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Volumn 331, Issue 1, 2015, Pages 58-72

Withaferin A disrupts ubiquitin-based NEMO reorganization induced by canonical NF-κB signaling

Author keywords

ABC type diffuse large B cell lymphoma; Apoptosis; IKK; NEMO; NEMO foci; NF B; Ubiquitin; Withaferin A

Indexed keywords

I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; POLYUBIQUITIN; UBIQUITIN; WITHAFERIN A; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEMO PROTEIN, MOUSE; SIGNAL PEPTIDE; TUMOR NECROSIS FACTOR; WITHANOLIDE;

EID: 84921282213     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2014.09.034     Document Type: Article
Times cited : (27)

References (77)
  • 1
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-kappaB in cancer development and progression
    • Karin M. Nuclear factor-kappaB in cancer development and progression. Nature 2006, 441:431-436. 10.1038/nature04870.
    • (2006) Nature , vol.441 , pp. 431-436
    • Karin, M.1
  • 2
    • 0036546501 scopus 로고    scopus 로고
    • NF-kappaB in cancer: from innocent bystander to major culprit
    • Karin M., Cao Y., Greten F.R., Li Z.-W. NF-kappaB in cancer: from innocent bystander to major culprit. Nat. Rev. Cancer 2002, 2:301-310. 10.1038/nrc780.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.-W.4
  • 3
    • 33749078761 scopus 로고    scopus 로고
    • NF-kappaB in solid tumors
    • Pacifico F., Leonardi A. NF-kappaB in solid tumors. Biochem. Pharmacol. 2006, 72:1142-1152. 10.1016/j.bcp.2006.07.032.
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1142-1152
    • Pacifico, F.1    Leonardi, A.2
  • 4
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins N.D. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 2007, 8:49-62. 10.1038/nrm2083.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 5
    • 84856213846 scopus 로고    scopus 로고
    • The diverse and complex roles of NF-κB subunits in cancer
    • Perkins N.D. The diverse and complex roles of NF-κB subunits in cancer. Nat. Rev. Cancer 2012, 12:121-132. 10.1038/nrc3204.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 121-132
    • Perkins, N.D.1
  • 6
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa B transcription factor
    • Baeuerle P.A., Baltimore D. I kappa B: a specific inhibitor of the NF-kappa B transcription factor. Science 1988, 242:540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • Adhikari A., Xu M., Chen Z.J. Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 2007, 26:3214-3226. 10.1038/sj.onc.1210413.
    • (2007) Oncogene , vol.26 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 8
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • Kanayama A., Seth R.B., Sun L., Ea C.-K., Hong M., Shaito A., et al. TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol. Cell 2004, 15:535-548. 10.1016/j.molcel.2004.08.008.
    • (2004) Mol. Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.-K.4    Hong, M.5    Shaito, A.6
  • 9
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • Brown K., Gerstberger S., Carlson L., Franzoso G., Siebenlist U. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 1995, 267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 10
    • 0032541657 scopus 로고    scopus 로고
    • IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex
    • Rothwarf D.M., Zandi E., Natoli G., Karin M. IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex. Nature 1998, 395:297-300. 10.1038/26261.
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 11
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP
    • Spencer E., Jiang J., Chen Z.J. Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. Genes Dev. 1999, 13:284-294.
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 12
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 1998, 93:1231-1240.
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6
  • 13
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway
    • Senftleben U., Cao Y., Xiao G., Greten F.R., Krähn G., Bonizzi G., et al. Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway. Science 2001, 293:1495-1499. 10.1126/science.1062677.
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1    Cao, Y.2    Xiao, G.3    Greten, F.R.4    Krähn, G.5    Bonizzi, G.6
  • 14
    • 0034745420 scopus 로고    scopus 로고
    • NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100
    • Xiao G., Harhaj E.W., Sun S.C. NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100. Mol. Cell 2001, 7:401-409.
    • (2001) Mol. Cell , vol.7 , pp. 401-409
    • Xiao, G.1    Harhaj, E.W.2    Sun, S.C.3
  • 16
    • 0028181648 scopus 로고
    • Enhanced I kappa B alpha degradation is responsible for constitutive NF-kappa B activity in mature murine B-cell lines
    • Miyamoto S., Chiao P.J., Verma I.M. Enhanced I kappa B alpha degradation is responsible for constitutive NF-kappa B activity in mature murine B-cell lines. Mol. Cell. Biol. 1994, 14:3276-3282.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3276-3282
    • Miyamoto, S.1    Chiao, P.J.2    Verma, I.M.3
  • 17
    • 0030927167 scopus 로고    scopus 로고
    • Constitutive activation of NF-kappaB during progression of breast cancer to hormone-independent growth
    • Nakshatri H., Bhat-Nakshatri P., Martin D.A., Goulet R.J., Sledge G.W. Constitutive activation of NF-kappaB during progression of breast cancer to hormone-independent growth. Mol. Cell. Biol. 1997, 17:3629-3639.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3629-3639
    • Nakshatri, H.1    Bhat-Nakshatri, P.2    Martin, D.A.3    Goulet, R.J.4    Sledge, G.W.5
  • 18
    • 1842579486 scopus 로고    scopus 로고
    • Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis
    • Bharti A.C., Shishodia S., Reuben J.M., Weber D., Alexanian R., Raj-Vadhan S., et al. Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis. Blood 2004, 103:3175-3184. 10.1182/blood-2003-06-2151.
    • (2004) Blood , vol.103 , pp. 3175-3184
    • Bharti, A.C.1    Shishodia, S.2    Reuben, J.M.3    Weber, D.4    Alexanian, R.5    Raj-Vadhan, S.6
  • 19
    • 0035905313 scopus 로고    scopus 로고
    • Constitutive nuclear factor kappaB activity is required for survival of activated B cell-like diffuse large B cell lymphoma cells
    • Davis R.E., Brown K.D., Siebenlist U., Staudt L.M. Constitutive nuclear factor kappaB activity is required for survival of activated B cell-like diffuse large B cell lymphoma cells. J. Exp. Med. 2001, 194:1861-1874.
    • (2001) J. Exp. Med. , vol.194 , pp. 1861-1874
    • Davis, R.E.1    Brown, K.D.2    Siebenlist, U.3    Staudt, L.M.4
  • 20
    • 61349144249 scopus 로고    scopus 로고
    • ATM mediates constitutive NF-kappaB activation in high-risk myelodysplastic syndrome and acute myeloid leukemia
    • Grosjean-Raillard J., Tailler M., Adès L., Perfettini J.-L., Fabre C., Braun T., et al. ATM mediates constitutive NF-kappaB activation in high-risk myelodysplastic syndrome and acute myeloid leukemia. Oncogene 2009, 28:1099-1109. 10.1038/onc.2008.457.
    • (2009) Oncogene , vol.28 , pp. 1099-1109
    • Grosjean-Raillard, J.1    Tailler, M.2    Adès, L.3    Perfettini, J.-L.4    Fabre, C.5    Braun, T.6
  • 21
    • 79551686422 scopus 로고    scopus 로고
    • Oncogenically active MYD88 mutations in human lymphoma
    • Ngo V.N., Young R.M., Schmitz R., Jhavar S., Xiao W., Lim K.-H., et al. Oncogenically active MYD88 mutations in human lymphoma. Nature 2011, 470:115-119. 10.1038/nature09671.
    • (2011) Nature , vol.470 , pp. 115-119
    • Ngo, V.N.1    Young, R.M.2    Schmitz, R.3    Jhavar, S.4    Xiao, W.5    Lim, K.-H.6
  • 22
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes
    • Shembade N., Ma A., Harhaj E.W. Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes. Science 2010, 327:1135-1139. 10.1126/science.1182364.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 23
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 2003, 424:793-796. 10.1038/nature01803.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 24
    • 0034598746 scopus 로고    scopus 로고
    • Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling
    • Alizadeh A.A., Eisen M.B., Davis R.E., Ma C., Lossos I.S., Rosenwald A., et al. Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling. Nature 2000, 403:503-511. 10.1038/35000501.
    • (2000) Nature , vol.403 , pp. 503-511
    • Alizadeh, A.A.1    Eisen, M.B.2    Davis, R.E.3    Ma, C.4    Lossos, I.S.5    Rosenwald, A.6
  • 25
    • 0141672946 scopus 로고    scopus 로고
    • Molecular diagnosis of primary mediastinal B cell lymphoma identifies a clinically favorable subgroup of diffuse large B cell lymphoma related to Hodgkin lymphoma
    • Rosenwald A., Wright G., Leroy K., Yu X., Gaulard P., Gascoyne R.D., et al. Molecular diagnosis of primary mediastinal B cell lymphoma identifies a clinically favorable subgroup of diffuse large B cell lymphoma related to Hodgkin lymphoma. J. Exp. Med. 2003, 198:851-862. 10.1084/jem.20031074.
    • (2003) J. Exp. Med. , vol.198 , pp. 851-862
    • Rosenwald, A.1    Wright, G.2    Leroy, K.3    Yu, X.4    Gaulard, P.5    Gascoyne, R.D.6
  • 26
    • 33750446341 scopus 로고    scopus 로고
    • Inhibitors of NF-κB signaling: 785 and counting
    • Gilmore T.D., Herscovitch M. Inhibitors of NF-κB signaling: 785 and counting. Oncogene 2006, 25:6887-6899. 10.1038/sj.onc.1209982.
    • (2006) Oncogene , vol.25 , pp. 6887-6899
    • Gilmore, T.D.1    Herscovitch, M.2
  • 27
    • 78650871053 scopus 로고    scopus 로고
    • Small molecule inhibitors of NF-κB and JAK/STAT signal transduction pathways as promising anti-inflammatory therapeutics
    • Ivanenkov Y.A., Balakin K.V., Lavrovsky Y. Small molecule inhibitors of NF-κB and JAK/STAT signal transduction pathways as promising anti-inflammatory therapeutics. Mini-Rev. Med. Chem. 2011, 11:55-78. 10.2174/138955711793564079.
    • (2011) Mini-Rev. Med. Chem. , vol.11 , pp. 55-78
    • Ivanenkov, Y.A.1    Balakin, K.V.2    Lavrovsky, Y.3
  • 28
    • 4444306858 scopus 로고    scopus 로고
    • The IkappaB kinase (IKK) inhibitor, NEMO-binding domain peptide, blocks osteoclastogenesis and bone erosion in inflammatory arthritis
    • Dai S., Hirayama T., Abbas S., Abu-Amer Y. The IkappaB kinase (IKK) inhibitor, NEMO-binding domain peptide, blocks osteoclastogenesis and bone erosion in inflammatory arthritis. J. Biol. Chem. 2004, 279:37219-37222. 10.1074/jbc.C400258200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37219-37222
    • Dai, S.1    Hirayama, T.2    Abbas, S.3    Abu-Amer, Y.4
  • 29
    • 79960394765 scopus 로고    scopus 로고
    • NEMO-binding domain peptide inhibits constitutive NF-κB activity and reduces tumor burden in a canine model of relapsed, refractory diffuse large B-cell lymphoma
    • Gaurnier-Hausser A., Patel R., Baldwin A.S., May M.J., Mason N.J. NEMO-binding domain peptide inhibits constitutive NF-κB activity and reduces tumor burden in a canine model of relapsed, refractory diffuse large B-cell lymphoma. Clin. Cancer Res. 2011, 17:4661-4671. 10.1158/1078-0432.CCR-10-3310.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 4661-4671
    • Gaurnier-Hausser, A.1    Patel, R.2    Baldwin, A.S.3    May, M.J.4    Mason, N.J.5
  • 30
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex
    • May M.J., D'Acquisto F., Madge L.A., Glöckner J., Pober J.S., Ghosh S. Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science 2000, 289:1550-1554.
    • (2000) Science , vol.289 , pp. 1550-1554
    • May, M.J.1    D'Acquisto, F.2    Madge, L.A.3    Glöckner, J.4    Pober, J.S.5    Ghosh, S.6
  • 31
    • 33750358664 scopus 로고    scopus 로고
    • Use of cell permeable NBD peptides for suppression of inflammation
    • Strickland I., Ghosh S. Use of cell permeable NBD peptides for suppression of inflammation. Ann. Rheum. Dis. 2006, 65(Suppl 3):iii75-iii82. 10.1136/ard.2006.058438.
    • (2006) Ann. Rheum. Dis. , vol.65 , pp. 375-382
    • Strickland, I.1    Ghosh, S.2
  • 32
    • 78649785240 scopus 로고    scopus 로고
    • Inhibition of the NEMO/IKKβ association complex formation, a novel mechanism associated with the NF-κB activation suppression by Withania somnifera's key metabolite withaferin A
    • Grover A., Shandilya A., Punetha A., Bisaria V.S., Sundar D. Inhibition of the NEMO/IKKβ association complex formation, a novel mechanism associated with the NF-κB activation suppression by Withania somnifera's key metabolite withaferin A. BMC Genomics 2010, 11(Suppl 4):S25. 10.1186/1471-2164-11-S4-S25.
    • (2010) BMC Genomics , vol.11 , pp. S25
    • Grover, A.1    Shandilya, A.2    Punetha, A.3    Bisaria, V.S.4    Sundar, D.5
  • 33
    • 0016701762 scopus 로고
    • Mode of action of Withaferin A and Withanolide D
    • Chowdhury K., Neogy R.K. Mode of action of Withaferin A and Withanolide D. Biochem. Pharmacol. 1975, 24:919-920.
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 919-920
    • Chowdhury, K.1    Neogy, R.K.2
  • 35
    • 33746048055 scopus 로고    scopus 로고
    • Withanolides potentiate apoptosis, inhibit invasion, and abolish osteoclastogenesis through suppression of nuclear factor-kappaB (NF-kappaB) activation and NF-kappaB-regulated gene expression
    • Ichikawa H., Takada Y., Shishodia S., Jayaprakasam B., Nair M.G., Aggarwal B.B. Withanolides potentiate apoptosis, inhibit invasion, and abolish osteoclastogenesis through suppression of nuclear factor-kappaB (NF-kappaB) activation and NF-kappaB-regulated gene expression. Mol. Cancer Ther. 2006, 5:1434-1445. 10.1158/1535-7163.MCT-06-0096.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1434-1445
    • Ichikawa, H.1    Takada, Y.2    Shishodia, S.3    Jayaprakasam, B.4    Nair, M.G.5    Aggarwal, B.B.6
  • 36
    • 63549126249 scopus 로고    scopus 로고
    • Withaferin A inhibits tumor necrosis factor-alpha-induced expression of cell adhesion molecules by inactivation of Akt and NF-kappaB in human pulmonary epithelial cells
    • Oh J.H., Kwon T.K. Withaferin A inhibits tumor necrosis factor-alpha-induced expression of cell adhesion molecules by inactivation of Akt and NF-kappaB in human pulmonary epithelial cells. Int. Immunopharmacol. 2009, 9:614-619. 10.1016/j.intimp.2009.02.002.
    • (2009) Int. Immunopharmacol. , vol.9 , pp. 614-619
    • Oh, J.H.1    Kwon, T.K.2
  • 37
    • 80053309063 scopus 로고    scopus 로고
    • Withaferin A inhibits breast cancer invasion and metastasis at sub-cytotoxic doses by inducing vimentin disassembly and serine 56 phosphorylation
    • Thaiparambil J.T., Bender L., Ganesh T., Kline E., Patel P., Liu Y., et al. Withaferin A inhibits breast cancer invasion and metastasis at sub-cytotoxic doses by inducing vimentin disassembly and serine 56 phosphorylation. Int. J. Cancer 2011, 129:2744-2755. 10.1002/ijc.25938.
    • (2011) Int. J. Cancer , vol.129 , pp. 2744-2755
    • Thaiparambil, J.T.1    Bender, L.2    Ganesh, T.3    Kline, E.4    Patel, P.5    Liu, Y.6
  • 38
    • 33947530134 scopus 로고    scopus 로고
    • Withaferin a strongly elicits IkappaB kinase beta hyperphosphorylation concomitant with potent inhibition of its kinase activity
    • Kaileh M., Vanden Berghe W., Heyerick A., Horion J., Piette J., Libert C., et al. Withaferin a strongly elicits IkappaB kinase beta hyperphosphorylation concomitant with potent inhibition of its kinase activity. J. Biol. Chem. 2007, 282:4253-4264. 10.1074/jbc.M606728200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4253-4264
    • Kaileh, M.1    Vanden Berghe, W.2    Heyerick, A.3    Horion, J.4    Piette, J.5    Libert, C.6
  • 39
    • 84884665456 scopus 로고    scopus 로고
    • Identifying post-translational modifications of NEMO by tandem mass spectrometry after high affinity purification
    • Jackson S.S., Coughlin E.E., Coon J.J., Miyamoto S. Identifying post-translational modifications of NEMO by tandem mass spectrometry after high affinity purification. Protein Expr. Purif. 2013, 92:48-53. 10.1016/j.pep.2013.08.020.
    • (2013) Protein Expr. Purif. , vol.92 , pp. 48-53
    • Jackson, S.S.1    Coughlin, E.E.2    Coon, J.J.3    Miyamoto, S.4
  • 40
    • 0036315743 scopus 로고    scopus 로고
    • The zinc finger domain of NEMO is selectively required for NF-kappa B activation by UV radiation and topoisomerase inhibitors
    • Huang T.T., Feinberg S.L., Suryanarayanan S., Miyamoto S. The zinc finger domain of NEMO is selectively required for NF-kappa B activation by UV radiation and topoisomerase inhibitors. Mol. Cell. Biol. 2002, 22:5813-5825.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5813-5825
    • Huang, T.T.1    Feinberg, S.L.2    Suryanarayanan, S.3    Miyamoto, S.4
  • 41
    • 0031594708 scopus 로고    scopus 로고
    • Novel IkappaB alpha proteolytic pathway in WEHI231 immature B cells
    • Miyamoto S., Seufzer B.J., Shumway S.D. Novel IkappaB alpha proteolytic pathway in WEHI231 immature B cells. Mol. Cell. Biol. 1998, 18:19-29.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 19-29
    • Miyamoto, S.1    Seufzer, B.J.2    Shumway, S.D.3
  • 42
    • 0028365496 scopus 로고
    • Qualitative changes in the subunit composition of kappa B-binding complexes during murine B-cell differentiation
    • Miyamoto S., Schmitt M.J., Verma I.M. Qualitative changes in the subunit composition of kappa B-binding complexes during murine B-cell differentiation. Proc. Natl. Acad. Sci. USA 1994, 91:5056-5060.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5056-5060
    • Miyamoto, S.1    Schmitt, M.J.2    Verma, I.M.3
  • 43
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes
    • Huang T.T., Kudo N., Yoshida M., Miyamoto S. A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes. Proc. Natl. Acad. Sci. USA 2000, 97:1014-1019.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 44
    • 77957374335 scopus 로고    scopus 로고
    • ATM- and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress
    • Wu Z.-H., Wong E.T., Shi Y., Niu J., Chen Z., Miyamoto S., et al. ATM- and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress. Mol. Cell 2010, 40:75-86. 10.1016/j.molcel.2010.09.010.
    • (2010) Mol. Cell , vol.40 , pp. 75-86
    • Wu, Z.-H.1    Wong, E.T.2    Shi, Y.3    Niu, J.4    Chen, Z.5    Miyamoto, S.6
  • 46
    • 33645977821 scopus 로고    scopus 로고
    • Ubiquitin, TAK1 and IKK: is there a connection?
    • Chen Z.J., Bhoj V., Seth R.B. Ubiquitin, TAK1 and IKK: is there a connection?. Cell Death Differ. 2006, 13:687-692. 10.1038/sj.cdd.4401869.
    • (2006) Cell Death Differ. , vol.13 , pp. 687-692
    • Chen, Z.J.1    Bhoj, V.2    Seth, R.B.3
  • 48
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 2001, 412:346-351. 10.1038/35085597.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5    Chen, Z.J.6
  • 49
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea C.-K., Deng L., Xia Z.-P., Pineda G., Chen Z.J. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 2006, 22:245-257. 10.1016/j.molcel.2006.03.026.
    • (2006) Mol. Cell , vol.22 , pp. 245-257
    • Ea, C.-K.1    Deng, L.2    Xia, Z.-P.3    Pineda, G.4    Chen, Z.J.5
  • 50
    • 84895822094 scopus 로고    scopus 로고
    • Mechanism underlying IκB kinase activation mediated by the linear ubiquitin chain assembly complex
    • Fujita H., Rahighi S., Akita M., Kato R., Sasaki Y., Wakatsuki S., et al. Mechanism underlying IκB kinase activation mediated by the linear ubiquitin chain assembly complex. Mol. Cell. Biol. 2014, 34:1322-1335. 10.1128/MCB.01538-13.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1322-1335
    • Fujita, H.1    Rahighi, S.2    Akita, M.3    Kato, R.4    Sasaki, Y.5    Wakatsuki, S.6
  • 51
    • 70350020147 scopus 로고    scopus 로고
    • NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine E., Fontan E., Chiaravalli J., Lopez T., Lakisic G., Véron M., et al. NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J. 2009, 28:2885-2895. 10.1038/emboj.2009.241.
    • (2009) EMBO J. , vol.28 , pp. 2885-2895
    • Laplantine, E.1    Fontan, E.2    Chiaravalli, J.3    Lopez, T.4    Lakisic, G.5    Véron, M.6
  • 52
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation
    • Rahighi S., Ikeda F., Kawasaki M., Akutsu M., Suzuki N., Kato R., et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Cell 2009, 136:1098-1109. 10.1016/j.cell.2009.03.007.
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1    Ikeda, F.2    Kawasaki, M.3    Akutsu, M.4    Suzuki, N.5    Kato, R.6
  • 53
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • Wu C.-J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat. Cell Biol. 2006, 8:398-406. 10.1038/ncb1384.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 398-406
    • Wu, C.-J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 55
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 2011, 471:591-596. 10.1038/nature09816.
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1    Cordier, S.M.2    Schmukle, A.C.3    Emmerich, C.H.4    Rieser, E.5    Haas, T.L.6
  • 56
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A., Cook A., Lin Y., Rodriguez Y., Kelliher M., Liu Z. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 2000, 12:419-429.
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 57
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation
    • Li H., Kobayashi M., Blonska M., You Y., Lin X. Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation. J. Biol. Chem. 2006, 281:13636-13643. 10.1074/jbc.M600620200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 58
    • 0032589935 scopus 로고    scopus 로고
    • IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex
    • Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B., Li J.W., et al. IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex. Mol. Cell. Biol. 1999, 19:1526-1538.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1526-1538
    • Mercurio, F.1    Murray, B.W.2    Shevchenko, A.3    Bennett, B.L.4    Young, D.B.5    Li, J.W.6
  • 59
    • 0034175632 scopus 로고    scopus 로고
    • Severe liver degeneration and lack of NF-kappaB activation in NEMO/IKKgamma-deficient mice
    • Rudolph D., Yeh W.C., Wakeham A., Rudolph B., Nallainathan D., Potter J., et al. Severe liver degeneration and lack of NF-kappaB activation in NEMO/IKKgamma-deficient mice. Genes Dev. 2000, 14:854-862.
    • (2000) Genes Dev. , vol.14 , pp. 854-862
    • Rudolph, D.1    Yeh, W.C.2    Wakeham, A.3    Rudolph, B.4    Nallainathan, D.5    Potter, J.6
  • 60
    • 58149202128 scopus 로고    scopus 로고
    • Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls
    • Baud V., Karin M. Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls. Nat. Rev. Drug Discov. 2009, 8:33-40. 10.1038/nrd2781.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 33-40
    • Baud, V.1    Karin, M.2
  • 61
    • 4944239830 scopus 로고    scopus 로고
    • A 32-week randomized, placebo-controlled clinical evaluation of RA-11, an Ayurvedic drug, on osteoarthritis of the knees
    • Chopra A., Lavin P., Patwardhan B., Chitre D. A 32-week randomized, placebo-controlled clinical evaluation of RA-11, an Ayurvedic drug, on osteoarthritis of the knees. J. Clin. Rheumatol. 2004, 10:236-245. 10.1097/01.rhu.0000138087.47382.6d.
    • (2004) J. Clin. Rheumatol. , vol.10 , pp. 236-245
    • Chopra, A.1    Lavin, P.2    Patwardhan, B.3    Chitre, D.4
  • 62
    • 69949168009 scopus 로고    scopus 로고
    • Naturopathic care for anxiety: a randomized controlled trial ISRCTN78958974
    • Cooley K., Szczurko O., Perri D., Mills E.J., Bernhardt B., Zhou Q., et al. Naturopathic care for anxiety: a randomized controlled trial ISRCTN78958974. PLoS One 2009, 4:e6628. 10.1371/journal.pone.0006628.
    • (2009) PLoS One , vol.4 , pp. e6628
    • Cooley, K.1    Szczurko, O.2    Perri, D.3    Mills, E.J.4    Bernhardt, B.5    Zhou, Q.6
  • 63
    • 84921294882 scopus 로고    scopus 로고
    • Withania somnifera: From Ayurveda towards Western medical practice: a systematic review
    • (accessed 13.6.14), Studium Press L.L.C., Houston, TX, 237-256
    • Werneke U. Withania somnifera: From Ayurveda towards Western medical practice: a systematic review. Recent Progress in Medicinal Plants: Search for Natural Drugs 2009, (accessed 13.6.14), Studium Press L.L.C., Houston, TX, 237-256.
    • (2009) Recent Progress in Medicinal Plants: Search for Natural Drugs
    • Werneke, U.1
  • 64
    • 84892852412 scopus 로고    scopus 로고
    • TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO-IKK supramolecular structures
    • Tarantino N., Tinevez J.-Y., Crowell E.F., Boisson B., Henriques R., Mhlanga M., et al. TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO-IKK supramolecular structures. J. Cell Biol. 2014, 204:231-245. 10.1083/jcb.201307172.
    • (2014) J. Cell Biol. , vol.204 , pp. 231-245
    • Tarantino, N.1    Tinevez, J.-Y.2    Crowell, E.F.3    Boisson, B.4    Henriques, R.5    Mhlanga, M.6
  • 65
    • 33751200630 scopus 로고    scopus 로고
    • IKKalpha regulates the mitotic phase of the cell cycle by modulating Aurora A phosphorylation
    • Prajapati S., Tu Z., Yamamoto Y., Gaynor R.B. IKKalpha regulates the mitotic phase of the cell cycle by modulating Aurora A phosphorylation. Cell Cycle 2006, 5:2371-2380.
    • (2006) Cell Cycle , vol.5 , pp. 2371-2380
    • Prajapati, S.1    Tu, Z.2    Yamamoto, Y.3    Gaynor, R.B.4
  • 66
    • 84871999611 scopus 로고    scopus 로고
    • Human T cell leukemia virus type 2 tax-mediated NF-κB activation involves a mechanism independent of Tax conjugation to ubiquitin and SUMO
    • Journo C., Bonnet A., Favre-Bonvin A., Turpin J., Vinera J., CÔté E., et al. Human T cell leukemia virus type 2 tax-mediated NF-κB activation involves a mechanism independent of Tax conjugation to ubiquitin and SUMO. J. Virol. 2013, 87:1123-1136. 10.1128/JVI.01792-12.
    • (2013) J. Virol. , vol.87 , pp. 1123-1136
    • Journo, C.1    Bonnet, A.2    Favre-Bonvin, A.3    Turpin, J.4    Vinera, J.5    Côté, E.6
  • 67
    • 78650985961 scopus 로고    scopus 로고
    • Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome
    • Kfoury Y., Setterblad N., El-Sabban M., Zamborlini A., Dassouki Z., El Hajj H., et al. Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome. Blood 2011, 117:190-199. 10.1182/blood-2010-05-285742.
    • (2011) Blood , vol.117 , pp. 190-199
    • Kfoury, Y.1    Setterblad, N.2    El-Sabban, M.3    Zamborlini, A.4    Dassouki, Z.5    El Hajj, H.6
  • 68
    • 84870579566 scopus 로고    scopus 로고
    • Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance
    • Khan S., Rammeloo A.W., Heikkila J.J. Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance. PLoS One 2012, 7:e50547. 10.1371/journal.pone.0050547.
    • (2012) PLoS One , vol.7
    • Khan, S.1    Rammeloo, A.W.2    Heikkila, J.J.3
  • 69
    • 84882721062 scopus 로고    scopus 로고
    • Withaferin A: a proteasomal inhibitor promotes healing after injury and exerts anabolic effect on osteoporotic bone
    • Khedgikar V., Kushwaha P., Gautam J., Verma A., Changkija B., Kumar A., et al. Withaferin A: a proteasomal inhibitor promotes healing after injury and exerts anabolic effect on osteoporotic bone. Cell Death Dis. 2013, 4:e778. 10.1038/cddis.2013.294.
    • (2013) Cell Death Dis. , vol.4 , pp. e778
    • Khedgikar, V.1    Kushwaha, P.2    Gautam, J.3    Verma, A.4    Changkija, B.5    Kumar, A.6
  • 70
    • 84865069079 scopus 로고    scopus 로고
    • Withaferin A inhibits the proteasome activity in mesothelioma in vitro and in vivo
    • Yang H., Wang Y., Cheryan V.T., Wu W., Cui C.Q., Polin L.A., et al. Withaferin A inhibits the proteasome activity in mesothelioma in vitro and in vivo. PLoS One 2012, 7:e41214. 10.1371/journal.pone.0041214.
    • (2012) PLoS One , vol.7 , pp. e41214
    • Yang, H.1    Wang, Y.2    Cheryan, V.T.3    Wu, W.4    Cui, C.Q.5    Polin, L.A.6
  • 71
    • 33846454701 scopus 로고    scopus 로고
    • The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from Indian winter cherry
    • Yang H., Shi G., Dou Q.P. The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from Indian winter cherry. Mol. Pharmacol. 2007, 71:426-437. 10.1124/mol.106.030015.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 426-437
    • Yang, H.1    Shi, G.2    Dou, Q.P.3
  • 72
    • 34250346795 scopus 로고    scopus 로고
    • The tumor inhibitor and antiangiogenic agent withaferin A targets the intermediate filament protein vimentin
    • Bargagna-Mohan P., Hamza A., Kim Y., Khuan Abby Ho Y., Mor-Vaknin N., Wendschlag N., et al. The tumor inhibitor and antiangiogenic agent withaferin A targets the intermediate filament protein vimentin. Chem. Biol. 2007, 14:623-634. 10.1016/j.chembiol.2007.04.010.
    • (2007) Chem. Biol. , vol.14 , pp. 623-634
    • Bargagna-Mohan, P.1    Hamza, A.2    Kim, Y.3    Khuan Abby Ho, Y.4    Mor-Vaknin, N.5    Wendschlag, N.6
  • 73
    • 84927005883 scopus 로고    scopus 로고
    • Withaferin A inhibits experimental epithelial-mesenchymal transition in MCF-10A cells and suppresses vimentin protein level in vivo in breast tumors
    • Lee J., Hahm E.-R., Marcus A.I., Singh S.V. Withaferin A inhibits experimental epithelial-mesenchymal transition in MCF-10A cells and suppresses vimentin protein level in vivo in breast tumors. Mol. Carcinog. 2013, 10.1002/mc.22110.
    • (2013) Mol. Carcinog.
    • Lee, J.1    Hahm, E.-R.2    Marcus, A.I.3    Singh, S.V.4
  • 74
    • 78149239365 scopus 로고    scopus 로고
    • Withaferin A inhibits activation of signal transducer and activator of transcription 3 in human breast cancer cells
    • Lee J., Hahm E.-R., Singh S.V. Withaferin A inhibits activation of signal transducer and activator of transcription 3 in human breast cancer cells. Carcinogenesis 2010, 31:1991-1998. 10.1093/carcin/bgq175.
    • (2010) Carcinogenesis , vol.31 , pp. 1991-1998
    • Lee, J.1    Hahm, E.-R.2    Singh, S.V.3
  • 76
    • 84928180770 scopus 로고    scopus 로고
    • Inhibition of VEGF: a novel mechanism to control angiogenesis by Withania somnifera's key metabolite Withaferin A
    • Saha S., Islam M.K., Shilpi J.A., Hasan S. Inhibition of VEGF: a novel mechanism to control angiogenesis by Withania somnifera's key metabolite Withaferin A. Silico Pharmacol. 2013, 1:1-9. 10.1186/2193-9616-1-11.
    • (2013) Silico Pharmacol. , vol.1 , pp. 1-9
    • Saha, S.1    Islam, M.K.2    Shilpi, J.A.3    Hasan, S.4
  • 77
    • 54749130365 scopus 로고    scopus 로고
    • Withaferin A causes FOXO3a- and Bim-dependent apoptosis and inhibits growth of human breast cancer cells in vivo
    • Stan S.D., Hahm E.-R., Warin R., Singh S.V. Withaferin A causes FOXO3a- and Bim-dependent apoptosis and inhibits growth of human breast cancer cells in vivo. Cancer Res. 2008, 68:7661-7669. 10.1158/0008-5472.CAN-08-1510.
    • (2008) Cancer Res. , vol.68 , pp. 7661-7669
    • Stan, S.D.1    Hahm, E.-R.2    Warin, R.3    Singh, S.V.4


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