메뉴 건너뛰기




Volumn 1773, Issue 6, 2007, Pages 694-706

SUMO on the road to neurodegeneration

Author keywords

Neurodegenerative diseases; Neuronal inclusions; Proteasome; SUMO; Ubiquitin

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; ANDROGEN RECEPTOR; ATAXIN 1; CHAPERONE; DJ 1 PROTEIN; DYNAMIN; HUNTINGTIN; PROTEASOME; PROTEIN SUMO 2; PROTEIN SUMO 3; PROTEIN SUMO 4; SUMO 1 PROTEIN; SUMO PROTEIN; TAU PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 34249733176     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.03.017     Document Type: Review
Times cited : (153)

References (114)
  • 1
  • 2
    • 0037151769 scopus 로고    scopus 로고
    • Molecular features of human ubiquitin-like SUMO genes and their encoded proteins
    • Su H.-L., and Li S.S.-L. Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. Gene 296 (2002) 65-73
    • (2002) Gene , vol.296 , pp. 65-73
    • Su, H.-L.1    Li, S.S.-L.2
  • 3
    • 3042644131 scopus 로고    scopus 로고
    • 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
    • Bohren K.M., Nadkarni V., Song J.H., Gabbay K.H., and Owerbach D. 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. J. Biol. Chem. 279 (2004) 27233-27238
    • (2004) J. Biol. Chem. , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 5
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • Desterro J.M.P., Rodriguez M.S., Kemp G.D., and Hay R.T. Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J. Biol. Chem. 274 (1999) 10618-10624
    • (1999) J. Biol. Chem. , vol.274 , pp. 10618-10624
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Kemp, G.D.3    Hay, R.T.4
  • 6
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro J.M.P., Thomson J., and Hay R.T. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 47 (1997) 297-300
    • (1997) FEBS Lett. , vol.47 , pp. 297-300
    • Desterro, J.M.P.1    Thomson, J.2    Hay, R.T.3
  • 8
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez M.S., Dargemont C., and Hay R.T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276 (2001) 12654-12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 9
    • 0037077265 scopus 로고    scopus 로고
    • Identification of a substrate recognition site on Ubc9
    • Lin D., Tatham M.H., Yu B., Kim S., Hay R.T., and Chen Y. Identification of a substrate recognition site on Ubc9. J. Biol. Chem. 277 (2002) 21740-21748
    • (2002) J. Biol. Chem. , vol.277 , pp. 21740-21748
    • Lin, D.1    Tatham, M.H.2    Yu, B.3    Kim, S.4    Hay, R.T.5    Chen, Y.6
  • 11
    • 26444593473 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction
    • Cooper H.J., Tatham M.H., Jaffray E., Heath J.K., Lam T.T., Marshall A.G., and Hay R.T. Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction. Anal. Chem. 77 (2005) 6310-6319
    • (2005) Anal. Chem. , vol.77 , pp. 6310-6319
    • Cooper, H.J.1    Tatham, M.H.2    Jaffray, E.3    Heath, J.K.4    Lam, T.T.5    Marshall, A.G.6    Hay, R.T.7
  • 12
    • 33644771265 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin
    • Wang H., Lim P.J., Yin C., Rieckher M., Vogel B.E., and Monteiro M.J. Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin. Hum. Mol. Genet. 15 (2006) 1025-1041
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1025-1041
    • Wang, H.1    Lim, P.J.2    Yin, C.3    Rieckher, M.4    Vogel, B.E.5    Monteiro, M.J.6
  • 13
    • 29144465033 scopus 로고    scopus 로고
    • The PML-nuclear inclusion of human supraoptic neurons: a new compartment with SUMO-1- and ubiquitin-proteasome-associated domains
    • Villagra N.T., Navascues J., Casafont I., Val-Bernal J.F., Lafarga M., and Berciano M.T. The PML-nuclear inclusion of human supraoptic neurons: a new compartment with SUMO-1- and ubiquitin-proteasome-associated domains. Neurobiol. Dis. 21 (2006) 181-193
    • (2006) Neurobiol. Dis. , vol.21 , pp. 181-193
    • Villagra, N.T.1    Navascues, J.2    Casafont, I.3    Val-Bernal, J.F.4    Lafarga, M.5    Berciano, M.T.6
  • 14
    • 14244249406 scopus 로고    scopus 로고
    • Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates
    • Gocke C.B., Yu H., and Kang J. Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. J. Biol. Chem. 280 (2005) 5004-5012
    • (2005) J. Biol. Chem. , vol.280 , pp. 5004-5012
    • Gocke, C.B.1    Yu, H.2    Kang, J.3
  • 16
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and α-synuclein
    • Dorval V., and Fraser P.E. Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and α-synuclein. J. Biol. Chem. 281 (2006) 9919-9924
    • (2006) J. Biol. Chem. , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 18
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal A.C.O., Andersen J.S., Ogg S.C., Hay R.T., Mann M., and Lamond A.I. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell. Proteomics 5 (2006) 2298-2310
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.O.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 19
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO2/3
    • Saitoh H., and Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO2/3. J. Biol. Chem. 275 (2000) 6252-6258
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 20
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson E.S., and Gupta A.A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106 (2001) 735-744
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 21
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo T., Nishida T., and Yasuda H. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8 (2001) 713-718
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 22
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A., Gast A., Seeler J.-S., Dejean A., and Melchior F. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108 (2002) 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
  • 23
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey M.H., Melhuish T.A., and Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell 113 (2003) 127-137
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 24
    • 24144483441 scopus 로고    scopus 로고
    • Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo
    • Weger S., Hammer E., and Heilbronn R. Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett. 579 (2005) 5007-5012
    • (2005) FEBS Lett. , vol.579 , pp. 5007-5012
    • Weger, S.1    Hammer, E.2    Heilbronn, R.3
  • 25
    • 27644559050 scopus 로고    scopus 로고
    • TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation
    • Morita Y., Kanei-Ishii C., Nomura T., and Ishii S. TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation. Mol. Biol. Cell 16 (2005) 5433-5444
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5433-5444
    • Morita, Y.1    Kanei-Ishii, C.2    Nomura, T.3    Ishii, S.4
  • 26
    • 34248338373 scopus 로고    scopus 로고
    • SUMO: regulating the regulator
    • Bossis G., and Melchior F. SUMO: regulating the regulator. Cell Div. 1 (2006) 349-357
    • (2006) Cell Div. , vol.1 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 28
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis G., and Melchior F. Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21 (2006) 349-357
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 29
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter D., and Lima C.D. A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 12 (2004) 1519-1531
    • (2004) Structure , vol.12 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 30
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • Gong L., and Yeh E.T.H. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem. 281 (2006) 15869-15877
    • (2006) J. Biol. Chem. , vol.281 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.H.2
  • 31
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen L.N., Dong C., Liu H., Naismith J.H., and Hay R.T. The structure of SENP1-SUMO2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem. J. 397 (2006) 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
  • 34
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest
    • Ulrich H.D. Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol. 15 (2005) 525-532
    • (2005) Trends Cell Biol. , vol.15 , pp. 525-532
    • Ulrich, H.D.1
  • 37
    • 29144473320 scopus 로고    scopus 로고
    • Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling
    • Bailey D., and O'Hare P. Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling. Biochem. J. 392 (2005) 271-281
    • (2005) Biochem. J. , vol.392 , pp. 271-281
    • Bailey, D.1    O'Hare, P.2
  • 39
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H., Karvonen U., Jänne O.A., and Palvimo J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 14145-14150
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Jänne, O.A.3    Palvimo, J.J.4
  • 40
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro J.M.P., Rodriguez M.S., and Hay R.T. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell 2 (1998) 233-239
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 41
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S.-J., and Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature 398 (1999) 246-251
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 42
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 44
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • Wohlschlegel J.A., Johnson E.S., Reed S.I., and Yates J.R.I. Global analysis of protein sumoylation in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004) 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.I.4
  • 45
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson E.S. Protein modification by SUMO. Annu. Rev. Biochem. 73 (2004) 355-382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 47
    • 33750604073 scopus 로고    scopus 로고
    • Functional modulation of parkin through physical interaction with SUMO-1
    • Um J.W., and Chung K.C. Functional modulation of parkin through physical interaction with SUMO-1. J. Neurosci. Res. 84 7 (2006) 1543-1554
    • (2006) J. Neurosci. Res. , vol.84 , Issue.7 , pp. 1543-1554
    • Um, J.W.1    Chung, K.C.2
  • 48
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • Takahashi H., Hatakeyama S., Saitoh H., and Nakayama K.-I. Noncovalent SUMO1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J. Biol. Chem. 280 (2005) 5611-5621
    • (2005) J. Biol. Chem. , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.-I.4
  • 49
    • 33645213038 scopus 로고    scopus 로고
    • SUMO-3 enhances androgen receptor transcriptional activity through a sumoylation-independent mechanism in prostate cancer cells
    • Zheng Z., Cai C., Omwancha J., Chen S.-Y., Baslan T., and Shemshedini L. SUMO-3 enhances androgen receptor transcriptional activity through a sumoylation-independent mechanism in prostate cancer cells. J. Biol. Chem. 281 (2006) 4002-4012
    • (2006) J. Biol. Chem. , vol.281 , pp. 4002-4012
    • Zheng, Z.1    Cai, C.2    Omwancha, J.3    Chen, S.-Y.4    Baslan, T.5    Shemshedini, L.6
  • 50
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73α by SUMO-1. Two hybrids screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty A., Dumont X., Kaghad M., and Caput D. Covalent modification of p73α by SUMO-1. Two hybrids screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275 (2000) 36316-36323
    • (2000) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 56
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal cell death
    • Arrasate M., Mitra S., Schweitzer E.S., Segal M.R., and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal cell death. Nature 431 (2004) 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 60
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A., and Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40 (2003) 427-446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 63
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: mechanisms and common principles
    • Gatchel J.R., and Zoghbi H.Y. Diseases of unstable repeat expansion: mechanisms and common principles. Nat. Rev., Genet. 6 (2005) 743-755
    • (2005) Nat. Rev., Genet. , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 65
    • 0037421691 scopus 로고    scopus 로고
    • SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity
    • Yoo S.Y., Pennesi M.E., Weeber E.J., Xu B., Atkinson R., Chen S., Armstrong D.L., Wu S.M., Sweatt J.D., and Zoghbi H.Y. SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity. Neuron 6 (2003) 383-401
    • (2003) Neuron , vol.6 , pp. 383-401
    • Yoo, S.Y.1    Pennesi, M.E.2    Weeber, E.J.3    Xu, B.4    Atkinson, R.5    Chen, S.6    Armstrong, D.L.7    Wu, S.M.8    Sweatt, J.D.9    Zoghbi, H.Y.10
  • 66
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman A.B., Yoo S.Y., Dantuma N.P., and Zoghbi H.Y. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet. 14 (2005) 679-691
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 68
    • 0037015833 scopus 로고    scopus 로고
    • SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death
    • Terashima T., Kawai H., Fujitani M., Maeda K., and Yasuda H. SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death. Neuroreport 13 (2002) 2359-2364
    • (2002) Neuroreport , vol.13 , pp. 2359-2364
    • Terashima, T.1    Kawai, H.2    Fujitani, M.3    Maeda, K.4    Yasuda, H.5
  • 71
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • Riley B.E., Zoghbi H.Y., and Orr H.T. SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J. Biol. Chem. 280 (2005) 21942-21948
    • (2005) J. Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 72
    • 0036850456 scopus 로고    scopus 로고
    • Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
    • Chan H.Y., Warrick J.M., Andriola I., Merry D., and Bonini N.M. Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum. Mol. Genet. 11 (2002) 2895-2904
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2895-2904
    • Chan, H.Y.1    Warrick, J.M.2    Andriola, I.3    Merry, D.4    Bonini, N.M.5
  • 75
    • 33644810026 scopus 로고    scopus 로고
    • Relationship between SUMO-1 modification of caspase-7 and its nuclear localization in human neuronal cells
    • Hayashi N., Shirakura H., Uehara T., and Nomura Y. Relationship between SUMO-1 modification of caspase-7 and its nuclear localization in human neuronal cells. Neurosci. Lett. 397 (2006) 5-9
    • (2006) Neurosci. Lett. , vol.397 , pp. 5-9
    • Hayashi, N.1    Shirakura, H.2    Uehara, T.3    Nomura, Y.4
  • 76
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress
    • Huang T.T., Wuerzberger-Davis S.M., Wu Z.-H., and Miyamoto S. Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress. Cell 115 (2003) 565-576
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.-H.3    Miyamoto, S.4
  • 78
    • 0037382641 scopus 로고    scopus 로고
    • Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    • Gill G. Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity. Curr. Opin. Genet. Dev. 13 (2003) 108-113
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 108-113
    • Gill, G.1
  • 83
    • 0018835157 scopus 로고
    • An unusual degenerative disorder of neurons associated with a novel intranuclear hyaline (neuronal intranuclear hyaline inclusion disease). A clinicopathological study of a case
    • Sung J.H., Ramirez-Lassepas M., Mastri A.R., and Larkin S.M. An unusual degenerative disorder of neurons associated with a novel intranuclear hyaline (neuronal intranuclear hyaline inclusion disease). A clinicopathological study of a case. J. Neuropathol. Exp. Neurol. 39 (1980) 107-130
    • (1980) J. Neuropathol. Exp. Neurol. , vol.39 , pp. 107-130
    • Sung, J.H.1    Ramirez-Lassepas, M.2    Mastri, A.R.3    Larkin, S.M.4
  • 91
    • 18844422710 scopus 로고    scopus 로고
    • SUMO-1 marks subdomains within glial cytoplasmic inclusions of multiple system atrophy
    • Pountney D.L., Chegini F., Shen X., Blumbergs P.C., and Gai W.P. SUMO-1 marks subdomains within glial cytoplasmic inclusions of multiple system atrophy. Neurosci. Lett. 381 (2005) 74-79
    • (2005) Neurosci. Lett. , vol.381 , pp. 74-79
    • Pountney, D.L.1    Chegini, F.2    Shen, X.3    Blumbergs, P.C.4    Gai, W.P.5
  • 92
    • 33645640622 scopus 로고    scopus 로고
    • Parkin ubiquitinates and promotes the degradation of RanBP2
    • Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., and Chung K.C. Parkin ubiquitinates and promotes the degradation of RanBP2. J. Biol. Chem. 281 (2006) 3595-3603
    • (2006) J. Biol. Chem. , vol.281 , pp. 3595-3603
    • Um, J.W.1    Min, D.S.2    Rhim, H.3    Kim, J.4    Paik, S.R.5    Chung, K.C.6
  • 93
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor
    • Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., and Ariga H. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor. J. Biol. Chem. 276 (2001) 37556-37563
    • (2001) J. Biol. Chem. , vol.276 , pp. 37556-37563
    • Takahashi, K.1    Taira, T.2    Niki, T.3    Seino, C.4    Iguchi-Ariga, S.M.M.5    Ariga, H.6
  • 95
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • Jenner P. Oxidative stress in Parkinson's disease. Ann. Neurol. 53 (2003) S26-S38
    • (2003) Ann. Neurol. , vol.53
    • Jenner, P.1
  • 98
    • 2942689352 scopus 로고    scopus 로고
    • Pathological properties of the Parkinson's disease-associated protein DJ-1 in α-synucleinopathies and tauopathies: relevance for multiple system atrophy and Pick's disease
    • Neumann M., Müller V., Görner K., Kretzschmar H.A., Haass C., and Kahle P.J. Pathological properties of the Parkinson's disease-associated protein DJ-1 in α-synucleinopathies and tauopathies: relevance for multiple system atrophy and Pick's disease. Acta Neuropathol. 107 (2004) 489-496
    • (2004) Acta Neuropathol. , vol.107 , pp. 489-496
    • Neumann, M.1    Müller, V.2    Görner, K.3    Kretzschmar, H.A.4    Haass, C.5    Kahle, P.J.6
  • 99
    • 33745614108 scopus 로고    scopus 로고
    • The γ-secretase complex: membrane-embedded proteolytic ensemble
    • Wolfe M.S. The γ-secretase complex: membrane-embedded proteolytic ensemble. Biochemistry 45 (2006) 7931-7939
    • (2006) Biochemistry , vol.45 , pp. 7931-7939
    • Wolfe, M.S.1
  • 101
    • 34249704660 scopus 로고    scopus 로고
    • Modulation of Aβ generation by small ubiquitin-like modifiers does not require conjugation to target proteins
    • Dorval V., Mazzella M.J., Mathews P.M., Hay R.T., and Fraser P.E. Modulation of Aβ generation by small ubiquitin-like modifiers does not require conjugation to target proteins. Biochem. J. 404 2 (2007) 309-316
    • (2007) Biochem. J. , vol.404 , Issue.2 , pp. 309-316
    • Dorval, V.1    Mazzella, M.J.2    Mathews, P.M.3    Hay, R.T.4    Fraser, P.E.5
  • 102
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau
    • Goedert M., Wischik C.M., Crowther R.A., Walker J.E., and Klug A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 4051-4055
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 103
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired-helical filaments in Alzheimer's disease
    • Mori H., Kondo J., and Ihara Y. Ubiquitin is a component of paired-helical filaments in Alzheimer's disease. Science 235 (1987) 1641-1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 104
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer's disease brains
    • Perry G., Friedman R., Shaw G., and Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer's disease brains. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3033-3036
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 105
    • 24044471309 scopus 로고    scopus 로고
    • Superoxide dismutases and their impact upon human health
    • Johnson F., and Giulivi C. Superoxide dismutases and their impact upon human health. Mol. Aspects Med. 26 (2005) 340-352
    • (2005) Mol. Aspects Med. , vol.26 , pp. 340-352
    • Johnson, F.1    Giulivi, C.2
  • 106
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • Zhou W., Ryan J.J., and Zhou H. Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J. Biol. Chem. 279 (2004) 32262-32268
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 107
    • 14644392172 scopus 로고    scopus 로고
    • Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast
    • Wykoff D.D., and O'Shea E.K. Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast. Mol. Cell. Proteomics 4 (2005) 73-83
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 73-83
    • Wykoff, D.D.1    O'Shea, E.K.2
  • 109
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin
    • Chen Z., and Pickart C.M. A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin. J. Biol. Chem. 265 (1990) 21835-21842
    • (1990) J. Biol. Chem. , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 111
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid β-protein at the cell surface
    • Chyung J.H., and Selkoe D. Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid β-protein at the cell surface. J. Biol. Chem. 278 (2003) 51035-51043
    • (2003) J. Biol. Chem. , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.2
  • 112
    • 23344432914 scopus 로고    scopus 로고
    • Role of molecular chaperones in neurodegenerative disorders
    • Meriin A.B., and Sherman M.Y. Role of molecular chaperones in neurodegenerative disorders. Int. J. Hypertherm. 21 (2005) 403-419
    • (2005) Int. J. Hypertherm. , vol.21 , pp. 403-419
    • Meriin, A.B.1    Sherman, M.Y.2
  • 113
    • 2442703973 scopus 로고    scopus 로고
    • Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins
    • Zhao Y., Kwon S.W., Anselmo A., Kaur K., and White M.A. Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. J. Biol. Chem. 279 (2004) 20999-21002
    • (2004) J. Biol. Chem. , vol.279 , pp. 20999-21002
    • Zhao, Y.1    Kwon, S.W.2    Anselmo, A.3    Kaur, K.4    White, M.A.5
  • 114
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies sumoylated substrate proteins in yeast
    • Panse V.G., Hardeland U., Werner T., Kuster B., and Hurt E. A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 279 (2004) 41346-41351
    • (2004) J. Biol. Chem. , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.