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Volumn 282, Issue 19, 2015, Pages 3669-3680

Mapping the SUMOylated landscape

Author keywords

cross talk; group modification; mass spectrometry; post translational modification; proteomics; site specific; small ubiquitin like modifier; SUMO; ubiquitin

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PROTEIN UBC9; PROTEINASE; RING FINGER PROTEIN; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE; LIGASE; PEPTIDE HYDROLASE; PROTEIN;

EID: 84942991847     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13378     Document Type: Review
Times cited : (68)

References (86)
  • 1
    • 40749131181 scopus 로고    scopus 로고
    • Emerging roles of the SUMO pathway in mitosis
    • Dasso M, (2008) Emerging roles of the SUMO pathway in mitosis. Cell Div 3, 5.
    • (2008) Cell Div , vol.3 , pp. 5
    • Dasso, M.1
  • 2
    • 84876886904 scopus 로고    scopus 로고
    • Regulation of DNA damage responses by ubiquitin and SUMO
    • Jackson SP, &, Durocher D, (2013) Regulation of DNA damage responses by ubiquitin and SUMO. Mol Cell 49, 795-807.
    • (2013) Mol Cell , vol.49 , pp. 795-807
    • Jackson, S.P.1    Durocher, D.2
  • 4
    • 59349108844 scopus 로고    scopus 로고
    • Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3
    • Evdokimov E, Sharma P, Lockett SJ, Lualdi M, &, Kuehn MR, (2008) Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. J Cell Sci 121, 4106-4113.
    • (2008) J Cell Sci , vol.121 , pp. 4106-4113
    • Evdokimov, E.1    Sharma, P.2    Lockett, S.J.3    Lualdi, M.4    Kuehn, M.R.5
  • 5
    • 84905370032 scopus 로고    scopus 로고
    • SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development
    • Wang L, Wansleeben C, Zhao S, Miao P, Paschen W, &, Yang W, (2014) SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development. EMBO Rep 15, 878-885.
    • (2014) EMBO Rep , vol.15 , pp. 878-885
    • Wang, L.1    Wansleeben, C.2    Zhao, S.3    Miao, P.4    Paschen, W.5    Yang, W.6
  • 7
    • 84888198951 scopus 로고    scopus 로고
    • SUMO rules: Regulatory concepts and their implication in neurologic functions
    • Droescher M, Chaugule VK, &, Pichler A, (2013) SUMO rules: regulatory concepts and their implication in neurologic functions. Neuromolecular Med 15, 639-660.
    • (2013) Neuromolecular Med , vol.15 , pp. 639-660
    • Droescher, M.1    Chaugule, V.K.2    Pichler, A.3
  • 8
    • 84871371484 scopus 로고    scopus 로고
    • In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice
    • Tirard M, Hsiao HH, Nikolov M, Urlaub H, Melchior F, &, Brose N, (2012) In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice. Proc Natl Acad Sci USA 109, 21122-21127.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 21122-21127
    • Tirard, M.1    Hsiao, H.H.2    Nikolov, M.3    Urlaub, H.4    Melchior, F.5    Brose, N.6
  • 10
    • 79952846685 scopus 로고    scopus 로고
    • SUMO Losing balance: SUMO proteases disrupt SUMO homeostasis to facilitate cancer development and progression
    • Bawa-Khalfe T, &, Yeh ET, (2010) SUMO Losing balance: SUMO proteases disrupt SUMO homeostasis to facilitate cancer development and progression. Genes Cancer 1, 748-752.
    • (2010) Genes Cancer , vol.1 , pp. 748-752
    • Bawa-Khalfe, T.1    Yeh, E.T.2
  • 12
    • 84866543814 scopus 로고    scopus 로고
    • SUMOylation in control of accurate chromosome segregation during mitosis
    • Wan J, Subramonian D, &, Zhang XD, (2012) SUMOylation in control of accurate chromosome segregation during mitosis. Curr Protein Pept Sci 13, 467-481.
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 467-481
    • Wan, J.1    Subramonian, D.2    Zhang, X.D.3
  • 13
    • 84872413578 scopus 로고    scopus 로고
    • SUMO: A multifaceted modifier of chromatin structure and function
    • Cubenas-Potts C, &, Matunis MJ, (2013) SUMO: a multifaceted modifier of chromatin structure and function. Dev Cell 24, 1-12.
    • (2013) Dev Cell , vol.24 , pp. 1-12
    • Cubenas-Potts, C.1    Matunis, M.J.2
  • 14
    • 84888617317 scopus 로고    scopus 로고
    • Control of nuclear activities by substrate-selective and protein-group SUMOylation
    • Jentsch S, &, Psakhye I, (2013) Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu Rev Genet 47, 167-186.
    • (2013) Annu Rev Genet , vol.47 , pp. 167-186
    • Jentsch, S.1    Psakhye, I.2
  • 15
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho A, &, Melchior F, (2013) Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem 82, 357-385.
    • (2013) Annu Rev Biochem , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 16
    • 80052697814 scopus 로고    scopus 로고
    • The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks
    • Bekker-Jensen S, &, Mailand N, (2011) The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks. FEBS Lett 585, 2914-2919.
    • (2011) FEBS Lett , vol.585 , pp. 2914-2919
    • Bekker-Jensen, S.1    Mailand, N.2
  • 17
    • 84925297959 scopus 로고    scopus 로고
    • SUMO-mediated regulation of DNA damage repair and responses
    • Sarangi P, &, Zhao X, (2015) SUMO-mediated regulation of DNA damage repair and responses. Trends Biochem Sci 40, 233-242.
    • (2015) Trends Biochem Sci , vol.40 , pp. 233-242
    • Sarangi, P.1    Zhao, X.2
  • 18
    • 0032433265 scopus 로고    scopus 로고
    • Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes
    • Chen A, Mannen H, &, Li SS, (1998) Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes. Biochem Mol Biol Int 46, 1161-1174.
    • (1998) Biochem Mol Biol Int , vol.46 , pp. 1161-1174
    • Chen, A.1    Mannen, H.2    Li, S.S.3
  • 20
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, &, Lamond AI, (2006) Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics 5, 2298-2310.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 22
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R, Delphin C, Guan T, Gerace L, &, Melchior F, (1997) A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 23
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis MJ, Coutavas E, &, Blobel G, (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 135, 1457-1470.
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 27
    • 76449092386 scopus 로고    scopus 로고
    • SUMO chains: Polymeric signals
    • Vertegaal AC, (2010) SUMO chains: polymeric signals. Biochem Soc Trans 38, 46-49.
    • (2010) Biochem Soc Trans , vol.38 , pp. 46-49
    • Vertegaal, A.C.1
  • 30
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor V, Sampson DA, Matunis MJ, &, Lima CD, (2002) Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108, 345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 31
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • Gnad F, Gunawardena J, &, Mann M, (2011) PHOSIDA 2011: the posttranslational modification database. Nucleic Acids Res 39, D253-D260.
    • (2011) Nucleic Acids Res , vol.39 , pp. D253-D260
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 34
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
    • Schmidt D, &, Muller S, (2002) Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc Natl Acad Sci USA 99, 2872-2877.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Muller, S.2
  • 35
    • 37749037140 scopus 로고    scopus 로고
    • PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription
    • Palvimo JJ, (2007) PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription. Biochem Soc Trans 35, 1405-1408.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1405-1408
    • Palvimo, J.J.1
  • 36
    • 84860743734 scopus 로고    scopus 로고
    • The RanBP2/RanGAP1∗SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase
    • Werner A, Flotho A, &, Melchior F, (2012) The RanBP2/RanGAP1∗SUMO1/Ubc9 complex is a multisubunit SUMO E3 ligase. Mol Cell 46, 287-298.
    • (2012) Mol Cell , vol.46 , pp. 287-298
    • Werner, A.1    Flotho, A.2    Melchior, F.3
  • 37
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A, Gast A, Seeler JS, Dejean A, &, Melchior F, (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 39
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey MH, Melhuish TA, &, Wotton D, (2003) The polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137.
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 40
    • 25444462980 scopus 로고    scopus 로고
    • Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications
    • Zhao X, Sternsdorf T, Bolger TA, Evans RM, &, Yao TP, (2005) Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. Mol Cell Biol 25, 8456-8464.
    • (2005) Mol Cell Biol , vol.25 , pp. 8456-8464
    • Zhao, X.1    Sternsdorf, T.2    Bolger, T.A.3    Evans, R.M.4    Yao, T.P.5
  • 43
    • 84920442558 scopus 로고    scopus 로고
    • Noncovalent interactions with SUMO and ubiquitin orchestrate distinct functions of the SLX4 complex in genome maintenance
    • Ouyang J, Garner E, Hallet A, Nguyen HD, Rickman KA, Gill G, Smogorzewska A, &, Zou L, (2015) Noncovalent interactions with SUMO and ubiquitin orchestrate distinct functions of the SLX4 complex in genome maintenance. Mol Cell 57, 108-122.
    • (2015) Mol Cell , vol.57 , pp. 108-122
    • Ouyang, J.1    Garner, E.2    Hallet, A.3    Nguyen, H.D.4    Rickman, K.A.5    Gill, G.6    Smogorzewska, A.7    Zou, L.8
  • 46
    • 84956927832 scopus 로고    scopus 로고
    • SUMO-specific proteases/isopeptidases: SENPs and beyond
    • Nayak A, &, Muller S, (2014) SUMO-specific proteases/isopeptidases: SENPs and beyond. Genome Biol 15, 422.
    • (2014) Genome Biol , vol.15 , pp. 422
    • Nayak, A.1    Muller, S.2
  • 48
  • 49
    • 33845370047 scopus 로고    scopus 로고
    • Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
    • Reverter D, &, Lima CD, (2006) Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat Struct Mol Biol 13, 1060-1068.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 1060-1068
    • Reverter, D.1    Lima, C.D.2
  • 50
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen LN, Dong C, Liu H, Naismith JH, &, Hay RT, (2006) The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J 397, 279-288.
    • (2006) Biochem J , vol.397 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 51
    • 84878616564 scopus 로고    scopus 로고
    • Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo
    • Sharma P, Yamada S, Lualdi M, Dasso M, &, Kuehn MR, (2013) Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo. Cell Rep 3, 1640-1650.
    • (2013) Cell Rep , vol.3 , pp. 1640-1650
    • Sharma, P.1    Yamada, S.2    Lualdi, M.3    Dasso, M.4    Kuehn, M.R.5
  • 52
    • 38749124386 scopus 로고    scopus 로고
    • Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family
    • Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, &, Salvesen GS, (2008) Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family. Biochem J 409, 461-469.
    • (2008) Biochem J , vol.409 , pp. 461-469
    • Drag, M.1    Mikolajczyk, J.2    Krishnakumar, I.M.3    Huang, Z.4    Salvesen, G.S.5
  • 53
    • 57649138450 scopus 로고    scopus 로고
    • Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7
    • Lima CD, &, Reverter D, (2008) Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J Biol Chem 283, 32045-32055.
    • (2008) J Biol Chem , vol.283 , pp. 32045-32055
    • Lima, C.D.1    Reverter, D.2
  • 55
    • 84863775612 scopus 로고    scopus 로고
    • Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily
    • Suh HY, Kim JH, Woo JS, Ku B, Shin EJ, Yun Y, &, Oh BH, (2012) Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily. Proteins 80, 2099-2104.
    • (2012) Proteins , vol.80 , pp. 2099-2104
    • Suh, H.Y.1    Kim, J.H.2    Woo, J.S.3    Ku, B.4    Shin, E.J.5    Yun, Y.6    Oh, B.H.7
  • 56
    • 2942564448 scopus 로고    scopus 로고
    • The RESID Database of Protein Modifications as a resource and annotation tool
    • Garavelli JS, (2004) The RESID Database of Protein Modifications as a resource and annotation tool. Proteomics 4, 1527-1533.
    • (2004) Proteomics , vol.4 , pp. 1527-1533
    • Garavelli, J.S.1
  • 62
    • 84921901572 scopus 로고    scopus 로고
    • PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation
    • Sahin U, de Thé H, &, Lallemand-Breitenbach V, (2014) PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation. Nucleus 5, 499-507.
    • (2014) Nucleus , vol.5 , pp. 499-507
    • Sahin, U.1    De Thé, H.2    Lallemand-Breitenbach, V.3
  • 63
    • 84878986048 scopus 로고    scopus 로고
    • Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation
    • Erker Y, Neyret-Kahn H, Seeler JS, Dejean A, Atfi A, &, Levy L, (2013) Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation. Mol Cell Biol 33, 2163-2177.
    • (2013) Mol Cell Biol , vol.33 , pp. 2163-2177
    • Erker, Y.1    Neyret-Kahn, H.2    Seeler, J.S.3    Dejean, A.4    Atfi, A.5    Levy, L.6
  • 66
    • 84863823240 scopus 로고    scopus 로고
    • Identification of protein SUMOylation sites by mass spectrometry using combined microwave-assisted aspartic acid cleavage and tryptic digestion
    • Osula O, Swatkoski S, &, Cotter RJ, (2012) Identification of protein SUMOylation sites by mass spectrometry using combined microwave-assisted aspartic acid cleavage and tryptic digestion. J Mass Spectrom 47, 644-654.
    • (2012) J Mass Spectrom , vol.47 , pp. 644-654
    • Osula, O.1    Swatkoski, S.2    Cotter, R.J.3
  • 70
    • 34447568143 scopus 로고    scopus 로고
    • Broad spectrum identification of SUMO substrates in melanoma cells
    • Ganesan AK, Kho Y, Kim SC, Chen Y, Zhao Y, &, White MA, (2007) Broad spectrum identification of SUMO substrates in melanoma cells. Proteomics 7, 2216-2221.
    • (2007) Proteomics , vol.7 , pp. 2216-2221
    • Ganesan, A.K.1    Kho, Y.2    Kim, S.C.3    Chen, Y.4    Zhao, Y.5    White, M.A.6
  • 72
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • Wohlschlegel JA, Johnson ES, Reed SI, &, Yates JR III, (2004) Global analysis of protein sumoylation in Saccharomyces cerevisiae. J Biol Chem 279, 45662-45668.
    • (2004) J Biol Chem , vol.279 , pp. 45662-45668
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates, J.R.4
  • 73
    • 78049235116 scopus 로고    scopus 로고
    • Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis
    • Miller MJ, Barrett-Wilt GA, Hua Z, &, Vierstra RD, (2010) Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc Natl Acad Sci USA 107, 16512-16517.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16512-16517
    • Miller, M.J.1    Barrett-Wilt, G.A.2    Hua, Z.3    Vierstra, R.D.4
  • 74
    • 84863011119 scopus 로고    scopus 로고
    • Analysis of oxygen/glucose-deprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics
    • Yang W, Thompson JW, Wang Z, Wang L, Sheng H, Foster MW, Moseley MA, &, Paschen W, (2012) Analysis of oxygen/glucose-deprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics. J Proteome Res 11, 1108-1117.
    • (2012) J Proteome Res , vol.11 , pp. 1108-1117
    • Yang, W.1    Thompson, J.W.2    Wang, Z.3    Wang, L.4    Sheng, H.5    Foster, M.W.6    Moseley, M.A.7    Paschen, W.8
  • 75
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, &, Vertegaal AC, (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol Cell 39, 641-652.
    • (2010) Mol Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    Van Santen, M.A.4    Van De Rijke, F.5    Van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.9
  • 78
    • 33645783699 scopus 로고    scopus 로고
    • Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies
    • Wohlschlegel JA, Johnson ES, Reed SI, &, Yates JR III, (2006) Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies. J Proteome Res 5, 761-770.
    • (2006) J Proteome Res , vol.5 , pp. 761-770
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates, J.R.4
  • 80
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson ES, &, Blobel G, (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 147, 981-994.
    • (1999) J Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 81
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye I, &, Jentsch S, (2012) Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807-820.
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 82
    • 84929658857 scopus 로고    scopus 로고
    • System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability
    • Xiao Z, Chang JG, Hendriks IA, Sigurdsson JO, Olsen JV, &, Vertegaal AC, (2015) System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability. Mol Cell Proteomics 14, 1419-1434.
    • (2015) Mol Cell Proteomics , vol.14 , pp. 1419-1434
    • Xiao, Z.1    Chang, J.G.2    Hendriks, I.A.3    Sigurdsson, J.O.4    Olsen, J.V.5    Vertegaal, A.C.6
  • 83
    • 83755178234 scopus 로고    scopus 로고
    • Uncovering ubiquitin and ubiquitin-like signaling networks
    • Vertegaal AC, (2011) Uncovering ubiquitin and ubiquitin-like signaling networks. Chem Rev 111, 7923-7940.
    • (2011) Chem Rev , vol.111 , pp. 7923-7940
    • Vertegaal, A.C.1
  • 84
    • 84859255877 scopus 로고    scopus 로고
    • Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity
    • Su YF, Yang T, Huang H, Liu LF, &, Hwang J, (2012) Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity. PLoS One 7, e34250.
    • (2012) PLoS One , vol.7 , pp. e34250
    • Su, Y.F.1    Yang, T.2    Huang, H.3    Liu, L.F.4    Hwang, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.