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Volumn 414, Issue 1, 2011, Pages 1-14

Interplay of posttranslational modifications in Sp1 mediates Sp1 stability during cell cycle progression

Author keywords

phosphorylation; RNF4; sumoylation; ubiquitin E3 ligase

Indexed keywords

PROTEIN RNF4; SHORT HAIRPIN RNA; TRANSCRIPTION FACTOR SP1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 81055156560     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.027     Document Type: Article
Times cited : (59)

References (56)
  • 1
    • 0037201722 scopus 로고    scopus 로고
    • Regulation of the activity of Sp1-related transcription factors
    • DOI 10.1016/S0303-7207(02)00221-6, PII S0303720702002216
    • Bouwman P., and Philipsen S. Regulation of the activity of Sp1-related transcription factors Mol. Cell. Endocrinol. 195 2002 27 38 (Pubitemid 35287159)
    • (2002) Molecular and Cellular Endocrinology , vol.195 , Issue.1-2 , pp. 27-38
    • Bouwman, P.1    Philipsen, S.2
  • 2
    • 33750849577 scopus 로고    scopus 로고
    • Overexpression of Sp1 transcription factor induces apoptosis
    • DOI 10.1038/sj.onc.1209696, PII 1209696
    • Deniaud E., Baguet J., Mathieu A.L., Pages G., Marvel J., and Leverrier Y. Overexpression of Sp1 transcription factor induces apoptosis Oncogene 25 2006 7096 7105 (Pubitemid 44722077)
    • (2006) Oncogene , vol.25 , Issue.53 , pp. 7096-7105
    • Deniaud, E.1    Baguet, J.2    Mathieu, A.-L.3    Pages, G.4    Marvel, J.5    Leverrier, Y.6
  • 3
    • 19444371383 scopus 로고    scopus 로고
    • E2F suppression and Sp1 overexpression are sufficient to induce the differentiation-specific marker, transglutaminase type 1, in a squamous cell carcinoma cell line
    • DOI 10.1038/sj.onc.1208372
    • Wong C.F., Barnes L.M., Dahler A.L., Smith L., Popa C., Serewko-Auret M.M., and Saunders N.A. E2F suppression and Sp1 overexpression are sufficient to induce the differentiation-specific marker, transglutaminase type 1, in a squamous cell carcinoma cell line Oncogene 24 2005 3525 3534 (Pubitemid 40756253)
    • (2005) Oncogene , vol.24 , Issue.21 , pp. 3525-3534
    • Wong, C.F.1    Barnes, L.M.2    Dahler, A.L.3    Smith, L.4    Popa, C.5    Serewko-Auret, M.M.6    Saunders, N.A.7
  • 4
    • 15744393419 scopus 로고    scopus 로고
    • Sp1: Regulation of gene expression by phosphorylation
    • DOI 10.1016/j.gene.2005.01.013
    • Chu S., and Ferro T.J. Sp1: regulation of gene expression by phosphorylation Gene 348 2005 1 11 (Pubitemid 40410011)
    • (2005) Gene , vol.348 , Issue.SUPPL. 1-2 , pp. 1-11
    • Chu, S.1    Ferro, T.J.2
  • 5
    • 0034929708 scopus 로고    scopus 로고
    • Sp1 and Krüppel-like factor family of transcription factors in cell growth regulation and cancer
    • DOI 10.1002/jcp.1111
    • Black A.R., Black J.D., and Azizkhan-Clifford J. Sp1 and Krüppel-like factor family of transcription factors in cell growth regulation and cancer J. Cell. Physiol. 188 2001 143 160 (Pubitemid 32622905)
    • (2001) Journal of Cellular Physiology , vol.188 , Issue.2 , pp. 143-160
    • Black, A.R.1    Black, J.D.2    Azizkhan-Clifford, J.3
  • 6
    • 33644511058 scopus 로고    scopus 로고
    • Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription
    • Hung J.J., Wang Y.T., and Chang W.C. Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription Mol. Cell. Biol. 26 2006 1770 1785
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1770-1785
    • Hung, J.J.1    Wang, Y.T.2    Chang, W.C.3
  • 7
    • 0030920226 scopus 로고    scopus 로고
    • Epidermal growth factor and okadaic acid stimulate Sp1 proteolysis
    • DOI 10.1074/jbc.272.26.16540
    • Mortensen E.R., Marks P.A., Shiotani A., and Merchant J.L. Epidermal growth factor and okadaic acid stimulate Sp1 proteolysis J. Biol. Chem. 272 1997 16540 16547 (Pubitemid 27276482)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16540-16547
    • Mortensen, E.R.1    Marks, P.A.2    Shiotani, A.3    Merchant, J.L.4
  • 8
    • 23044452436 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitors decrease vascular endothelial growth factor expression in colon cancer cells by enhanced degradation of Sp1 and Sp4 proteins
    • DOI 10.1124/mol.105.011825
    • Abdelrahim M., and Safe S. Cyclooxygenase-2 inhibitors decrease vascular endothelial growth factor expression in colon cancer cells by enhanced degradation of Sp1 and Sp4 proteins Mol. Pharmacol. 68 2005 317 329 (Pubitemid 41058295)
    • (2005) Molecular Pharmacology , vol.68 , Issue.2 , pp. 317-329
    • Abdelrahim, M.1    Safe, S.2
  • 9
    • 45849120181 scopus 로고    scopus 로고
    • Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process
    • Wang Y.T., Chuang J.Y., Shen M.R., Yang W.B., Chang W.C., and Hung J.J. Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process J. Mol. Biol. 380 2008 869 885
    • (2008) J. Mol. Biol. , vol.380 , pp. 869-885
    • Wang, Y.T.1    Chuang, J.Y.2    Shen, M.R.3    Yang, W.B.4    Chang, W.C.5    Hung, J.J.6
  • 11
    • 33745771813 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor receptor-2 expression in pancreatic cancer cells by Sp proteins
    • DOI 10.1016/j.bbrc.2006.04.111, PII S0006291X06009314
    • Higgins K.J., Abdelrahim M., Liu S., Yoon K., and Safe S. Regulation of vascular endothelial growth factor receptor-2 expression in pancreatic cancer cells by Sp proteins Biochem. Biophys. Res. Commun. 345 2006 292 301 (Pubitemid 44269283)
    • (2006) Biochemical and Biophysical Research Communications , vol.345 , Issue.1 , pp. 292-301
    • Higgins, K.J.1    Abdelrahim, M.2    Liu, S.3    Yoon, K.4    Safe, S.5
  • 12
    • 56049125650 scopus 로고    scopus 로고
    • Expression and prognostic value of transcriptional factor sp1 in breast cancer
    • Wang X.B., Peng W.Q., Yi Z.J., Zhu S.L., and Gan Q.H. Expression and prognostic value of transcriptional factor sp1 in breast cancer Ai Zheng 26 2007 996 1000
    • (2007) Ai Zheng , vol.26 , pp. 996-1000
    • Wang, X.B.1    Peng, W.Q.2    Yi, Z.J.3    Zhu, S.L.4    Gan, Q.H.5
  • 14
    • 34447121976 scopus 로고    scopus 로고
    • EGFR activation results in enhanced cyclooxygenase-2 expression through p38 mitogen-activated protein kinase-dependent activation of the Sp1/Sp3 transcription factors in human gliomas
    • DOI 10.1158/0008-5472.CAN-07-0141
    • Xu K., and Shu H.K. EGFR activation results in enhanced cyclooxygenase-2 expression through p38 mitogen-activated protein kinase-dependent activation of the Sp1/Sp3 transcription factors in human gliomas Cancer Res. 67 2007 6121 6129 (Pubitemid 47037492)
    • (2007) Cancer Research , vol.67 , Issue.13 , pp. 6121-6129
    • Xu, K.1    Shu, H.-K.G.2
  • 15
    • 3042753807 scopus 로고    scopus 로고
    • MAPK and JNK transduction pathways can phosphorylate Sp1 to activate the uPA minimal promoter element and endogenous gene transcription
    • DOI 10.1182/blood-2003-08-2661
    • Benasciutti E., Pages G., Kenzior O., Folk W., Blasi F., and Crippa M.P. MAPK and JNK transduction pathways can phosphorylate Sp1 to activate the uPA minimal promoter element and endogenous gene transcription Blood 104 2004 256 262 (Pubitemid 38879866)
    • (2004) Blood , vol.104 , Issue.1 , pp. 256-262
    • Benasciutti, E.1    Pages, G.2    Kenzior, O.3    Folk, W.4    Blasi, F.5    Crippa, M.P.6
  • 19
    • 67650178047 scopus 로고    scopus 로고
    • α-Tocopheryl succinate and derivatives mediate the transcriptional repression of androgen receptor in prostate cancer cells by targeting the PP2A-JNK-Sp1-signaling axis
    • Huang P.H., Wang D., Chuang H.C., Wei S., Kulp S.K., and Chen C.S. α-Tocopheryl succinate and derivatives mediate the transcriptional repression of androgen receptor in prostate cancer cells by targeting the PP2A-JNK-Sp1-signaling axis Carcinogenesis 30 2009 1125 1131
    • (2009) Carcinogenesis , vol.30 , pp. 1125-1131
    • Huang, P.H.1    Wang, D.2    Chuang, H.C.3    Wei, S.4    Kulp, S.K.5    Chen, C.S.6
  • 21
    • 42449103052 scopus 로고    scopus 로고
    • Sp1-like sequences mediate human caspase-3 promoter activation by p73 and cisplatin
    • DOI 10.1111/j.1742-4658.2008.06373.x
    • Sudhakar C., Jain N., and Swarup G. Sp1-like sequences mediate human caspase-3 promoter activation by p73 and cisplatin FEBS J. 275 2008 2200 2213 (Pubitemid 351569559)
    • (2008) FEBS Journal , vol.275 , Issue.9 , pp. 2200-2213
    • Sudhakar, C.1    Jain, N.2    Swarup, G.3
  • 22
    • 0033583315 scopus 로고    scopus 로고
    • Constitutive Fas ligand gene transcription in Sertoli cells is regulated by Sp1
    • McClure R.F., Heppelmann C.J., and Paya C.V. Constitutive Fas ligand gene transcription in Sertoli cells is regulated by Sp1 J. Biol. Chem. 274 1999 7756 7762
    • (1999) J. Biol. Chem. , vol.274 , pp. 7756-7762
    • McClure, R.F.1    Heppelmann, C.J.2    Paya, C.V.3
  • 23
    • 0034067856 scopus 로고    scopus 로고
    • An Sp1 binding site involves the transcription of the Fas ligand gene induced by PMA and ionomycin in Jurkat cells
    • Chou C.F., Peng H.W., Wang C.Y., Yang Y.T., and Han S.H. An Sp1 binding site involves the transcription of the Fas ligand gene induced by PMA and ionomycin in Jurkat cells J. Biomed. Sci. 7 2000 136 143
    • (2000) J. Biomed. Sci. , vol.7 , pp. 136-143
    • Chou, C.F.1    Peng, H.W.2    Wang, C.Y.3    Yang, Y.T.4    Han, S.H.5
  • 24
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IBα inhibits NF-B activation
    • Desterro J.M., Rodriguez M.S., and Hay R.T. SUMO-1 modification of IκBα inhibits NF-κB activation Mol. Cell 2 1998 233 239 (Pubitemid 128373648)
    • (1998) Molecular Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 25
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • DOI 10.1074/jbc.M110453200
    • Bies J., Markus J., and Wolff L. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity J. Biol. Chem. 277 2002 8999 9009 (Pubitemid 34952972)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 26
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • DOI 10.1016/j.gde.2005.07.004, PII S0959437X05001309
    • Gill G. Something about SUMO inhibits transcription Curr. Opin. Genet. Dev. 15 2005 536 541 (Pubitemid 41262410)
    • (2005) Current Opinion in Genetics and Development , vol.15 , Issue.5 SPEC. ISS. , pp. 536-541
    • Gill, G.1
  • 27
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • DOI 10.1038/sj.emboj.7601839, PII 7601839
    • Sun H., Leverson J.D., and Hunter T. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins EMBO J. 26 2007 4102 4112 (Pubitemid 47462098)
    • (2007) EMBO Journal , vol.26 , Issue.18 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 28
    • 63049116472 scopus 로고    scopus 로고
    • Genome stability roles of SUMO-targeted ubiquitin ligases
    • Heideker J., Perry J.J., and Boddy M.N. Genome stability roles of SUMO-targeted ubiquitin ligases DNA Repair 8 2009 517 524
    • (2009) DNA Repair , vol.8 , pp. 517-524
    • Heideker, J.1    Perry, J.J.2    Boddy, M.N.3
  • 32
    • 51249085621 scopus 로고    scopus 로고
    • Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML
    • Weisshaar S.R., Keusekotten K., Krause A., Horst C., Springer H.M., and Gottsche K. Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML FEBS Lett. 582 2008 3174 3178
    • (2008) FEBS Lett. , vol.582 , pp. 3174-3178
    • Weisshaar, S.R.1    Keusekotten, K.2    Krause, A.3    Horst, C.4    Springer, H.M.5    Gottsche, K.6
  • 33
    • 78650109515 scopus 로고    scopus 로고
    • Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies
    • Geoffroy M.C., Jaffray E.G., Walker K.J., and Hay R.T. Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies Mol. Biol. Cell 21 2010 4227 4239
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4227-4239
    • Geoffroy, M.C.1    Jaffray, E.G.2    Walker, K.J.3    Hay, R.T.4
  • 34
    • 77951211689 scopus 로고    scopus 로고
    • RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated hypoxia-inducible factor-2α
    • van Hagen M., Overmeer R.M., Abolvardi S.S., and Vertegaal A.C. RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated hypoxia-inducible factor-2α Nucleic Acids Res. 38 2010 1922 1931
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1922-1931
    • Van Hagen, M.1    Overmeer, R.M.2    Abolvardi, S.S.3    Vertegaal, A.C.4
  • 35
  • 37
    • 0035968277 scopus 로고    scopus 로고
    • The RING finger protein SNURF is a bifunctional protein possessing DNA binding activity
    • Hakli M., Karvonen U., Janne O.A., and Palvimo J.J. The RING finger protein SNURF is a bifunctional protein possessing DNA binding activity J. Biol. Chem. 276 2001 23653 23660
    • (2001) J. Biol. Chem. , vol.276 , pp. 23653-23660
    • Hakli, M.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 38
    • 0034714280 scopus 로고    scopus 로고
    • Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers
    • Lyngso C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S., and Norby P.L. Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers J. Biol. Chem. 275 2000 26144 26149
    • (2000) J. Biol. Chem. , vol.275 , pp. 26144-26149
    • Lyngso, C.1    Bouteiller, G.2    Damgaard, C.K.3    Ryom, D.4    Sanchez-Munoz, S.5    Norby, P.L.6
  • 40
    • 0033829607 scopus 로고    scopus 로고
    • The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor
    • Poukka H., Karvonen U., Yoshikawa N., Tanaka H., Palvimo J.J., and Janne O.A. The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor J. Cell Sci. 113 2000 2991 3001
    • (2000) J. Cell Sci. , vol.113 , pp. 2991-3001
    • Poukka, H.1    Karvonen, U.2    Yoshikawa, N.3    Tanaka, H.4    Palvimo, J.J.5    Janne, O.A.6
  • 41
    • 2342635250 scopus 로고    scopus 로고
    • Small nuclear RING finger protein stimulates the rat luteinizing hormone-β promoter by interacting with Sp1 and steroidogenic factor-1 and protects from androgen suppression
    • DOI 10.1210/me.2003-0221
    • Curtin D., Ferris H.A., Hakli M., Gibson M., Janne O.A., Palvimo J.J., and Shupnik M.A. Small nuclear RING finger protein stimulates the rat luteinizing hormone-β promoter by interacting with Sp1 and steroidogenic factor-1 and protects from androgen suppression Mol. Endocrinol. 18 2004 1263 1276 (Pubitemid 38591290)
    • (2004) Molecular Endocrinology , vol.18 , Issue.5 , pp. 1263-1276
    • Curtin, D.1    Ferris, H.A.2    Hakli, M.3    Gibson, M.4    Janne, O.A.5    Palvimo, J.J.6    Shupnik, M.A.7
  • 42
    • 0141866764 scopus 로고    scopus 로고
    • The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor
    • DOI 10.1074/jbc.M306259200
    • Kaiser F.J., Moroy T., Chang G.T., Horsthemke B., and Ludecke H.J. The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor J. Biol. Chem. 278 2003 38780 38785 (Pubitemid 37221777)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38780-38785
    • Kaiser, F.J.1    Moroy, T.2    Chang, G.T.G.3    Horsthemke, B.4    Ludecke, H.-J.5
  • 43
    • 1342265499 scopus 로고    scopus 로고
    • Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity
    • DOI 10.1016/S0014-5793(04)00070-5
    • Hakli M., Lorick K.L., Weissman A.M., Janne O.A., and Palvimo J.J. Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity FEBS Lett. 560 2004 56 62 (Pubitemid 38264293)
    • (2004) FEBS Letters , vol.560 , Issue.1-3 , pp. 56-62
    • Hakli, M.1    Lorick, K.L.2    Weissman, A.M.3    Janne, O.A.4    Palvimo, J.J.5
  • 44
    • 13544254439 scopus 로고    scopus 로고
    • SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies
    • DOI 10.1016/j.yexcr.2004.10.029
    • Hakli M., Karvonen U., Janne O.A., and Palvimo J.J. SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies Exp. Cell Res. 304 2005 224 233 (Pubitemid 40222089)
    • (2005) Experimental Cell Research , vol.304 , Issue.1 , pp. 224-233
    • Hakli, M.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 46
    • 33646838989 scopus 로고    scopus 로고
    • Sumoylation inhibits cleavage of Sp1 N-terminal Negative regulatory domain and inhibits Sp1-dependent transcription
    • DOI 10.1074/jbc.M600035200
    • Spengler M.L., and Brattain M.G. Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription J. Biol. Chem. 281 2006 5567 5574 (Pubitemid 43847653)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5567-5574
    • Spengler, M.L.1    Brattain, M.G.2
  • 47
    • 1642535446 scopus 로고    scopus 로고
    • Fibroblast Growth Factor-2 Represses Platelet-derived Growth Factor Receptor-α (PDGFR-α) Transcription via ERK1/2-dependent Sp1 Phosphorylation and an Atypical cis-Acting Element in the Proximal PDGFR-α Promoter
    • DOI 10.1074/jbc.M308254200
    • Bonello M.R., and Khachigian L.M. Fibroblast growth factor-2 represses platelet-derived growth factor receptor-α (PDGFR-α) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-α promoter J. Biol. Chem. 279 2004 2377 2382 (Pubitemid 38114220)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2377-2382
    • Bonello, M.R.1    Khachigian, L.M.2
  • 48
    • 66349099956 scopus 로고    scopus 로고
    • Sp1 phosphorylation and its regulation of gene transcription
    • Tan N.Y., and Khachigian L.M. Sp1 phosphorylation and its regulation of gene transcription Mol. Cell. Biol. 29 2009 2483 2488
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2483-2488
    • Tan, N.Y.1    Khachigian, L.M.2
  • 49
    • 41849083427 scopus 로고    scopus 로고
    • Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation
    • Spengler M.L., Guo L.W., and Brattain M.G. Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation Cell Cycle 7 2008 623 630 (Pubitemid 351499001)
    • (2008) Cell Cycle , vol.7 , Issue.5 , pp. 623-630
    • Spengler, M.L.1    Guo, L.-W.2    Brattain, M.G.3
  • 50
    • 66149124844 scopus 로고    scopus 로고
    • Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation
    • Abdel-Hafiz H., Dudevoir M.L., and Horwitz K.B. Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation J. Biol. Chem. 284 2009 9099 9108
    • (2009) J. Biol. Chem. , vol.284 , pp. 9099-9108
    • Abdel-Hafiz, H.1    Dudevoir, M.L.2    Horwitz, K.B.3
  • 51
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • DOI 10.1093/emboj/17.1.61
    • Muller S., Matunis M.J., and Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus EMBO J. 17 1998 61 70 (Pubitemid 28041048)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 53
    • 1342271367 scopus 로고    scopus 로고
    • SUMO and transcriptional repression: Dynamic interactions between the MAP kinase and SUMO pathways
    • Yang S.H., Jaffray E., Senthinathan B., Hay R.T., and Sharrocks A.D. SUMO and transcriptional repression: dynamic interactions between the MAP kinase and SUMO pathways Cell Cycle 2 2003 528 530
    • (2003) Cell Cycle , vol.2 , pp. 528-530
    • Yang, S.H.1    Jaffray, E.2    Senthinathan, B.3    Hay, R.T.4    Sharrocks, A.D.5
  • 54
    • 67649866042 scopus 로고    scopus 로고
    • Thiazolidinediones mimic glucose starvation in facilitating Sp1 degradation through the up-regulation of β-transducin repeat-containing protein
    • Wei S., Chuang H.C., Tsai W.C., Yang H.C., Ho S.R., and Paterson A.J. Thiazolidinediones mimic glucose starvation in facilitating Sp1 degradation through the up-regulation of β-transducin repeat-containing protein Mol. Pharmacol. 76 2009 47 57
    • (2009) Mol. Pharmacol. , vol.76 , pp. 47-57
    • Wei, S.1    Chuang, H.C.2    Tsai, W.C.3    Yang, H.C.4    Ho, S.R.5    Paterson, A.J.6
  • 55
    • 0033591451 scopus 로고    scopus 로고
    • An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro
    • Su K., Roos M.D., Yang X., Han I., Paterson A.J., and Kudlow J.E. An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro J. Biol. Chem. 274 1999 15194 15202
    • (1999) J. Biol. Chem. , vol.274 , pp. 15194-15202
    • Su, K.1    Roos, M.D.2    Yang, X.3    Han, I.4    Paterson, A.J.5    Kudlow, J.E.6
  • 56
    • 78649676124 scopus 로고    scopus 로고
    • Efficacy and tolerability of extended release quetiapine fumarate (quetiapine XR) monotherapy in major depressive disorder: A placebo-controlled, randomized study
    • Bortnick B., El-Khalili N., Banov M., Adson D., Datto C., and Raines S. Efficacy and tolerability of extended release quetiapine fumarate (quetiapine XR) monotherapy in major depressive disorder: a placebo-controlled, randomized study J. Affect. Disord. 128 2011 83 94
    • (2011) J. Affect. Disord. , vol.128 , pp. 83-94
    • Bortnick, B.1    El-Khalili, N.2    Banov, M.3    Adson, D.4    Datto, C.5    Raines, S.6


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