메뉴 건너뛰기




Volumn 2, Issue 3, 2001, Pages 202-210

Sumo, ubiquitin's mysterious cousin

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; PROTEIN; SUMO 1 PROTEIN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME UBC9; UBIQUITIN-CONJUGATING ENZYME UBC9;

EID: 0035286622     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35056591     Document Type: Review
Times cited : (673)

References (101)
  • 1
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439 (1996).
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 2
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. & Pyrowolakis, G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 3
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biol. 2, E153-E157 (2000).
    • (2000) Nature Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 4
    • 0033199037 scopus 로고    scopus 로고
    • Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death
    • Hanania, U., Furman-Matarasso, N., Ron, M. & Avni, A. Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death. Plant J. 19, 533-541 (1999).
    • (1999) Plant J. , vol.19 , pp. 533-541
    • Hanania, U.1    Furman-Matarasso, N.2    Ron, M.3    Avni, A.4
  • 5
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Kito, K., Nguyen, H. P., Fukuda-Kamitani, T. & Yeh, E. T. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 11349-11353 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 6
    • 0029736651 scopus 로고    scopus 로고
    • PIC1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy, M. N., Howe, K., Etkin, L. D., Solomon, E. & Freemont, P. S. PIC1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13, 971-982 (1996).
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 7
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura, T. et al. Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J. Immunol. 157, 4277-4281 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 4277-4281
    • Okura, T.1
  • 8
    • 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, M. J., Coutavas, E. & Blobel, G. 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). RanGAP1 is identified as the first substrate for SUMO and the role of sumoylation in regulating the localization of RanGAP1 is shown.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 9
    • 0032504021 scopus 로고    scopus 로고
    • Structure determination of the small ubiquitin-related modifier SUMO-1
    • Bayer, P. et al. Structure determination of the small ubiquitin-related modifier SUMO-1. J. Mol. Biol. 280, 275-286 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 275-286
    • Bayer, P.1
  • 10
    • 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. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107 (1997). This important study identifies RanGAP1 as a SUMO substrate and shows that sumoylation of RanGAP1 determines its interaction with RanBP2.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 11
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M. et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644 (1999).
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1
  • 12
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E. S., Schwienhorst, I., Dohmen, R. J. & Blobel, G. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16, 5509-5519 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 13
    • 0033060826 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex
    • Gong, L., Li, B., Millas, S. & Yeh, E. T. Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. FEBS Lett. 448, 185-189 (1999).
    • (1999) FEBS Lett. , vol.448 , pp. 185-189
    • Gong, L.1    Li, B.2    Millas, S.3    Yeh, E.T.4
  • 14
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • Desterro, J. M., Rodriguez, M. S., Kemp, G. D. & Hay, R. T. Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J. Biol. Chem. 274, 10618-10624 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10618-10624
    • Desterro, J.M.1    Rodriguez, M.S.2    Kemp, G.D.3    Hay, R.T.4
  • 15
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro, J. M., Thomson, J. & Hay, R. T. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 417, 297-300 (1997).
    • (1997) FEBS Lett. , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 16
    • 0030657575 scopus 로고    scopus 로고
    • Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9
    • Gong, L., Kamitani, T., Fujise, K., Caskey, L. S. & Yeh, E. T. Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9. J. Biol. Chem. 272, 28198-28201 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28198-28201
    • Gong, L.1    Kamitani, T.2    Fujise, K.3    Caskey, L.S.4    Yeh, E.T.5
  • 17
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • Johnson, E. S. & Blobel, G. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem. 272, 26799-26802 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 19
    • 0033546283 scopus 로고    scopus 로고
    • The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1)
    • Liu, Q. et al. The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). J. Biol. Chem. 274, 16979-16987 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 16979-16987
    • Liu, Q.1
  • 20
    • 0032168745 scopus 로고    scopus 로고
    • Structure of ubiquitin-conjugating enzyme 9 displays significant differences with other ubiquitin-conjugating enzymes which may reflect its specificity for sumo rather than ubiquitin
    • Giraud, M. F., Desterro, J. M. & Naismith, J. H. Structure of ubiquitin-conjugating enzyme 9 displays significant differences with other ubiquitin-conjugating enzymes which may reflect its specificity for sumo rather than ubiquitin. Acta Crystallogr. D. Biol. Crystallogr. 54, 891-898 (1998).
    • (1998) Acta Crystallogr. D. Biol. Crystallogr. , vol.54 , pp. 891-898
    • Giraud, M.F.1    Desterro, J.M.2    Naismith, J.H.3
  • 21
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J. & Hochstrasser, M. A new protease required for cell-cycle progression in yeast. Nature 398, 246-251 (1999). This paper describes the identification of the yeast Ulp1 protease as the first SUMO de-conjugating enzyme and shows that de-sumoylation is essential for viability in yeast.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 22
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULPZ (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li, S. J. & Hochstrasser, M. The yeast ULPZ (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol. Cell. Biol. 20, 2367-2377 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 24
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova, E. & Lima, C. D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5, 865-876 (2000). This important study provides insight into the mechanism of substrate recognition and catalysis by Ulp1.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 25
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., Gong, L. & Kamitani, T. Ubiquitin-like proteins: new wines in new bottles. Gene 248, 1-14 (2000).
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 26
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase
    • Nishida, T., Tanaka, H. & Yasuda, H. A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur. J. Biochem. 267, 6423-6427 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 27
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • Gong, L., Millas, S., Maul, G. G. & Yeh, E. T. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J. Biol. Chem. 275, 3355-3359 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 28
    • 0001720254 scopus 로고    scopus 로고
    • A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs
    • Kim, K. I. et al. A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs. J. Biol. Chem. 275, 14102-14106 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14102-14106
    • Kim, K.I.1
  • 29
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich, D. & Kutay, U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell. Dev. Biol. 15, 607-660 (1999).
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 30
    • 0030963425 scopus 로고    scopus 로고
    • RanBP2 associates with Ubc9p and a modified form of RanGAP1
    • Saitoh, H., Pu, R., Cavenagh, M. & Dasso, M. RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proc. Natl Acad. Sci. USA 94, 3736-3741 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3736-3741
    • Saitoh, H.1    Pu, R.2    Cavenagh, M.3    Dasso, M.4
  • 31
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan, R., Gerace, L. & Melchior, F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140, 259-270 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 32
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • Matunis, M. J., Wu, J. & Blobel, G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140, 499-509 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 33
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1
  • 34
    • 0033661793 scopus 로고    scopus 로고
    • Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins
    • Takahashi, Y. Mizoi, J., Toh, E. A. & Kikuchi, Y. Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins. J. Biochem. 128, 723-725 (2000).
    • (2000) J. Biochem. , vol.128 , pp. 723-725
    • Takahashi, Y.1    Mizoi, J.2    Toh, E.A.3    Kikuchi, Y.4
  • 35
    • 0032547959 scopus 로고    scopus 로고
    • The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis
    • Epps, J. L. & Tanda, S. The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis. Curr. Biol. 8, 1277-1280 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1277-1280
    • Epps, J.L.1    Tanda, S.2
  • 36
    • 1842410751 scopus 로고    scopus 로고
    • Preferential modification of nuclear proteins by a novel ubiquitin-like molecule
    • Kamitani, T., Nguyen, H. P. & Yeh, E. T. Preferential modification of nuclear proteins by a novel ubiquitin-like molecule. J. Biol. Chem. 272, 14001-14004 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 14001-14004
    • Kamitani, T.1    Nguyen, H.P.2    Yeh, E.T.3
  • 37
    • 0034306019 scopus 로고    scopus 로고
    • The function of PML in p53-dependent apoptosis
    • Guo, A. et al. The function of PML in p53-dependent apoptosis. Nature Cell Biol. 2, 730-736 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 730-736
    • Guo, A.1
  • 38
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • Fogal, V. et al. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19, 6185-6195 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6185-6195
    • Fogal, V.1
  • 39
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M. J. & Dejean, A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70 (1998). This study identifies PML as a substrate for SUMO and implicates sumoylation of PML in the regulation of its compartmentalization in nuclear bodies.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 40
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf, T., Jensen, K. & Will, H. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139, 1621-1634 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 41
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Nguyen, H. P., Kito, K., Fukuda-Kamitani, T. & Yeh, E. T. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 3117-3120 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 42
    • 0032500634 scopus 로고    scopus 로고
    • Identification of three major sentrinization sites in PML
    • Kamitani, T. et al. Identification of three major sentrinization sites in PML. J. Biol. Chem. 273, 26675-26682 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 26675-26682
    • Kamitani, T.1
  • 43
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localization
    • Duprez, E. et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localization. J. Cell Sci. 112, 381-393 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 381-393
    • Duprez, E.1
  • 44
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D. et al. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72, 6581-6591 (1998).
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1
  • 45
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller, S. & Dejean, A. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73, 5137-5143 (1999).
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 46
  • 47
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-1-modified PML in nuclear body formation
    • Zhong, S. et al. Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748-2752 (2000).
    • (2000) Blood , vol.95 , pp. 2748-2752
    • Zhong, S.1
  • 48
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M. et al. PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1
  • 49
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li, H. et al. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20, 1784-1796 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1784-1796
    • Li, H.1
  • 50
    • 0035804220 scopus 로고    scopus 로고
    • Regulation of Pax3 transcriptional activity by SUMO-1-modified PML
    • Lehembre, F., Muller, S., Pandolfi, P. P. & Dejean, A. Regulation of Pax3 transcriptional activity by SUMO-1-modified PML. Oncogene 20, 1-9 (2001).
    • (2001) Oncogene , vol.20 , pp. 1-9
    • Lehembre, F.1    Muller, S.2    Pandolfi, P.P.3    Dejean, A.4
  • 51
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson, M. et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406, 207-210 (2000).
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1
  • 52
    • 0033570892 scopus 로고    scopus 로고
    • Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
    • Gostissa, M. et al. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18, 6462-6471 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6462-6471
    • Gostissa, M.1
  • 53
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • Rodriguez, M. S. et al. SUMO-1 modification activates the transcriptional response of p53. EMBO J. 18, 6455-6461 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1
  • 54
    • 0034607653 scopus 로고    scopus 로고
    • c-Jun and p53 activity is modulated by SUMO-1 modification
    • Muller, S. et al. c-Jun and p53 activity is modulated by SUMO-1 modification. J. Biol. Chem. 275, 13321-13329 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13321-13329
    • Muller, S.1
  • 55
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1 -interacting proteins and a SUMO-1 interaction motif
    • Minty, A., Dumont, X., Kaghad, M. & Caput, D. Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1 -interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275, 36316-36323 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 56
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler, J. S., Marchio, A., Sitterlin, D., Transy, C. & Dejean, A. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl Acad. Sci. USA 95, 7316-7321 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 57
    • 0032560469 scopus 로고    scopus 로고
    • Chromatin components as part of a putative transcriptional repressing complex
    • Lehming, N., Le Saux, A., Schuller, J. & Ptashne, M. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl Acad. Sci. USA 95, 7322-7326 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7322-7326
    • Lehming, N.1    Le Saux, A.2    Schuller, J.3    Ptashne, M.4
  • 58
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein SP100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T., Jensen, K., Reich, B. & Will, H. The nuclear dot protein SP100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274, 12555-12566 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 59
    • 0346785203 scopus 로고    scopus 로고
    • Common properties of the nuclear body protein SP100 and the TIF1α chromatin factor: The role of SUMO modification
    • in the press
    • Seeler, J. S. et al. Common properties of the nuclear body protein SP100 and the TIF1α chromatin factor: the role of SUMO modification. Mol. Cell. Biol. (in the press).
    • Mol. Cell. Biol.
    • Seeler, J.S.1
  • 60
    • 0347790260 scopus 로고    scopus 로고
    • Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
    • Kim, Y. H., Choi, C. Y. & Kim, Y. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proc. Natl Acad. Sci. USA 96, 12350-12355 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12350-12355
    • Kim, Y.H.1    Choi, C.Y.2    Kim, Y.3
  • 61
    • 0034700082 scopus 로고    scopus 로고
    • Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell-cycle-dependent assembly into nuclear bodies
    • Chakrabarti, S. R., Sood, R., Nandi, S. & Nucifora, G. Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell-cycle-dependent assembly into nuclear bodies. Proc. Natl Acad. Sci. USA 97, 13281-13285 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13281-13285
    • Chakrabarti, S.R.1    Sood, R.2    Nandi, S.3    Nucifora, G.4
  • 62
    • 0033594979 scopus 로고    scopus 로고
    • Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9
    • Chakrabarti, S. R. et al. Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9. Proc. Natl Acad. Sci. USA 96, 7467-7472 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7467-7472
    • Chakrabarti, S.R.1
  • 63
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., Karvonen, U., Janne, O. A. & Palvimo, J. J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl Acad. Sci. USA 97, 14145-14150 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 64
    • 0033977682 scopus 로고    scopus 로고
    • Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies
    • Lehembre, F. et al. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Mol. Cell. Biol. 20, 1072-1082 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1072-1082
    • Lehembre, F.1
  • 65
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J. M., Rodriguez, M. S. & Hay, R. T. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell 2, 233-239 (1998). This report identifies IκBα as a target for SUMO and provides evidence for a role of sumoylation in counteracting the ubiquitylation of IκBα, thus leading to the model that SUMO acts as a protein stabilizer.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 66
    • 0034705319 scopus 로고    scopus 로고
    • SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53
    • Buschmann, T., Fuchs, S. Y., Lee, C. G., Pan, Z. Q. & Ronai, Z. SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101, 753-762 (2000). This study reports that SUMO and ubiquitin share an identical lysine residue within the RING finger of Mdm2 and suggest that sumoylation stabilizes Mdm2.
    • (2000) Cell , vol.101 , pp. 753-762
    • Buschmann, T.1    Fuchs, S.Y.2    Lee, C.G.3    Pan, Z.Q.4    Ronai, Z.5
  • 67
    • 0034175930 scopus 로고    scopus 로고
    • The IKK complex: An integrator of all signals that activate NF-κB?
    • Israel, A. The IKK complex: an integrator of all signals that activate NF-κB? Trends Cell Biol. 10, 129-133 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 129-133
    • Israel, A.1
  • 68
    • 0034635361 scopus 로고    scopus 로고
    • A functional interaction between dorsal and components of the Smt3 conjugation machinery
    • Bhaskar, V., Valentine, S. A. & Courey, A. J. A functional interaction between dorsal and components of the Smt3 conjugation machinery. J. Biol. Chem. 275, 4033-4040 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4033-4040
    • Bhaskar, V.1    Valentine, S.A.2    Courey, A.J.3
  • 69
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H. & Weissman, A. M. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945-8951 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 70
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda, R. & Yasuda, H. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19, 1473-1476 (2000).
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 72
    • 0028898059 scopus 로고
    • The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis
    • al-Khodairy, F., Enoch, T., Hagan, I. M. & Carr, A. M. The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis. J. Cell Sci. 108, 475-486 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 475-486
    • Al-Khodairy, F.1    Enoch, T.2    Hagan, I.M.3    Carr, A.M.4
  • 73
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert, W., Futcher, B. & Jentsch, S. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 373, 78-81 (1995).
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 74
    • 0033574967 scopus 로고    scopus 로고
    • Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast
    • Takahashi, Y. et al. Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast. Biochem. Biophys. Res. Commun. 259, 582-587 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 582-587
    • Takahashi, Y.1
  • 75
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson, E. S. & Blobel, G. Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol. 147, 981-994 (1999). This comprehensive study identifies septins as the major substrates for SUMO in yeast and suggests a role of septin sumoylation in cytokinesis.
    • (1999) J. Cell Biol. , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 76
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P. B. & Koshland, D. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6, 793-807 (1995). This work initially identifies the yeast SMT3 gene among other genes as a suppressor of MIF2 mutations, suggesting a role of SUMO for the maintenance of genomic integrity.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 77
    • 0027483798 scopus 로고
    • MIF2 is required for mitotic spindle integrity during anaphase spindle elongation in Saccharomyces cerevisiae
    • Brown, M. T., Goetsch, L. & Hartwell, L. H. MIF2 is required for mitotic spindle integrity during anaphase spindle elongation in Saccharomyces cerevisiae. J. Cell Biol. 123, 387-403 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 387-403
    • Brown, M.T.1    Goetsch, L.2    Hartwell, L.H.3
  • 78
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka, K. et al. Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19, 8660-8672 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1
  • 79
    • 0030249870 scopus 로고    scopus 로고
    • UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins
    • Shen, Z., Pardington-Purtymun, P. E., Comeaux, J. C., Moyzis, R. K. & Chen, D. J. UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins. Genomics 36, 271-279 (1996).
    • (1996) Genomics , vol.36 , pp. 271-279
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 80
    • 0030588127 scopus 로고    scopus 로고
    • Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system
    • Shen, Z., Pardington-Purtymun, P. E., Comeaux, J. C., Moyzis, R. K. & Chen, D. J. Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system. Genomics 37, 183-186 (1996).
    • (1996) Genomics , vol.37 , pp. 183-186
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 81
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • Kovalenko, O. V. et al. Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc. Natl Acad. Sci. USA 93, 2598-2563 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2598-12563
    • Kovalenko, O.V.1
  • 82
    • 0034159893 scopus 로고    scopus 로고
    • Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein
    • Li, W. et al. Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. Nucleic Acids Res. 28, 1145-1153 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1145-1153
    • Li, W.1
  • 83
    • 0034635958 scopus 로고    scopus 로고
    • SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage
    • Mao, Y., Sun, M., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to topoisomerase I: a possible repair response to topoisomerase-mediated DNA damage. Proc. Natl Acad. Sci. USA 97, 4046-4051 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4046-4051
    • Mao, Y.1    Sun, M.2    Desai, S.D.3    Liu, L.F.4
  • 84
    • 0034714278 scopus 로고    scopus 로고
    • SUMO-1 conjugation to human DNA topoisomerase II isozymes
    • Mao, Y., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to human DNA topoisomerase II isozymes. J. Biol. Chem. 275, 26066-26073 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26066-26073
    • Mao, Y.1    Desai, S.D.2    Liu, L.F.3
  • 85
    • 0034647556 scopus 로고    scopus 로고
    • Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1
    • Kawabe, Y. et al. Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1. J. Biol. Chem. 275, 20963-20966 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 20963-20966
    • Kawabe, Y.1
  • 86
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Yeager, T. R. et al. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res. 59, 4175-4179 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 4175-4179
    • Yeager, T.R.1
  • 87
    • 0033598931 scopus 로고    scopus 로고
    • A role for PML and the nuclear body in genomic stability
    • Zhong, S. et al. A role for PML and the nuclear body in genomic stability. Oncogene 18, 7941-7947 (1999).
    • (1999) Oncogene , vol.18 , pp. 7941-7947
    • Zhong, S.1
  • 88
    • 0034162770 scopus 로고    scopus 로고
    • Association of the Bloom syndrome protein with topoisomerase IIIα in somatic and meiotic cells
    • Johnson, F. B. et al. Association of the Bloom syndrome protein with topoisomerase IIIα in somatic and meiotic cells. Cancer Res. 60, 1162-1167 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 1162-1167
    • Johnson, F.B.1
  • 89
    • 0032744386 scopus 로고    scopus 로고
    • A dynamic connection between centromeres and ND10 proteins
    • Everett, R. D. et al. A dynamic connection between centromeres and ND10 proteins. J. Cell Sci. 112, 3443-3454 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 3443-3454
    • Everett, R.D.1
  • 90
    • 0033779119 scopus 로고    scopus 로고
    • ICP0 induces the accumulation of colocalizing conjugated ubiquitin
    • Everett, R. D. ICP0 induces the accumulation of colocalizing conjugated ubiquitin. J. Virol. 74, 9994-10005 (2000).
    • (2000) J. Virol. , vol.74 , pp. 9994-10005
    • Everett, R.D.1
  • 91
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P. & Pandolfi, P. P. The transcriptional role of PML and the nuclear body. Nature Cell Biol. 2, E85-E90 (2000).
    • (2000) Nature Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 92
    • 0033152703 scopus 로고    scopus 로고
    • The PML nuclear bodies: Actors or extras?
    • Seeler, J. S. & Dejean, A. The PML nuclear bodies: actors or extras? Curr. Opin. Genet. Dev. 9, 362-367 (1999).
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 362-367
    • Seeler, J.S.1    Dejean, A.2
  • 93
    • 0343340071 scopus 로고    scopus 로고
    • Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b
    • Hofmann, H., Floss, S. & Stamminger, T. Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b. J. Virol. 74, 2510-2524 (2000).
    • (2000) J. Virol. , vol.74 , pp. 2510-2524
    • Hofmann, H.1    Floss, S.2    Stamminger, T.3
  • 94
    • 0033982336 scopus 로고    scopus 로고
    • The epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia (PML) bodies
    • Adamson, A. L. & Kenney, S. The epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia (PML) bodies. J. Virol. 74, 1224-1233 (2000).
    • (2000) J. Virol. , vol.74 , pp. 1224-1233
    • Adamson, A.L.1    Kenney, S.2
  • 95
    • 0028268278 scopus 로고
    • Functional and physical interaction between p53 and BZLF1: Implications for Epstein-Barr virus latency
    • Zhang, Q., Gutsch, D. & Kenney, S. Functional and physical interaction between p53 and BZLF1: implications for Epstein-Barr virus latency. Mol. Cell. Biol. 14, 1929-1938 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1929-1938
    • Zhang, Q.1    Gutsch, D.2    Kenney, S.3
  • 96
    • 0035808469 scopus 로고    scopus 로고
    • African swine fever virus protease: A new viral member of the SUMO-1-specific protease family
    • Andres, G., Alejo, A., Simon-Mateo, C. & Salas, M. L. African swine fever virus protease: A new viral member of the SUMO-1-specific protease family. J. Biol. Chem. 276, 780-787 (2000).
    • (2000) J. Biol. Chem. , vol.276 , pp. 780-787
    • Andres, G.1    Alejo, A.2    Simon-Mateo, C.3    Salas, M.L.4
  • 97
    • 0034711403 scopus 로고    scopus 로고
    • Disruption of signaling by yersinia effector YopJ, a ubiquitin-like protein protease
    • Orth, K. et al. Disruption of signaling by yersinia effector YopJ, a ubiquitin-like protein protease. Science 290, 1594-1597 (2000).
    • (2000) Science , vol.290 , pp. 1594-1597
    • Orth, K.1
  • 98
    • 0032518581 scopus 로고    scopus 로고
    • Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2
    • Saitoh, H. et al. Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2. Curr. Biol. 8, 121-124 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 121-124
    • Saitoh, H.1
  • 99
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino, F. et al. The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc. Natl Acad. Sci. USA 97, 1125-1130 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1125-1130
    • Giorgino, F.1
  • 100
    • 0034731301 scopus 로고    scopus 로고
    • Identification and characterization of a SUMO-1 conjugation system that modifies neuronal CaMKII in Drosophila melanogaster
    • Long, X. & Griffith, L. C. Identification and characterization of a SUMO-1 conjugation system that modifies neuronal CaMKII in Drosophila melanogaster. J. Biol. Chem. 275, 40765-40776 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 40765-40776
    • Long, X.1    Griffith, L.C.2
  • 101
    • 0034532450 scopus 로고    scopus 로고
    • SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation
    • Rangasamy, D., Woytek, K., Khan, S. A. & Wilson, V. G. SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation. J. Biol. Chem. 275, 37999-38004 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 37999-38004
    • Rangasamy, D.1    Woytek, K.2    Khan, S.A.3    Wilson, V.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.