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SUMO-Proteine (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "SUMO-Proteine" in German language version.

refsWebsite
Global rank German rank
40nih.gov
4th place
7th place
37doi.org
2nd place
3rd place
9zdb-katalog.de
123rd place
6th place
1nbn-resolving.de
3,251st place
238th place

doi.org

  • J. R. Gareau, C. D. Lima: The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. In: Nat Rev Mol Cell Biol. (2010), Band 11, Ausgabe 12, S. 861–871. doi:10.1038/nrm3011. PMID 21102611; PMC 3079294 (freier Volltext).
  • E. S. Johnson: Protein modification by SUMO. In: Annual review of biochemistry. Band 73, 2004, S. 355–382, doi:10.1146/annurev.biochem.73.011303.074118, PMID 15189146 (Review).
  • R. Sabate, A. Espargaro, R. Graña-Montes, D. Reverter, S. Ventura: Native structure protects SUMO proteins from aggregation into amyloid fibrils. In: Biomacromolecules. Band 13, Nummer 6, Juni 2012, S. 1916, doi:10.1021/bm3004385, PMID 22559198.
  • H. J. Park, W. Y. Kim, H. C. Park, S. Y. Lee, H. J. Bohnert, D. J. Yun: SUMO and SUMOylation in plants. In: Molecules and cells. Band 32, Nummer 4, Oktober 2011, S. 305–316, doi:10.1007/s10059-011-0122-7, PMID 21912873, PMC 3887640 (freier Volltext) (Review).
  • S. Vijay-Kumar, C. E. Bugg, W. J. Cook: Structure of ubiquitin refined at 1.8 A resolution. In: Journal of molecular biology. Band 194, Nummer 3, 5. April 1987, S. 531–544, doi:10.1016/0022-2836(87)90679-6, PMID 3041007.
  • P. Bayer, A. Arndt, S. Metzger, R. Mahajan, F. Melchior, R. Jaenicke, J. Becker: Structure determination of the small ubiquitin-related modifier SUMO-1. In: Journal of molecular biology. Band 280, Nummer 2, 10. Juli 1998, S. 275–286, doi:10.1006/jmbi.1998.1839, PMID 9654451.
  • K. D. Wilkinson: Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. In: FASEB Journal. Band 11, Nummer 14, Dezember 1997, S. 1245–1256, doi:10.1096/fasebj.11.14.9409543, PMID 9409543 (Review).
  • C. N. Larsen, B. A. Krantz, K. D. Wilkinson: Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. In: Biochemistry. Band 37, Nummer 10, 10. März 1998, S. 3358–3368, doi:10.1021/bi972274d, PMID 9521656.
  • S. J. Li, M. Hochstrasser: A new protease required for cell-cycle progression in yeast. In: Nature. Band 398, Nummer 6724, 18. März 1999, S. 246–251, doi:10.1038/18457, PMID 10094048.
  • S. Fang, A. M. Weissman: A field guide to ubiquitylation. In: Cellular and molecular life sciences. Band 61, Nummer 13, Juli 2004, S. 1546–1561, doi:10.1007/s00018-004-4129-5, PMID 15224180 (Review).
  • W. Li, Y. Ye: Polyubiquitin chains: functions, structures, and mechanisms. In: Cellular and molecular life sciences. Band 65, Nummer 15, August 2008, S. 2397–2406, doi:10.1007/s00018-008-8090-6, PMID 18438605, PMC 2700825 (freier Volltext) (Review).
  • A. Alonso, M. Greenlee, J. Matts, J. Kline, K. J. Davis, R. K. Miller: Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins. In: Cytoskeleton. Band 72, Nummer 7, Juli 2015, S. 305–339, doi:10.1002/cm.21226, PMID 26033929, PMC 5049490 (freier Volltext) (Review).
  • J. Song, Z. Zhang, W. Hu, Y. Chen: Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. In: Journal of Biological Chemistry. Band 280, Nummer 48, Dezember 2005, S. 40122–40129, doi:10.1074/jbc.M507059200, PMID 16204249.
  • W. C. Huang, T. P. Ko, S. S. Li, A. H. Wang: Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins. In: European Journal of Biochemistry. Band 271, Nummer 20, Oktober 2004, S. 4114–4122, doi:10.1111/j.1432-1033.2004.04349.x, PMID 15479240.
  • F. Melchior: SUMO–nonclassical ubiquitin. In: Annual review of cell and developmental biology. Band 16, 2000, S. 591–626, doi:10.1146/annurev.cellbio.16.1.591, PMID 11031248 (Review).
  • H. A. Blomster, V. Hietakangas, J. Wu, P. Kouvonen, S. Hautaniemi, L. Sistonen: Novel proteomics strategy brings insight into the prevalence of SUMO-2 target sites. In: Molecular & cellular proteomics : MCP. Band 8, Nummer 6, Juni 2009, S. 1382–1390, doi:10.1074/mcp.M800551-MCP200, PMID 19240082, PMC 2690485 (freier Volltext).
  • I. Matic, J. Schimmel, I. A. Hendriks, M. A. van Santen, F. van de Rijke, H. van Dam, F. Gnad, M. Mann, A. C. Vertegaal: Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. In: Molecular cell. Band 39, Nummer 4, 27. August 2010, S. 641–652, doi:10.1016/j.molcel.2010.07.026, PMID 20797634.
  • S. Teng, H. Luo, L. Wang: Predicting protein sumoylation sites from sequence features. In: Amino Acids. Band 43, Nummer 1, Juli 2012, S. 447–455, doi:10.1007/s00726-011-1100-2, PMID 21986959.
  • A. Pichler, C. Fatouros, H. Lee, N. Eisenhardt: SUMO conjugation - a mechanistic view. In: Biomolecular concepts. Band 8, Nummer 1, März 2017, S. 13–36, doi:10.1515/bmc-2016-0030, PMID 28284030 (Review).
  • L. Wang, C. Wansleeben, S. Zhao, P. Miao, W. Paschen, W. Yang: SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development. In: EMBO reports. Band 15, Nummer 8, August 2014, S. 878–885, doi:10.15252/embr.201438534, PMID 24891386, PMC 4197045 (freier Volltext).
  • K. M. Bohren, V. Nadkarni, J. H. Song, K. H. Gabbay, D. Owerbach: A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. In: Journal of Biological Chemistry. Band 279, Nummer 26, 25. Juni 2004, S. 27233–27238, doi:10.1074/jbc.M402273200, PMID 15123604.
  • H. Saitoh, J. Hinchey: Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. In: The Journal of Biological Chemistry. Band 275, Nr. 9, 3. März 2000, ISSN 0021-9258, S. 6252–6258, doi:10.1074/jbc.275.9.6252, PMID 10692421.
  • I. Matic, M. van Hagen, J. Schimmel, B. Macek, S. C. Ogg, M. H. Tatham, R. T. Hay, A. I. Lamond, M. Mann, A. C. Vertegaal: In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. In: Molecular & cellular proteomics : MCP. Band 7, Nummer 1, Januar 2008, S. 132–144, doi:10.1074/mcp.M700173-MCP200, PMID 17938407, PMC 3840926 (freier Volltext).
  • P. B. Meluh, D. Koshland: Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. In: Molecular Biology of the Cell. Band 6, Nummer 7, Juli 1995, S. 793–807, doi:10.1091/mbc.6.7.793, PMID 7579695, PMC 301241 (freier Volltext).
  • U. Hanania, N. Furman-Matarasso, M. Ron, A. Avni: Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death. In: The Plant journal : for cell and molecular biology. Band 19, Nummer 5, September 1999, S. 533–541, doi:10.1046/j.1365-313x.1999.00547.x, PMID 10504575.
  • K. D. Sarge, O. K. Park-Sarge: Sumoylation and human disease pathogenesis. In: Trends Biochem Sci. (2009), Band 34, Ausgabe 4, S. 200–205. doi:10.1016/j.tibs.2009.01.004. PMID 19282183; PMC 2974900 (freier Volltext).
  • S. P. Jackson, D. Durocher: Regulation of DNA damage responses by ubiquitin and SUMO. In: Mol Cell. (2013), Band 49, Ausgabe 5, S. 795–807. doi:10.1016/j.molcel.2013.01.017. PMID 23416108.
  • Deena Jalal, Jisha Chalissery, Ahmed H. Hassan: Genome maintenance in Saccharomyces cerevisiae: the role of SUMO and SUMO-targeted ubiquitin ligases. In: Nucleic Acids Research. Band 45, Nr. 5, 17. März 2017, ISSN 1362-4962, S. 2242–2261, doi:10.1093/nar/gkw1369, PMID 28115630, PMC 5389695 (freier Volltext).
  • Grace Gill: Something about SUMO inhibits transcription. In: Current Opinion in Genetics & Development. Band 15, Nr. 5, Oktober 2005, ISSN 0959-437X, S. 536–541, doi:10.1016/j.gde.2005.07.004, PMID 16095902.
  • Xiang-Dong Zhang, Jacqueline Goeres, Hong Zhang, Tim J. Yen, Andrew C. G. Porter: SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. In: Molecular Cell. Band 29, Nr. 6, 28. März 2008, ISSN 1097-4164, S. 729–741, doi:10.1016/j.molcel.2008.01.013, PMID 18374647, PMC 2366111 (freier Volltext).
  • Yoshiaki Azuma, Alexei Arnaoutov, Mary Dasso: SUMO-2/3 regulates topoisomerase II in mitosis. In: The Journal of Cell Biology. Band 163, Nr. 3, 10. November 2003, ISSN 0021-9525, S. 477–487, doi:10.1083/jcb.200304088, PMID 14597774, PMC 2173648 (freier Volltext).
  • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. In: The Journal of Cell Biology. Band 135, Nr. 6, 2. Dezember 1996, ISSN 0021-9525, S. 1457–1470, doi:10.1083/jcb.135.6.1457, PMID 8978815, PMC 2133973 (freier Volltext).
  • Tai-Shan Cheng, Li-Kwan Chang, Shen-Long Howng, Pei-Jung Lu, Chu-I. Lee: SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization. In: Life Sciences. Band 78, Nr. 10, 2. Februar 2006, ISSN 0024-3205, S. 1114–1120, doi:10.1016/j.lfs.2005.06.021, PMID 16154161.
  • Wenzhong Wei, Ping Yang, Junfeng Pang, Shu Zhang, Ying Wang: A stress-dependent SUMO4 sumoylation of its substrate proteins. In: Biochemical and Biophysical Research Communications. Band 375, Nr. 3, 24. Oktober 2008, ISSN 1090-2104, S. 454–459, doi:10.1016/j.bbrc.2008.08.028, PMID 18708028.
  • P. Wimmer, S. Schreiner, T. Dobner: Human pathogens and the host cell SUMOylation system. In: J Virol. (2012), Band 86, Ausgabe 2, S. 642–54. doi:10.1128/JVI.06227-11. PMID 22072786; PMC 3255802 (freier Volltext).
  • Y. E. Wang, O. Pernet, B. Lee: Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin-related modifiers. In: Biol Cell (2012), Band 104, Ausgabe 3, S. 121–138. doi:10.1111/boc.201100105. PMID 22188262; PMC 3625690 (freier Volltext).
  • Richard R. Burgess: Refolding solubilized inclusion body proteins. In: Methods in Enzymology. Band 463, 2009, ISSN 1557-7988, S. 259–282, doi:10.1016/S0076-6879(09)63017-2, PMID 19892177.

nbn-resolving.de

  • Schulze, Christine: SUMOylierung: ein neuer Regulations-mechanismus des Transportes von CFTR zur Membran. Dissertation, LMU München: Fakultät für Biologie, 2009, urn:nbn:de:bvb:19-107929.

nih.gov

ncbi.nlm.nih.gov

  • J. R. Gareau, C. D. Lima: The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. In: Nat Rev Mol Cell Biol. (2010), Band 11, Ausgabe 12, S. 861–871. doi:10.1038/nrm3011. PMID 21102611; PMC 3079294 (freier Volltext).
  • E. S. Johnson: Protein modification by SUMO. In: Annual review of biochemistry. Band 73, 2004, S. 355–382, doi:10.1146/annurev.biochem.73.011303.074118, PMID 15189146 (Review).
  • R. Sabate, A. Espargaro, R. Graña-Montes, D. Reverter, S. Ventura: Native structure protects SUMO proteins from aggregation into amyloid fibrils. In: Biomacromolecules. Band 13, Nummer 6, Juni 2012, S. 1916, doi:10.1021/bm3004385, PMID 22559198.
  • H. J. Park, W. Y. Kim, H. C. Park, S. Y. Lee, H. J. Bohnert, D. J. Yun: SUMO and SUMOylation in plants. In: Molecules and cells. Band 32, Nummer 4, Oktober 2011, S. 305–316, doi:10.1007/s10059-011-0122-7, PMID 21912873, PMC 3887640 (freier Volltext) (Review).
  • S. Vijay-Kumar, C. E. Bugg, W. J. Cook: Structure of ubiquitin refined at 1.8 A resolution. In: Journal of molecular biology. Band 194, Nummer 3, 5. April 1987, S. 531–544, doi:10.1016/0022-2836(87)90679-6, PMID 3041007.
  • P. Bayer, A. Arndt, S. Metzger, R. Mahajan, F. Melchior, R. Jaenicke, J. Becker: Structure determination of the small ubiquitin-related modifier SUMO-1. In: Journal of molecular biology. Band 280, Nummer 2, 10. Juli 1998, S. 275–286, doi:10.1006/jmbi.1998.1839, PMID 9654451.
  • E. Ozkaynak, D. Finley, M. J. Solomon, A. Varshavsky: The yeast ubiquitin genes: a family of natural gene fusions. In: The EMBO Journal. Band 6, Nummer 5, Mai 1987, S. 1429–1439, PMID 3038523, PMC 553949 (freier Volltext).
  • K. D. Wilkinson: Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. In: FASEB Journal. Band 11, Nummer 14, Dezember 1997, S. 1245–1256, doi:10.1096/fasebj.11.14.9409543, PMID 9409543 (Review).
  • C. N. Larsen, B. A. Krantz, K. D. Wilkinson: Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. In: Biochemistry. Band 37, Nummer 10, 10. März 1998, S. 3358–3368, doi:10.1021/bi972274d, PMID 9521656.
  • S. J. Li, M. Hochstrasser: A new protease required for cell-cycle progression in yeast. In: Nature. Band 398, Nummer 6724, 18. März 1999, S. 246–251, doi:10.1038/18457, PMID 10094048.
  • S. Fang, A. M. Weissman: A field guide to ubiquitylation. In: Cellular and molecular life sciences. Band 61, Nummer 13, Juli 2004, S. 1546–1561, doi:10.1007/s00018-004-4129-5, PMID 15224180 (Review).
  • W. Li, Y. Ye: Polyubiquitin chains: functions, structures, and mechanisms. In: Cellular and molecular life sciences. Band 65, Nummer 15, August 2008, S. 2397–2406, doi:10.1007/s00018-008-8090-6, PMID 18438605, PMC 2700825 (freier Volltext) (Review).
  • A. Alonso, M. Greenlee, J. Matts, J. Kline, K. J. Davis, R. K. Miller: Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins. In: Cytoskeleton. Band 72, Nummer 7, Juli 2015, S. 305–339, doi:10.1002/cm.21226, PMID 26033929, PMC 5049490 (freier Volltext) (Review).
  • J. Song, Z. Zhang, W. Hu, Y. Chen: Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. In: Journal of Biological Chemistry. Band 280, Nummer 48, Dezember 2005, S. 40122–40129, doi:10.1074/jbc.M507059200, PMID 16204249.
  • W. C. Huang, T. P. Ko, S. S. Li, A. H. Wang: Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins. In: European Journal of Biochemistry. Band 271, Nummer 20, Oktober 2004, S. 4114–4122, doi:10.1111/j.1432-1033.2004.04349.x, PMID 15479240.
  • F. Melchior: SUMO–nonclassical ubiquitin. In: Annual review of cell and developmental biology. Band 16, 2000, S. 591–626, doi:10.1146/annurev.cellbio.16.1.591, PMID 11031248 (Review).
  • H. A. Blomster, V. Hietakangas, J. Wu, P. Kouvonen, S. Hautaniemi, L. Sistonen: Novel proteomics strategy brings insight into the prevalence of SUMO-2 target sites. In: Molecular & cellular proteomics : MCP. Band 8, Nummer 6, Juni 2009, S. 1382–1390, doi:10.1074/mcp.M800551-MCP200, PMID 19240082, PMC 2690485 (freier Volltext).
  • I. Matic, J. Schimmel, I. A. Hendriks, M. A. van Santen, F. van de Rijke, H. van Dam, F. Gnad, M. Mann, A. C. Vertegaal: Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. In: Molecular cell. Band 39, Nummer 4, 27. August 2010, S. 641–652, doi:10.1016/j.molcel.2010.07.026, PMID 20797634.
  • S. Teng, H. Luo, L. Wang: Predicting protein sumoylation sites from sequence features. In: Amino Acids. Band 43, Nummer 1, Juli 2012, S. 447–455, doi:10.1007/s00726-011-1100-2, PMID 21986959.
  • A. Pichler, C. Fatouros, H. Lee, N. Eisenhardt: SUMO conjugation - a mechanistic view. In: Biomolecular concepts. Band 8, Nummer 1, März 2017, S. 13–36, doi:10.1515/bmc-2016-0030, PMID 28284030 (Review).
  • L. Wang, C. Wansleeben, S. Zhao, P. Miao, W. Paschen, W. Yang: SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development. In: EMBO reports. Band 15, Nummer 8, August 2014, S. 878–885, doi:10.15252/embr.201438534, PMID 24891386, PMC 4197045 (freier Volltext).
  • K. M. Bohren, V. Nadkarni, J. H. Song, K. H. Gabbay, D. Owerbach: A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. In: Journal of Biological Chemistry. Band 279, Nummer 26, 25. Juni 2004, S. 27233–27238, doi:10.1074/jbc.M402273200, PMID 15123604.
  • H. Saitoh, J. Hinchey: Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. In: The Journal of Biological Chemistry. Band 275, Nr. 9, 3. März 2000, ISSN 0021-9258, S. 6252–6258, doi:10.1074/jbc.275.9.6252, PMID 10692421.
  • I. Matic, M. van Hagen, J. Schimmel, B. Macek, S. C. Ogg, M. H. Tatham, R. T. Hay, A. I. Lamond, M. Mann, A. C. Vertegaal: In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. In: Molecular & cellular proteomics : MCP. Band 7, Nummer 1, Januar 2008, S. 132–144, doi:10.1074/mcp.M700173-MCP200, PMID 17938407, PMC 3840926 (freier Volltext).
  • P. B. Meluh, D. Koshland: Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. In: Molecular Biology of the Cell. Band 6, Nummer 7, Juli 1995, S. 793–807, doi:10.1091/mbc.6.7.793, PMID 7579695, PMC 301241 (freier Volltext).
  • U. Hanania, N. Furman-Matarasso, M. Ron, A. Avni: Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death. In: The Plant journal : for cell and molecular biology. Band 19, Nummer 5, September 1999, S. 533–541, doi:10.1046/j.1365-313x.1999.00547.x, PMID 10504575.
  • K. D. Sarge, O. K. Park-Sarge: Sumoylation and human disease pathogenesis. In: Trends Biochem Sci. (2009), Band 34, Ausgabe 4, S. 200–205. doi:10.1016/j.tibs.2009.01.004. PMID 19282183; PMC 2974900 (freier Volltext).
  • R. Mahajan, C. Delphin, T. Guan, L. Gerace, F. Melchior: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. In: Cell (1997), Band 88, Ausgabe 1, S. 97–107. PMID 9019411.
  • S. P. Jackson, D. Durocher: Regulation of DNA damage responses by ubiquitin and SUMO. In: Mol Cell. (2013), Band 49, Ausgabe 5, S. 795–807. doi:10.1016/j.molcel.2013.01.017. PMID 23416108.
  • J. Wan, D. Subramonian, X. D. Zhang: SUMOylation in control of accurate chromosome segregation during mitosis. In: Curr Protein Pept Sci. (2012), Band 13, Ausgabe 5, S. 467–481. PMID 22812528; PMC 3474960 (freier Volltext).
  • Deena Jalal, Jisha Chalissery, Ahmed H. Hassan: Genome maintenance in Saccharomyces cerevisiae: the role of SUMO and SUMO-targeted ubiquitin ligases. In: Nucleic Acids Research. Band 45, Nr. 5, 17. März 2017, ISSN 1362-4962, S. 2242–2261, doi:10.1093/nar/gkw1369, PMID 28115630, PMC 5389695 (freier Volltext).
  • Grace Gill: Something about SUMO inhibits transcription. In: Current Opinion in Genetics & Development. Band 15, Nr. 5, Oktober 2005, ISSN 0959-437X, S. 536–541, doi:10.1016/j.gde.2005.07.004, PMID 16095902.
  • Xiang-Dong Zhang, Jacqueline Goeres, Hong Zhang, Tim J. Yen, Andrew C. G. Porter: SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. In: Molecular Cell. Band 29, Nr. 6, 28. März 2008, ISSN 1097-4164, S. 729–741, doi:10.1016/j.molcel.2008.01.013, PMID 18374647, PMC 2366111 (freier Volltext).
  • Yoshiaki Azuma, Alexei Arnaoutov, Mary Dasso: SUMO-2/3 regulates topoisomerase II in mitosis. In: The Journal of Cell Biology. Band 163, Nr. 3, 10. November 2003, ISSN 0021-9525, S. 477–487, doi:10.1083/jcb.200304088, PMID 14597774, PMC 2173648 (freier Volltext).
  • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. In: The Journal of Cell Biology. Band 135, Nr. 6, 2. Dezember 1996, ISSN 0021-9525, S. 1457–1470, doi:10.1083/jcb.135.6.1457, PMID 8978815, PMC 2133973 (freier Volltext).
  • Tai-Shan Cheng, Li-Kwan Chang, Shen-Long Howng, Pei-Jung Lu, Chu-I. Lee: SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization. In: Life Sciences. Band 78, Nr. 10, 2. Februar 2006, ISSN 0024-3205, S. 1114–1120, doi:10.1016/j.lfs.2005.06.021, PMID 16154161.
  • Wenzhong Wei, Ping Yang, Junfeng Pang, Shu Zhang, Ying Wang: A stress-dependent SUMO4 sumoylation of its substrate proteins. In: Biochemical and Biophysical Research Communications. Band 375, Nr. 3, 24. Oktober 2008, ISSN 1090-2104, S. 454–459, doi:10.1016/j.bbrc.2008.08.028, PMID 18708028.
  • P. Wimmer, S. Schreiner, T. Dobner: Human pathogens and the host cell SUMOylation system. In: J Virol. (2012), Band 86, Ausgabe 2, S. 642–54. doi:10.1128/JVI.06227-11. PMID 22072786; PMC 3255802 (freier Volltext).
  • Y. E. Wang, O. Pernet, B. Lee: Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin-related modifiers. In: Biol Cell (2012), Band 104, Ausgabe 3, S. 121–138. doi:10.1111/boc.201100105. PMID 22188262; PMC 3625690 (freier Volltext).
  • Richard R. Burgess: Refolding solubilized inclusion body proteins. In: Methods in Enzymology. Band 463, 2009, ISSN 1557-7988, S. 259–282, doi:10.1016/S0076-6879(09)63017-2, PMID 19892177.

zdb-katalog.de