{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T11:00:07Z","timestamp":1776078007618,"version":"3.50.1"},"reference-count":77,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2015,2,1]],"date-time":"2015-02-01T00:00:00Z","timestamp":1422748800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,2,1]],"date-time":"2015-02-01T00:00:00Z","timestamp":1422748800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["UL1TR0000427"],"award-info":[{"award-number":["UL1TR0000427"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32GM008692"],"award-info":[{"award-number":["T32GM008692"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["KL2TR000428"],"award-info":[{"award-number":["KL2TR000428"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["F30CA171840"],"award-info":[{"award-number":["F30CA171840"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01CA077474"],"award-info":[{"award-number":["R01CA077474"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM083681"],"award-info":[{"award-number":["R01GM083681"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Experimental Cell Research"],"published-print":{"date-parts":[[2015,2]]},"DOI":"10.1016\/j.yexcr.2014.09.034","type":"journal-article","created":{"date-parts":[[2014,10,9]],"date-time":"2014-10-09T06:09:40Z","timestamp":1412834980000},"page":"58-72","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":28,"title":["Withaferin A disrupts ubiquitin-based NEMO reorganization induced by canonical NF-\u03baB signaling"],"prefix":"10.1016","volume":"331","author":[{"given":"Shawn S.","family":"Jackson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher","family":"Oberley","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher P.","family":"Hooper","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kreg","family":"Grindle","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shelly","family":"Wuerzberger-Davis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jared","family":"Wolff","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin","family":"McCool","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lixin","family":"Rui","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shigeki","family":"Miyamoto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.yexcr.2014.09.034_bib1","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nature04870","article-title":"Nuclear factor-kappaB in cancer development and progression","volume":"441","author":"Karin","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib2","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/nrc780","article-title":"NF-kappaB in cancer: from innocent bystander to major culprit","volume":"2","author":"Karin","year":"2002","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.yexcr.2014.09.034_bib3","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1016\/j.bcp.2006.07.032","article-title":"NF-kappaB in solid tumors","volume":"72","author":"Pacifico","year":"2006","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib4","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrm2083","article-title":"Integrating cell-signalling pathways with NF-kappaB and IKK function","volume":"8","author":"Perkins","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib5","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1038\/nrc3204","article-title":"The diverse and complex roles of NF-\u03baB subunits in cancer","volume":"12","author":"Perkins","year":"2012","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.yexcr.2014.09.034_bib6","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1126\/science.3140380","article-title":"I kappa B: a specific inhibitor of the NF-kappa B transcription factor","volume":"242","author":"Baeuerle","year":"1988","journal-title":"Science"},{"key":"10.1016\/j.yexcr.2014.09.034_bib7","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.1038\/sj.onc.1210413","article-title":"Ubiquitin-mediated activation of TAK1 and IKK","volume":"26","author":"Adhikari","year":"2007","journal-title":"Oncogene"},{"key":"10.1016\/j.yexcr.2014.09.034_bib8","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.molcel.2004.08.008","article-title":"TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains","volume":"15","author":"Kanayama","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1016\/j.yexcr.2014.09.034_bib9","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1126\/science.7878466","article-title":"Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation","volume":"267","author":"Brown","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.yexcr.2014.09.034_bib10","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/26261","article-title":"IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex","volume":"395","author":"Rothwarf","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib11","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1101\/gad.13.3.284","article-title":"Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb\/beta-TrCP","volume":"13","author":"Spencer","year":"1999","journal-title":"Genes Dev."},{"key":"10.1016\/j.yexcr.2014.09.034_bib12","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/S0092-8674(00)81466-X","article-title":"Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation","volume":"93","author":"Yamaoka","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.yexcr.2014.09.034_bib13","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1126\/science.1062677","article-title":"Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway","volume":"293","author":"Senftleben","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.yexcr.2014.09.034_bib14","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S1097-2765(01)00187-3","article-title":"NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100","volume":"7","author":"Xiao","year":"2001","journal-title":"Mol. Cell"},{"issue":"Pt 1","key":"10.1016\/j.yexcr.2014.09.034_bib15","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1042\/bj3040087","article-title":"Constitutive nuclear NF-kappa B in cells of the monocyte lineage","volume":"304","author":"Frankenberger","year":"1994","journal-title":"Biochem. J."},{"key":"10.1016\/j.yexcr.2014.09.034_bib16","first-page":"3276","article-title":"Enhanced I kappa B alpha degradation is responsible for constitutive NF-kappa B activity in mature murine B-cell lines","volume":"14","author":"Miyamoto","year":"1994","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib17","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1128\/MCB.17.7.3629","article-title":"Constitutive activation of NF-kappaB during progression of breast cancer to hormone-independent growth","volume":"17","author":"Nakshatri","year":"1997","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib18","doi-asserted-by":"crossref","first-page":"3175","DOI":"10.1182\/blood-2003-06-2151","article-title":"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","volume":"103","author":"Bharti","year":"2004","journal-title":"Blood"},{"key":"10.1016\/j.yexcr.2014.09.034_bib19","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1084\/jem.194.12.1861","article-title":"Constitutive nuclear factor kappaB activity is required for survival of activated B cell-like diffuse large B cell lymphoma cells","volume":"194","author":"Davis","year":"2001","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.yexcr.2014.09.034_bib20","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1038\/onc.2008.457","article-title":"ATM mediates constitutive NF-kappaB activation in high-risk myelodysplastic syndrome and acute myeloid leukemia","volume":"28","author":"Grosjean-Raillard","year":"2009","journal-title":"Oncogene"},{"key":"10.1016\/j.yexcr.2014.09.034_bib21","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1038\/nature09671","article-title":"Oncogenically active MYD88 mutations in human lymphoma","volume":"470","author":"Ngo","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib22","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1126\/science.1182364","article-title":"Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes","volume":"327","author":"Shembade","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.yexcr.2014.09.034_bib23","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1038\/nature01803","article-title":"CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members","volume":"424","author":"Trompouki","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib24","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/35000501","article-title":"Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling","volume":"403","author":"Alizadeh","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib25","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1084\/jem.20031074","article-title":"Molecular diagnosis of primary mediastinal B cell lymphoma identifies a clinically favorable subgroup of diffuse large B cell lymphoma related to Hodgkin lymphoma","volume":"198","author":"Rosenwald","year":"2003","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.yexcr.2014.09.034_bib26","doi-asserted-by":"crossref","first-page":"6887","DOI":"10.1038\/sj.onc.1209982","article-title":"Inhibitors of NF-\u03baB signaling: 785 and counting","volume":"25","author":"Gilmore","year":"2006","journal-title":"Oncogene"},{"key":"10.1016\/j.yexcr.2014.09.034_bib27","doi-asserted-by":"crossref","first-page":"55","DOI":"10.2174\/138955711793564079","article-title":"Small molecule inhibitors of NF-\u03baB and JAK\/STAT signal transduction pathways as promising anti-inflammatory therapeutics","volume":"11","author":"Ivanenkov","year":"2011","journal-title":"Mini-Rev. Med. Chem."},{"key":"10.1016\/j.yexcr.2014.09.034_bib28","doi-asserted-by":"crossref","first-page":"37219","DOI":"10.1074\/jbc.C400258200","article-title":"The IkappaB kinase (IKK) inhibitor, NEMO-binding domain peptide, blocks osteoclastogenesis and bone erosion in inflammatory arthritis","volume":"279","author":"Dai","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yexcr.2014.09.034_bib29","doi-asserted-by":"crossref","first-page":"4661","DOI":"10.1158\/1078-0432.CCR-10-3310","article-title":"NEMO-binding domain peptide inhibits constitutive NF-\u03baB activity and reduces tumor burden in a canine model of relapsed, refractory diffuse large B-cell lymphoma","volume":"17","author":"Gaurnier-Hausser","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.yexcr.2014.09.034_bib30","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1126\/science.289.5484.1550","article-title":"Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex","volume":"289","author":"May","year":"2000","journal-title":"Science"},{"issue":"Suppl 3","key":"10.1016\/j.yexcr.2014.09.034_bib31","doi-asserted-by":"crossref","first-page":"iii75","DOI":"10.1136\/ard.2006.058438","article-title":"Use of cell permeable NBD peptides for suppression of inflammation","volume":"65","author":"Strickland","year":"2006","journal-title":"Ann. Rheum. Dis."},{"issue":"Suppl 4","key":"10.1016\/j.yexcr.2014.09.034_bib32","doi-asserted-by":"crossref","first-page":"S25","DOI":"10.1186\/1471-2164-11-S4-S25","article-title":"Inhibition of the NEMO\/IKK\u03b2 association complex formation, a novel mechanism associated with the NF-\u03baB activation suppression by Withania somnifera\u05f3s key metabolite withaferin A","volume":"11","author":"Grover","year":"2010","journal-title":"BMC Genomics"},{"key":"10.1016\/j.yexcr.2014.09.034_bib33","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/0006-2952(75)90165-3","article-title":"Mode of action of Withaferin A and Withanolide D","volume":"24","author":"Chowdhury","year":"1975","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib34","first-page":"271","article-title":"Antitumor activity of withaferin A (NSC-101088)","volume":"51","author":"Shohat","year":"1967","journal-title":"Cancer Chemother. Rep."},{"key":"10.1016\/j.yexcr.2014.09.034_bib35","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.1158\/1535-7163.MCT-06-0096","article-title":"Withanolides potentiate apoptosis, inhibit invasion, and abolish osteoclastogenesis through suppression of nuclear factor-kappaB (NF-kappaB) activation and NF-kappaB-regulated gene expression","volume":"5","author":"Ichikawa","year":"2006","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.yexcr.2014.09.034_bib36","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.intimp.2009.02.002","article-title":"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","volume":"9","author":"Oh","year":"2009","journal-title":"Int. Immunopharmacol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib37","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1002\/ijc.25938","article-title":"Withaferin A inhibits breast cancer invasion and metastasis at sub-cytotoxic doses by inducing vimentin disassembly and serine 56 phosphorylation","volume":"129","author":"Thaiparambil","year":"2011","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.yexcr.2014.09.034_bib38","doi-asserted-by":"crossref","first-page":"4253","DOI":"10.1074\/jbc.M606728200","article-title":"Withaferin a strongly elicits IkappaB kinase beta hyperphosphorylation concomitant with potent inhibition of its kinase activity","volume":"282","author":"Kaileh","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yexcr.2014.09.034_bib39","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.pep.2013.08.020","article-title":"Identifying post-translational modifications of NEMO by tandem mass spectrometry after high affinity purification","volume":"92","author":"Jackson","year":"2013","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.yexcr.2014.09.034_bib40","doi-asserted-by":"crossref","first-page":"5813","DOI":"10.1128\/MCB.22.16.5813-5825.2002","article-title":"The zinc finger domain of NEMO is selectively required for NF-kappa B activation by UV radiation and topoisomerase inhibitors","volume":"22","author":"Huang","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib41","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1128\/MCB.18.1.19","article-title":"Novel IkappaB alpha proteolytic pathway in WEHI231 immature B cells","volume":"18","author":"Miyamoto","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib42","doi-asserted-by":"crossref","first-page":"5056","DOI":"10.1073\/pnas.91.11.5056","article-title":"Qualitative changes in the subunit composition of kappa B-binding complexes during murine B-cell differentiation","volume":"91","author":"Miyamoto","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.yexcr.2014.09.034_bib43","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1073\/pnas.97.3.1014","article-title":"A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB\/IkappaBalpha complexes","volume":"97","author":"Huang","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.yexcr.2014.09.034_bib44","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.molcel.2010.09.010","article-title":"ATM- and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress","volume":"40","author":"Wu","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.yexcr.2014.09.034_bib45","series-title":"Nonparametric Statistical Methods","author":"Hollander","year":"2013"},{"key":"10.1016\/j.yexcr.2014.09.034_bib46","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1038\/sj.cdd.4401869","article-title":"Ubiquitin, TAK1 and IKK: is there a connection?","volume":"13","author":"Chen","year":"2006","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.yexcr.2014.09.034_bib47","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0022-2836(02)01404-3","article-title":"TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway","volume":"326","author":"Takaesu","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib48","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/35085597","article-title":"TAK1 is a ubiquitin-dependent kinase of MKK and IKK","volume":"412","author":"Wang","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib49","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.molcel.2006.03.026","article-title":"Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO","volume":"22","author":"Ea","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/j.yexcr.2014.09.034_bib50","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1128\/MCB.01538-13","article-title":"Mechanism underlying I\u03baB kinase activation mediated by the linear ubiquitin chain assembly complex","volume":"34","author":"Fujita","year":"2014","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib51","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1038\/emboj.2009.241","article-title":"NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain","volume":"28","author":"Laplantine","year":"2009","journal-title":"EMBO J."},{"key":"10.1016\/j.yexcr.2014.09.034_bib52","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1016\/j.cell.2009.03.007","article-title":"Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation","volume":"136","author":"Rahighi","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.yexcr.2014.09.034_bib53","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/ncb1384","article-title":"Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]","volume":"8","author":"Wu","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib54","doi-asserted-by":"crossref","first-page":"2902","DOI":"10.1074\/jbc.M806655200","article-title":"The zinc finger of NEMO is a functional ubiquitin-binding domain","volume":"284","author":"Cordier","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yexcr.2014.09.034_bib55","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/nature09816","article-title":"Linear ubiquitination prevents inflammation and regulates immune signalling","volume":"471","author":"Gerlach","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.yexcr.2014.09.034_bib56","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/S1074-7613(00)80194-6","article-title":"The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation","volume":"12","author":"Devin","year":"2000","journal-title":"Immunity"},{"key":"10.1016\/j.yexcr.2014.09.034_bib57","doi-asserted-by":"crossref","first-page":"13636","DOI":"10.1074\/jbc.M600620200","article-title":"Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation","volume":"281","author":"Li","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yexcr.2014.09.034_bib58","doi-asserted-by":"crossref","first-page":"1526","DOI":"10.1128\/MCB.19.2.1526","article-title":"IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex","volume":"19","author":"Mercurio","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib59","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1101\/gad.14.7.854","article-title":"Severe liver degeneration and lack of NF-kappaB activation in NEMO\/IKKgamma-deficient mice","volume":"14","author":"Rudolph","year":"2000","journal-title":"Genes Dev."},{"key":"10.1016\/j.yexcr.2014.09.034_bib60","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/nrd2781","article-title":"Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls","volume":"8","author":"Baud","year":"2009","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.yexcr.2014.09.034_bib61","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1097\/01.rhu.0000138087.47382.6d","article-title":"A 32-week randomized, placebo-controlled clinical evaluation of RA-11, an Ayurvedic drug, on osteoarthritis of the knees","volume":"10","author":"Chopra","year":"2004","journal-title":"J. Clin. Rheumatol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib62","doi-asserted-by":"crossref","first-page":"e6628","DOI":"10.1371\/journal.pone.0006628","article-title":"Naturopathic care for anxiety: a randomized controlled trial ISRCTN78958974","volume":"4","author":"Cooley","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.yexcr.2014.09.034_bib63","series-title":"Recent Progress in Medicinal Plants: Search for Natural Drugs","article-title":"Withania somnifera: From Ayurveda towards Western medical practice: a systematic review","author":"Werneke","year":"2009"},{"key":"10.1016\/j.yexcr.2014.09.034_bib64","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1083\/jcb.201307172","article-title":"TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO\u2013IKK supramolecular structures","volume":"204","author":"Tarantino","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib65","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.4161\/cc.5.20.3359","article-title":"IKKalpha regulates the mitotic phase of the cell cycle by modulating Aurora A phosphorylation","volume":"5","author":"Prajapati","year":"2006","journal-title":"Cell Cycle"},{"key":"10.1016\/j.yexcr.2014.09.034_bib66","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1128\/JVI.01792-12","article-title":"Human T cell leukemia virus type 2 tax-mediated NF-\u03baB activation involves a mechanism independent of Tax conjugation to ubiquitin and SUMO","volume":"87","author":"Journo","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib67","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1182\/blood-2010-05-285742","article-title":"Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome","volume":"117","author":"Kfoury","year":"2011","journal-title":"Blood"},{"key":"10.1016\/j.yexcr.2014.09.034_bib68","doi-asserted-by":"crossref","first-page":"e50547","DOI":"10.1371\/journal.pone.0050547","article-title":"Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance","volume":"7","author":"Khan","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.yexcr.2014.09.034_bib69","doi-asserted-by":"crossref","first-page":"e778","DOI":"10.1038\/cddis.2013.294","article-title":"Withaferin A: a proteasomal inhibitor promotes healing after injury and exerts anabolic effect on osteoporotic bone","volume":"4","author":"Khedgikar","year":"2013","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.yexcr.2014.09.034_bib70","doi-asserted-by":"crossref","first-page":"e41214","DOI":"10.1371\/journal.pone.0041214","article-title":"Withaferin A inhibits the proteasome activity in mesothelioma in vitro and in vivo","volume":"7","author":"Yang","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.yexcr.2014.09.034_bib71","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1124\/mol.106.030015","article-title":"The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from Indian winter cherry","volume":"71","author":"Yang","year":"2007","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib72","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.chembiol.2007.04.010","article-title":"The tumor inhibitor and antiangiogenic agent withaferin A targets the intermediate filament protein vimentin","volume":"14","author":"Bargagna-Mohan","year":"2007","journal-title":"Chem. Biol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib73","article-title":"Withaferin A inhibits experimental epithelial-mesenchymal transition in MCF-10A cells and suppresses vimentin protein level in vivo in breast tumors","author":"Lee","year":"2013","journal-title":"Mol. Carcinog."},{"key":"10.1016\/j.yexcr.2014.09.034_bib74","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1093\/carcin\/bgq175","article-title":"Withaferin A inhibits activation of signal transducer and activator of transcription 3 in human breast cancer cells","volume":"31","author":"Lee","year":"2010","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.yexcr.2014.09.034_bib75","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s10456-004-1026-3","article-title":"Withaferin A is a potent inhibitor of angiogenesis","volume":"7","author":"Mohan","year":"2004","journal-title":"Angiogenesis"},{"key":"10.1016\/j.yexcr.2014.09.034_bib76","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/2193-9616-1-11","article-title":"Inhibition of VEGF: a novel mechanism to control angiogenesis by Withania somnifera\u05f3s key metabolite Withaferin A","volume":"1","author":"Saha","year":"2013","journal-title":"Silico Pharmacol."},{"key":"10.1016\/j.yexcr.2014.09.034_bib77","doi-asserted-by":"crossref","first-page":"7661","DOI":"10.1158\/0008-5472.CAN-08-1510","article-title":"Withaferin A causes FOXO3a- and Bim-dependent apoptosis and inhibits growth of human breast cancer cells in vivo","volume":"68","author":"Stan","year":"2008","journal-title":"Cancer Res."}],"container-title":["Experimental Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S001448271400439X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S001448271400439X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T05:15:12Z","timestamp":1762146912000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S001448271400439X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,2]]},"references-count":77,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2015,2]]}},"alternative-id":["S001448271400439X"],"URL":"https:\/\/doi.org\/10.1016\/j.yexcr.2014.09.034","relation":{},"ISSN":["0014-4827"],"issn-type":[{"value":"0014-4827","type":"print"}],"subject":[],"published":{"date-parts":[[2015,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Withaferin A disrupts ubiquitin-based NEMO reorganization induced by canonical NF-\u03baB signaling","name":"articletitle","label":"Article Title"},{"value":"Experimental Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.yexcr.2014.09.034","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}