature Cell Biol. 4, E113-E116. Jesenberger, V. and Jentsch, S. (2002). Deadly encounter: ubiquitin meets apoptosis. Nature Reviews Mol. Cell Biol. 3, 112-121. Hoppe, T., Rape, M., and Jentsch, S. (2001). Membrane-bound transcription factors: regulated release by RIP or RUP. Current Opinion in Cell Biology 13, 344-348. Mller S., Hoege C., Pyrowolakis G. and Jentsch S. (2001). SUMO, ubiquitin's mysterious cousin Nature Reviews Mol. Cell Biol.2, 202-213. Jentsch, S. and Pyrowolakis, G. (2000). Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342. Finley et al., (1998). Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends Biochem. Sci. 23, 244-245. Jentsch, S. and Ulrich, H. D. (1998). Ubiquitous dj vu. Nature 393, 321-323. Scheffner, M., Smith, S., and Jentsch, S. (1998). The ubiquitin-conjugation system. In: Ubiquitin. J. M. Peters, J. R. Harris , and D. Finley, eds., Plenum Press, New York, pp 65-98. Jentsch, S. (1996). When proteins receive deadly messages at birth. Science 271, 955-956. Smith, S. E., Koegl, M., and Jentsch, S. (1996). Role of the ubiquitin/proteasome system in regulated protein degradation in Saccharomyces cerevisiae. Biol. Chem. 377, 437-446. Jentsch, S. and Schlenker, S. (1995). Selective protein degradation: a journey's end within the proteasome. Cell 82, 881-884. Jentsch, S. and Bachmair, A. (1992). Principles of protein turnover - Possible manipulations. In: Protein Engineering, a Practical Approach. A. R. Rees, R. Wetzel, and M. J. E. Sternberg, eds., IRL Press, Oxford UK, pp 221-228. Jentsch, S. (1992). Ubiquitin-dependent protein degradation: a cellular perspective. Trends Cell Biol. 2, 98-103. Jentsch, S. (1992). The ubiquitin-conjugation system. Annu. Rev. Genet. 26, 177-205. Jentsch, S., Seufert, W., and Hauser, H.-P. (1991). Genetic analysis of the ubiquitin-system. Biochim. Biophys. Acta 1089, 127-139. Jentsch, S., Seufert, W., Sommer, T., and Reins, H.-A. (1990). Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells. Trends Biochem. Sci. 15, 195-198. Finley, D., zkaynak, E., Jentsch, S., McGrath, J. P., Pazin, M., Snapka, R. M., Bartel, B., and Varshavsky, A. (1988). Molecular genetics of the ubiquitin-system. In: Ubiquitin. M. Rechsteiner, eds., Plenum Press, New York, pp 39-75. STEFAN JENTSCH - PUBLICATIONS  !\<  U ^ _ a ̸̤̤̓̓̂pjVBpjVpB&ha5B*CJOJQJmH phsH &ha6B*CJOJQJmH phsH  haCJ#haB*CJOJQJmH phsH !ha5CJOJPJQJmH sH !ha6CJOJPJQJmH sH 'haha5CJOJPJQJmH sH 'haha6CJOJPJQJmH sH haCJOJPJQJmH sH haCJOJQJmH sH haCJOJQJmH sH hamH sH  !\]~FY<  U l m  & 0` P@1$7$8$H$$a$:<:a m , ; = ? 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"C"E"z"|""""##$$S%T%w%%%%%&@&j&l&&& ''I'p'''((0(((((()8)Y)}))))***I*8+@+r++ ,,3,F,,,,,,,,,'-)-5-^-r----...0....../A/:::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::://A/@FYb;FFs  d !#$%@/p @pp8@p(pT@p,p.p`@UnknownGTimes New Roman5Symbol3 Arial;HelveticaC MArialMTArial3Times qh+;F;F?'S!>4d/@aOriginal Peer-Reviewed ArticlesStefan JentschStefan Jentsch Oh+'0 $ @ L X dpx' Original Peer-Reviewed Articles Stefan Jentschs NormalStefan Jentschs24Microsoft Word 11.0@:@.A@L`@OA' ՜.+,0P hp  'MPI fr BiochemieS/  Original Peer-Reviewed Articles Original Peer-Reviewed Articles TitelTitle  !"#$%&'()*+,-./012345789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXZ[\]^_`bcdefghkRoot Entry F"I`Am1Table6DWordDocument.jSummaryInformation(YDocumentSummaryInformation8aCompObjX FMicrosoft Word-DokumentNB6WWord.Document.8