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Ledoux, Constitutive and B-cell receptor-induced activation of STAT3 are important signaling pathways targeted by bortezomib in leukemic mantle cell lymphoma. Haematologica 95, 1865–1872 (2010)",{"doi":681},"10.3324\u002Fhaematol.2009.019745",{"id":20,"text":683,"url":20,"identifiers":684},"L.V. Pham, A.T. Tamayo, C. Li, W. Bornmann, W. Priebe, R.J. Ford, Degrasyn potentiates the antitumor effects of bortezomib in mantle cell lymphoma cells in vitro and in vivo: therapeutic implications. Mol. Cancer Ther. 9, 2026–2036 (2010)",{"doi":685},"10.1158\u002F1535-7163.MCT-10-0238",{"id":20,"text":687,"url":20,"identifiers":688},"S. Tauzin, H. Ding, K. Khatib, I. Ahmad, D. Burdevet, G. van Echten-Deckert, J.A. Lindquist, B. Schraven, N.U. Din, B. Borisch, D.C. Hoessli, Oncogenic association of the Cbp\u002FPAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts. Blood 111, 2310–2320 (2008)",{"doi":689},"10.1182\u002Fblood-2007-05-090985",{"id":20,"text":691,"url":20,"identifiers":692},"M.A. Yared, J.D. Khoury, L.J. Medeiros, G.Z. Rassidakis, R. Lai, Activation status of the JAK\u002FSTAT3 pathway in mantle cell lymphoma. Arch. Pathol. Lab. Med. 129, 990–996 (2005)",{"doi":693},"10.5858\u002F2005-129-990-ASOTSP",{"id":20,"text":695,"url":20,"identifiers":696},"R. Lai, G.Z. Rassidakis, L.J. Medeiros, V. Leventaki, M. Keating, T.J. McDonnell, Expression of STAT3 and its phosphorylated forms in mantle cell lymphoma cell lines and tumours. J. Pathol. 199, 84–89 (2003)",{"doi":697},"10.1002\u002Fpath.1253",{"id":20,"text":699,"url":20,"identifiers":700},"J.A. Diehl, M. Cheng, M.F. Roussel, C.J. Sherr, Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12, 3499–3511 (1998)",{"doi":701},"10.1101\u002Fgad.12.22.3499",{"id":20,"text":703,"url":20,"identifiers":704},"J. Camps, I. Salaverria, M.J. Garcia, E. Prat, S. Bea, J.C. Pole, L. Hernandez, J. Del Rey, J.C. Cigudosa, M. Bernues, C. Caldas, D. Colomer, R. Miro, E. Campo, Genomic imbalances and patterns of karyotypic variability in mantle-cell lymphoma cell lines. Leuk. Res. 30, 923–934 (2006)",{"doi":705},"10.1016\u002Fj.leukres.2005.11.013",{"id":20,"text":707,"url":20,"identifiers":708},"S.W. Tait, D.R. Green, Mitochondria and cell death: outer membrane permeabilization and beyond. Nat. Rev. Mol. Cell Biol. 11, 621–632 (2010)",{"doi":709},"10.1038\u002Fnrm2952",{"id":20,"text":711,"url":20,"identifiers":712},"T. Miyashita, J.C. Reed, Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 80, 293–299 (1995)",{"doi":713},"10.1016\u002F0092-8674(95)90412-3",{"id":20,"text":715,"url":20,"identifiers":716},"F. Zhou, J. Hu, H. Ma, M.L. Harrison, R.L. Geahlen, Nucleocytoplasmic trafficking of the Syk protein tyrosine kinase. Mol. Cell. Biol. 26, 3478–3491 (2006)",{"doi":717},"10.1128\u002FMCB.26.9.3478-3491.2006",{"id":20,"text":719,"url":20,"identifiers":720},"L. Wang, L. Duke, P.S. Zhang, R.B. Arlinghaus, W.F. Symmans, A. Sahin, R. Mendez, J.L. Dai, Alternative splicing disrupts a nuclear localization signal in spleen tyrosine kinase that is required for invasion suppression in breast cancer. Cancer Res. 63, 4724–4730 (2003)",{},{"id":20,"text":722,"url":20,"identifiers":723},"L. Bordin, C. Fiore, M. Bragadin, A.M. Brunati, G. Clari, Regulation of membrane band 3 Tyr-phosphorylation by proteolysis of p72(Syk) and possible involvement in senescence process. Acta. Biochim. Biophys. Sin. (Shanghai) 41, 846–851 (2009)",{"doi":724},"10.1093\u002Fabbs\u002Fgmp071",{"id":20,"text":726,"url":20,"identifiers":727},"A. Zamo, G. Ott, T. Katzenberger, P. Adam, C. Parolini, A. Scarpa, M. Lestani, F. Menestrina, M. Chilosi, Establishment of the MAVER-1 cell line, a model for leukemic and aggressive mantle cell lymphoma. Haematologica 91, 40–47 (2006)",{},{"id":20,"text":729,"url":20,"identifiers":730},"G. Dennis Jr., B.T. Sherman, D.A. Hosack, J. Yang, W. Gao, H.C. Lane, R.A. Lempicki, DAVID: Database for Annotation, Visualization, and Integrated Discovery. Genome Biol. 4, P3 (2003)",{"doi":731},"10.1186\u002Fgb-2003-4-5-p3",false,{"id":734,"createTime":735,"updateTime":736,"relativeEntities":737,"slug":738,"properties":739,"entityType":189,"verifyStatus":190,"verifyTime":748,"verifyNote":191,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":749,"fullTextUrl":20,"authors":750,"publicationType":425,"publisherRelationship":844,"citationCount":21,"citationInfo":904,"publishDate":907,"publishYear":905,"citationAnalyzeStatus":19,"lastCitationAnalyze":908,"indexDatabases":909,"openAccess":20,"references":910,"isForceReanalyzing":732},"7139b71a-d3b8-46cf-8077-98367cd990c6","2023-11-28T08:55:45.891+00:00","2026-07-13T05:44:40.198+00:00",[],"The-dual-role-of-tumor-necrosis-factor-alpha-TNF-%CE%B1-in-breast-cancer-molecular-insights-and-therapeutic-approaches",{"abstract":740,"title":742,"gsPaper":744,"doi":746},{"EN":741},"Breast cancer is the most prevalent cancer among women worldwide and the fifth cause of death among all cancer patients. Breast cancer development is driven by genetic and epigenetic alterations, with the tumor microenvironment (TME) playing an essential role in disease progression and evolution through mechanisms like inflammation promotion. TNF-α is one of the essential pro-inflammatory cytokines found in the TME of breast cancer patients, being secreted both by stromal cells, mainly by tumor-associated macrophages, and by the cancer cells themselves. In this review, we explore the biological and clinical impact of TNF-α in all stages of breast cancer development. First of all, we explore the correlation between TNF-α expression levels at the tumor site or in plasma\u002Fserum of breast cancer patients and their respective clinical status and outcome. Secondly, we emphasize the role of TNF-α signaling in both estrogen-positive and -negative breast cancer cells. Thirdly, we underline TNF-α involvement in epithelial-to-mesenchymal transition (EMT) and metastasis of breast cancer cells, and we point out the contribution of TNF-α to the development of acquired drug resistance. Collectively, these data reveal a pro-tumorigenic role of TNF-α during breast cancer progression and metastasis. We systemize the knowledge regarding TNF-α-related therapies in breast cancer, and we explain how TNF-α may act as both a target and a drug in different breast cancer therapeutic approaches. By corroborating the known molecular effects of TNF-α signaling in breast cancer cells with the results from several preclinical and clinical trials, including TNF-α-related clinical observations, we conclude that the potential of TNF-α in breast cancer therapy promises to be of great interest.",{"EN":743},"The dual role of tumor necrosis factor-alpha (TNF-α) in breast cancer: molecular insights and therapeutic 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Bray, J. Ferlay, I. Soerjomataram, R.L. Siegel, L.A. Torre, A. Jemal, Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin (2018). https:\u002F\u002Fdoi.org\u002F10.3322\u002Fcaac.21492","https:\u002F\u002Facsjournals.onlinelibrary.wiley.com\u002Fdoi\u002F10.3322\u002Fcaac.21492",{"doi":916},"10.3322\u002Fcaac.21492",{"id":918,"text":919,"url":920,"identifiers":921},"4c68646b-0035-4279-8000-0006b275d4fa","K.D. Voduc, M.C. Cheang, S. Tyldesley, K. Gelmon, T.O. Nielsen, H. Kennecke, Breast cancer subtypes and the risk of local and regional relapse. J Clin Oncol. 28, 1684–1691 (2010)","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":922},"10.1007\u002Fs10440-022-00541-7",{"id":918,"text":924,"url":920,"identifiers":925},"M.D. Althuis, J.M. Dozier, W.F. Anderson, S.S. Devesa, L.A. Brinton, Global trends in breast cancer incidence and mortality 1973-1997. Int J Epidemiol 34, 405–412 (2005)",{"doi":922},{"id":918,"text":927,"url":920,"identifiers":928},"D. Hanahan, L.M. Coussens, Accessories to the crime: Functions of cells recruited to the tumor microenvironment. Cancer Cell 21, 309–322 (2012)",{"doi":922},{"id":918,"text":930,"url":920,"identifiers":931},"Y.A. Fouad, C. Aanei, Revisiting the hallmarks of cancer. Am J Cancer Res 7, 1016–1036 (2017)",{"doi":922},{"id":933,"text":934,"url":935,"identifiers":936},"e0f37236-92e9-4946-8ad6-b2efffa8d25c","N. Eiro, L. Gonzalez, A. Martinez-Ordonez, B. Fernandez-Garcia, L.O. Gonzalez, S. Cid, F. Dominguez, R. Perez-Fernandez, F.J. Vizoso, Cancer-associated fibroblasts affect breast cancer cell gene expression, invasion and angiogenesis. Cell Oncol 41, 369–378 (2018)","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs13402-018-0371-y",{"doi":937},"10.1007\u002Fs13402-018-0371-y",{"id":939,"text":940,"url":941,"identifiers":942},"34f63ac5-63b6-4d1a-b39b-edda6a369a59","P. Nilendu, S.C. 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Clin Cancer Res 10, 6528–6534 (2004)",{"doi":922},{"id":1389,"createTime":1390,"updateTime":1391,"relativeEntities":1392,"slug":1393,"properties":1394,"entityType":189,"verifyStatus":190,"verifyTime":1403,"verifyNote":191,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1404,"fullTextUrl":20,"authors":1405,"publicationType":425,"publisherRelationship":1506,"citationCount":21,"citationInfo":1566,"publishDate":1569,"publishYear":1567,"citationAnalyzeStatus":19,"lastCitationAnalyze":1570,"indexDatabases":1571,"openAccess":20,"references":1572,"isForceReanalyzing":732},"f8d47a33-0e20-437e-807f-23e0eba64be3","2023-12-02T06:09:49.682+00:00","2026-06-18T01:04:06.084+00:00",[],"Epigenetic-markers-in-basal-cell-carcinoma-universal-themes-in-oncogenesis-and-tumor-stratification-a-short-report",{"abstract":1395,"title":1397,"gsPaper":1399,"doi":1401},{"EN":1396},"Advanced basal cell carcinomas (BCCs) suffer from a scarcity of effective treatment options. Previously, we found that the targetable histone methyltransferase EZH2 was upregulated in aggressive BCC subtypes, suggesting that epigenetics may play a role in BCC progression. The purpose of this study was to determine whether EZH2-associated proteins and marks may be employed for the stratification of BCC histologic subtypes. Sixty-two specimens (from 61 patients), representing more or less aggressive BCC histologic subtypes and matching non-malignant epidermal cells, were included in this study. Immunohistochemistry of H3K27me3, 5hmC, NSD2, MOF and JARID1B was performed to assess their putative associations with BCC histologic subtypes, as well as with EZH2 and Ki67 expression levels. We found that H3K27me3 and 5hmC upregulation was positively correlated with the occurrence of a less aggressive BCC histology. The modifications were also positively correlated with each other. Interestingly, we found that they were negatively correlated with the expression of EZH2, a marker for an aggressive BCC histology. The levels of NSD2, MOF, H3K27me3 and 5hmC were found to be universally upregulated in BCCs versus non-malignant epidermal cells. Our data reveal an EZH2-associated epigenetic marker profile that correlates with histologic signs of BCC aggressiveness. Our findings may have diagnostic and therapeutic implications, and indicate that epigenetic markers may be shared even with relatively less aggressive tumor types, thereby suggesting universal themes.",{"EN":1398},"Epigenetic markers in basal cell carcinoma: universal themes in oncogenesis and tumor stratification? - a short report",{"VOID":1400},"[\"141731335804767635\"]",{"VOID":1402},"10.1007\u002Fs13402-018-0402-8","2024-05-03T22:12:17.924+00:00","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs13402-018-0402-8",[1406,1447,1470,1485],{"id":1407,"sortIndex":21,"researcher":20,"roles":1408,"affiliations":1409,"properties":1442,"displayName":1444,"givenName":20,"familyName":20},"73fa5813-f9b1-4901-a743-3adc20e39582",[754],[1410,1418,1426,1434],{"id":1411,"sortIndex":21,"affiliation":1412,"properties":20},"3bff5d34-a7cf-45bd-afbb-440f71e05d89",{"id":1411,"createTime":20,"updateTime":20,"relativeEntities":1413,"slug":20,"properties":1414,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1417,"statistic":20},[],{"title":1415},{"VI":1416},"Department of Ophthalmology and Visual Sciences, W. 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Kellogg Eye Center, University of Michigan, Ann Arbor, USA",[],{"id":1419,"sortIndex":219,"affiliation":1420,"properties":20},"0a02b1a3-eaf3-4be4-8581-fae9d0dad9c8",{"id":1419,"createTime":20,"updateTime":20,"relativeEntities":1421,"slug":20,"properties":1422,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1425,"statistic":20},[],{"title":1423},{"VI":1424},"Department of Pathology, University of Michigan, Ann Arbor, USA",[],{"id":1427,"sortIndex":237,"affiliation":1428,"properties":20},"5c677f17-20a1-468e-99e1-e4cc24ca139c",{"id":1427,"createTime":20,"updateTime":20,"relativeEntities":1429,"slug":20,"properties":1430,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1433,"statistic":20},[],{"title":1431},{"VI":1432},"Comprehensive Cancer Center, University of Michigan, Ann Arbor, USA",[],{"id":1435,"sortIndex":253,"affiliation":1436,"properties":20},"87f6d432-3c31-49f0-8562-ae2b3e8db1de",{"id":1435,"createTime":20,"updateTime":20,"relativeEntities":1437,"slug":20,"properties":1438,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1441,"statistic":20},[],{"title":1439},{"VI":1440},"Section of Ophthalmology, Surgery Service, VA Ann Arbor Health System, Ann Arbor, USA",[],{"title":1443,"gsAuthor":1445},{"VI":1444},"Rajesh C. 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Chan",{"VOID":1469},"[\"PvN1GZsAAAAJ\"]",{"id":1471,"sortIndex":237,"researcher":20,"roles":1472,"affiliations":1473,"properties":1480,"displayName":1482,"givenName":20,"familyName":20},"0fe73a99-c4c7-4851-9801-b693fae6faa8",[754],[1474],{"id":1411,"sortIndex":21,"affiliation":1475,"properties":20},{"id":1411,"createTime":20,"updateTime":20,"relativeEntities":1476,"slug":20,"properties":1477,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1479,"statistic":20},[],{"title":1478},{"VI":1416},[],{"title":1481,"gsAuthor":1483},{"VI":1482},"Chris A. 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Saal, S.P. Ethier, P.O. Bendahl, O. Stal, P. Malmstrom, M. Ferno, L. Ryden, C. Hegardt, A. Borg and M. Ringner, Global H3K27 trimethylation and EZH2 abundance in breast tumor subtypes. Mol Oncol. 6, 494-506 (2012). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.molonc.2012.06.002","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1574789112000579",{"doi":1593},"10.1016\u002Fj.molonc.2012.06.002",{"id":1595,"text":1596,"url":1597,"identifiers":1598},"0bd07b6d-da0d-4c0a-bc41-fb326543d980","R. Margueron, G. Li, K. Sarma, A. Blais, J. Zavadil, C.L. Woodcock, B.D. Dynlacht, D. Reinberg, Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol. Cell 32, 503–518 (2008). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.molcel.2008.11.004","https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS1097276508007703",{"doi":1599},"10.1016\u002Fj.molcel.2008.11.004",{"id":20,"text":1601,"url":1602,"identifiers":1603},"Y. Xiang, Z. Zhu, G. Han, X. Ye, B. Xu, Z. Peng, Y. Ma, Y. Yu, H. Lin, A.P. Chen and C.D. Chen, JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer. Proc. Natl. Acad. Sci. U. S. A. 104, 19226-19231 (2007). https:\u002F\u002Fdoi.org\u002F10.1073\u002Fpnas.0700735104","https:\u002F\u002Fdoi.org\u002F10.1073\u002Fpnas.0700735104",{"mag":1604,"pmc":1605,"openalex":1606,"pm":1607,"doi":1608},"2090805227","2148272","W2090805227","18048344","10.1073\u002Fpnas.0700735104",{"id":1610,"text":1611,"url":1612,"identifiers":1613},"b73cc3c5-350b-4c6e-802c-3f9addfcdc78","M.S. Banck, S. Li, H. Nishio, C. Wang, A.S. Beutler, M.J. Walsh, The ZNF217 oncogene is a candidate organizer of repressive histone modifiers. Epigenetics 4, 100–106 (2009)","http:\u002F\u002Fwww.tandfonline.com\u002Fdoi\u002Fabs\u002F10.4161\u002Fepi.4.2.7953",{"doi":1614},"10.4161\u002Fepi.4.2.7953",{"id":1616,"text":1617,"url":1618,"identifiers":1619},"2aeffa27-a292-4e28-b85f-5b1805bb94eb","I.A. Asangani, B. Ateeq, Q. Cao, L. Dodson, M. Pandhi, L.P. Kunju, R. Mehra, R.J. Lonigro, J. Siddiqui, N. Palanisamy, Y.M. Wu, X. Cao, J.H. Kim, M. Zhao, Z.S. Qin, M.K. Iyer, C.A. Maher, C. Kumar-Sinha, S. Varambally, A.M. Chinnaiyan, Characterization of the EZH2-MMSET histone methyltransferase regulatory axis in cancer. Mol. Cell 49, 80–93 (2013). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.molcel.2012.10.008","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1097276512008611",{"doi":1620},"10.1016\u002Fj.molcel.2012.10.008",{"id":20,"text":1622,"url":1623,"identifiers":1624},"Q. Li, H. Sun, Y. Shu, X. Zou, Y. Zhao, C. Ge, hMOF (human males absent on the first), an oncogenic protein of human oral tongue squamous cell carcinoma, targeting EZH2 (enhancer of zeste homolog 2). 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BMC Cancer, 10.1186\u002Fs12885-016-2108-5 16, 160 (2016)","https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs12885-016-2108-5",{"mag":1645,"pmc":1646,"openalex":1647,"pm":1648,"doi":1649},"2278682036","4768424","W2278682036","26917489","10.1186\u002Fs12885-016-2108-5",{"id":1651,"text":1652,"url":1653,"identifiers":1654},"d33cde40-8608-49ed-966f-5e307918239c","K. Xu, Z.J. Wu, A.C. Groner, H.H. He, C. Cai, R.T. Lis, X. Wu, E.C. Stack, M. Loda, T. Liu, H. Xu, L. Cato, J.E. Thornton, R.I. Gregory, C. Morrissey, R.L. Vessella, R. Montironi, C. Magi-Galluzzi, P.W. Kantoff, S.P. Balk, X.S. Liu, M. Brown, EZH2 oncogenic activity in castration-resistant prostate cancer cells is Polycomb-independent. Science 338, 1465–1469 (2012). https:\u002F\u002Fdoi.org\u002F10.1126\u002Fscience.1227604","https:\u002F\u002Fwww.science.org\u002Fdoi\u002F10.1126\u002Fscience.1227604",{"doi":1655},"10.1126\u002Fscience.1227604",{"id":20,"text":1657,"url":1658,"identifiers":1659},"T. Swigut, J. Wysocka, H3K27 demethylases, at long last. Cell 131, 29–32 (2007). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cell.2007.09.026","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cell.2007.09.026",{"mag":1660,"openalex":1661,"pm":1662,"doi":1663},"1971180847","W1971180847","17923085","10.1016\u002Fj.cell.2007.09.026",{"id":20,"text":1665,"url":1666,"identifiers":1667},"K.H. Kim, C.W. Roberts, Targeting EZH2 in cancer. Nat. Med 22, 128–134 (2016). https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnm.4036","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnm.4036",{"mag":1668,"pmc":1669,"openalex":1670,"pm":1671,"doi":1672},"2264682687","4918227","W2264682687","26845405","10.1038\u002Fnm.4036",{"id":20,"text":1674,"url":1675,"identifiers":1676},"E. di Luccio, Inhibition of nuclear receptor binding SET domain 2\u002Fmultiple myeloma SET domain by LEM-06 implication for epigenetic cancer therapies. J. Cancer Prev. 20, 113–120 (2015). https:\u002F\u002Fdoi.org\u002F10.15430\u002FJCP.2015.20.2.113","https:\u002F\u002Fdoi.org\u002F10.15430\u002Fjcp.2015.20.2.113",{"mag":1677,"pmc":1678,"openalex":1679,"pm":1680,"doi":1681},"2282073262","4492355","W2282073262","26151044","10.15430\u002Fjcp.2015.20.2.113",{"id":1683,"text":1684,"url":1685,"identifiers":1686},"ffd2307f-2705-4890-a7bc-f491e7d60202","A. Tumber, A. Nuzzi, E.S. Hookway, S.B. Hatch, S. Velupillai, C. Johansson, A. Kawamura, P. Savitsky, C. Yapp, A. Szykowska, N. Wu, C. Bountra, C. Strain-Damerell, N.A. Burgess-Brown, G.F. Ruda, O. Fedorov, S. Munro, K.S. England, R.P. Nowak, C.J. Schofield, N.B. La Thangue, C. Pawlyn, F. Davies, G. Morgan, N. Athanasou, S. Muller, U. Oppermann, P.E. Brennan, Potent and selective KDM5 inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells. Cell Chem. Biol. 24, 371–380 (2017). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.chembiol.2017.02.006","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS2451945617300363",{"doi":1687},"10.1016\u002Fj.chembiol.2017.02.006",{"id":1689,"createTime":1690,"updateTime":1691,"relativeEntities":1692,"slug":1693,"properties":1694,"entityType":189,"verifyStatus":190,"verifyTime":1703,"verifyNote":191,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1704,"fullTextUrl":20,"authors":1705,"publicationType":425,"publisherRelationship":1818,"citationCount":21,"citationInfo":1877,"publishDate":1879,"publishYear":489,"citationAnalyzeStatus":19,"lastCitationAnalyze":1880,"indexDatabases":1881,"openAccess":20,"references":1882,"isForceReanalyzing":732},"f82a49d3-e9b6-49fb-8081-4f26b78e8660","2024-01-04T12:22:10.284+00:00","2026-04-28T17:12:49.152+00:00",[],"Pharmacological-inhibition-of-AKT-sensitizes-MCF-7-human-breast-cancer-initiating-cells-to-radiation",{"abstract":1695,"title":1697,"gsPaper":1699,"doi":1701},{"EN":1696},"Caner-initiating cells (CICs or cancer stem cells) have been shown both experimentally and clinically to be resistant to radiation. The mechanism underlying radioresistance remains unclear. In the present study, we screened 51 genes which are potentially important in mediating radioresistance of breast CICs. The expression of AKT1 and AKT2 at protein and mRNA levels was dramatically increased among the screened genes by 8 Gy radiation treatment in MCF-7 mammosphere cells (predominantly CD24–\u002Flow\u002FCD44+ CICs), but not in the bulk population of MCF-7 cells (predominantly CD24+\u002FCD44+). Using apoptosis and clonogenic survival assays, we found pharmacological inhibition of AKT with selective inhibitors of AKT sensitized MCF-7 mammosphere cells, but not MCF-7 monolayer cells to radiation. The present findings suggest that treatment with AKT inhibitors prior to ionizing radiation treatment may be a potential benefit to patients with breast cancer, in particular to eradiate breast CICs.",{"EN":1698},"Pharmacological inhibition of AKT sensitizes MCF-7 human breast cancer-initiating cells to radiation",{"VOID":1700},"[\"14315561981520451834\"]",{"VOID":1702},"10.1007\u002Fs13402-011-0020-1","2024-05-04T07:14:29.114+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13402-011-0020-1",[1706,1721,1736,1751,1766,1779,1792,1805],{"id":1707,"sortIndex":21,"researcher":20,"roles":1708,"affiliations":1709,"properties":1718,"displayName":1720,"givenName":20,"familyName":20},"ca7ec995-d378-4793-af5f-b34518b951d9",[754],[1710],{"id":1711,"sortIndex":21,"affiliation":1712,"properties":20},"4825424c-c24c-4b96-89b2-f5a56b4529fa",{"id":1711,"createTime":20,"updateTime":20,"relativeEntities":1713,"slug":20,"properties":1714,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1717,"statistic":20},[],{"title":1715},{"VI":1716},"Health Management Centre, Guangzhou First Municipal People’s Hospital, Guangzhou Medical College, Guangzhou, China",[],{"title":1719},{"VI":1720},"Jun-Fang Zhan",{"id":1722,"sortIndex":219,"researcher":20,"roles":1723,"affiliations":1724,"properties":1733,"displayName":1735,"givenName":20,"familyName":20},"434aebf4-dbc2-44a6-9721-138c9b79930c",[754],[1725],{"id":1726,"sortIndex":21,"affiliation":1727,"properties":20},"cc6158e5-ebda-4390-9d13-9edba71eb56b",{"id":1726,"createTime":20,"updateTime":20,"relativeEntities":1728,"slug":20,"properties":1729,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1732,"statistic":20},[],{"title":1730},{"VI":1731},"Department of General Surgery, General Hospital of Guangzhou Military Command, Guangzhou, China",[],{"title":1734},{"VI":1735},"Liang-Ping Wu",{"id":1737,"sortIndex":237,"researcher":20,"roles":1738,"affiliations":1739,"properties":1748,"displayName":1750,"givenName":20,"familyName":20},"ae1befbb-02b4-47e4-a56c-fe1c0a4e4b9d",[754],[1740],{"id":1741,"sortIndex":21,"affiliation":1742,"properties":20},"5c7699d4-ca73-45a9-9b9d-12268337450a",{"id":1741,"createTime":20,"updateTime":20,"relativeEntities":1743,"slug":20,"properties":1744,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1747,"statistic":20},[],{"title":1745},{"VI":1746},"Department of Radiation Oncology, Nanfang Hospital, Southern Medical University, Guangzhou, China",[],{"title":1749},{"VI":1750},"Long-Hua 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Jemal, R. Siegel, E. Ward, Y. Hao, J. Xu, M.J. Thun, Cancer Statistics, 2009. CA Cancer J Clin 59, 225–249 (2009)",{},{"id":918,"text":1887,"url":920,"identifiers":1888},"J.K. Jameel, V.S. Rao, L. Cawkwell, P.J. Drew, Radioresistance in carcinoma of the breast. Breast 13, 452–460 (2004)",{"doi":922},{"id":918,"text":1890,"url":920,"identifiers":1891},"M. Zhang, R.L. Atkinson, J.M. Rosen, Selective targeting of radiation-resistant tumor-initiating cells. Proc Natl Acad Sci U S A 107, 3522–3527 (2010)",{"doi":922},{"id":1893,"text":1894,"url":1895,"identifiers":1896},"cfb055db-77d7-4f2c-ab56-881d4ab8cc13","M. Al-Hajj, M.S. Wicha, A. Benito-Hernandez, S.J. Morrison, M.F. Clarke, Prospective identification of tumorigenic breast cancer cells. Proc Natl Acad Sci U S A 100, 3983–3988 (2003)","https:\u002F\u002Fpnas.org\u002Fdoi\u002Ffull\u002F10.1073\u002Fpnas.0530291100",{"doi":1897},"10.1073\u002Fpnas.0530291100",{"id":918,"text":1899,"url":920,"identifiers":1900},"J.M. Rosen, C.T. Jordan, The increasing complexity of the cancer stem cell paradigm. Science 324, 1670–1673 (2009)",{"doi":922},{"id":918,"text":1902,"url":920,"identifiers":1903},"T.M. Phillips, W.H. McBride, F. Pajonk, The response of CD24(−\u002Flow)\u002FCD44+ breast cancer-initiating cells to radiation. J Natl Cancer Inst 98, 1777–1785 (2006)",{"doi":922},{"id":1905,"text":1906,"url":1907,"identifiers":1908},"24299839-b20f-428b-9c36-f71250e676fa","F. Karimi-Busheri, A. Rasouli-Nia, J.R. Mackey, M. Weinfeld, Senescence evasion by MCF-7 human breast tumor-initiating cells. Breast Cancer Res 12, R31 (2010)","http:\u002F\u002Fbreast-cancer-research.biomedcentral.com\u002Farticles\u002F10.1186\u002Fbcr2583",{"doi":1909},"10.1186\u002Fbcr2583",{"id":918,"text":1911,"url":920,"identifiers":1912},"R.L. Dillon, W.J. Muller, Distinct biological roles for the akt family in mammary tumor progression. Cancer Res 70, 4260–4264 (2010)",{"doi":922},{"id":1914,"text":1915,"url":1916,"identifiers":1917},"9dd3344a-e0b7-4790-8f42-8e6540524326","A. Sanchez-Munoz, E. Perez-Ruiz, B. Jimenez, N. Ribelles, A. Marquez, I. Garcia-Rios, E. Alba Conejo, Targeted therapy of metastatic breast cancer. Clin Transl Oncol 11, 643–650 (2009)","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12094-009-0419-6",{"doi":1918},"10.1007\u002Fs12094-009-0419-6",{"id":918,"text":1920,"url":920,"identifiers":1921},"K. Liang, W. Jin, C. Knuefermann, M. Schmidt, G.B. Mills, K.K. Ang, L. Milas, Z. Fan, Targeting the phosphatidylinositol 3-kinase\u002FAkt pathway for enhancing breast cancer cells to radiotherapy. Mol Cancer Ther 2, 353–360 (2003)",{"doi":922},{"id":918,"text":1923,"url":920,"identifiers":1924},"C. Ginestier, S. Liu, M.E. Diebel, H. Korkaya, M. Luo, M. Brown, J. Wicinski, O. Cabaud, E. Charafe-Jauffret, D. Birnbaum, J.L. Guan, G. Dontu, M.S. Wicha, CXCR1 blockade selectively targets human breast cancer stem cells in vitro and in xenografts. J Clin Invest 120, 485–497 (2010)",{"doi":922},{"id":918,"text":1926,"url":920,"identifiers":1927},"D. Ponti, A. Costa, N. Zaffaroni, G. Pratesi, G. Petrangolini, D. Coradini, S. Pilotti, M.A. Pierotti, M.G. Daidone, Isolation and in vitro propagation of tumorigenic breast cancer cells with stem\u002Fprogenitor cell properties. Cancer Res 65, 5506–5511 (2005)",{"doi":922},{"id":918,"text":1929,"url":920,"identifiers":1930},"S.J. Veuger, J.E. Hunter, B.W. Durkacz, Ionizing radiation-induced NF-kappaB activation requires PARP-1 function to confer radioresistance. Oncogene 28, 832–842 (2009)",{"doi":922},{"id":918,"text":1932,"url":920,"identifiers":1933},"B.G. Debeb, W. Xu, W.A. Woodward, Radiation resistance of breast cancer stem cells: understanding the clinical framework. J Mammary Gland Biol Neoplasia 14, 11–17 (2009)",{"doi":922},{"id":918,"text":1935,"url":920,"identifiers":1936},"W.A. Woodward, M.S. Chen, F. Behbod, M.P. Alfaro, T.A. Buchholz, J.M. Rosen, WNT\u002Fbeta-catenin mediates radiation resistance of mouse mammary progenitor cells. Proc Natl Acad Sci U S A 104, 618–623 (2007)",{"doi":922},{"id":918,"text":1938,"url":920,"identifiers":1939},"M.S. Chen, W.A. Woodward, F. Behbod, S. Peddibhotla, M.P. Alfaro, T.A. Buchholz, J.M. Rosen, Wnt\u002Fbeta-catenin mediates radiation resistance of Sca1+ progenitors in an immortalized mammary gland cell line. J Cell Sci 120, 468–477 (2007)",{"doi":922},{"id":918,"text":1941,"url":920,"identifiers":1942},"A.M. Martelli, P.L. Tazzari, G. Tabellini, R. Bortul, A.M. Billi, L. Manzoli, A. Ruggeri, R. Conte, L. Cocco, A new selective AKT pharmacological inhibitor reduces resistance to chemotherapeutic drugs. TRAIL, all-trans-retinoic acid, and ionizing radiation of human leukemia cells. Leukemia 17, 1794–1805 (2003)",{"doi":922},{"id":918,"text":1944,"url":920,"identifiers":1945},"K. Fujiwara, E. Iwado, G.B. Mills, R. Sawaya, S. Kondo, Y. Kondo, Akt inhibitor shows anticancer and radiosensitizing effects in malignant glioma cells by inducing autophagy. Int J Oncol 31, 753–760 (2007)",{"doi":922},{"id":918,"text":1947,"url":920,"identifiers":1948},"H. Korkaya, A. Paulson, E. Charafe-Jauffret, C. Ginestier, M. Brown, J. Dutcher, S.G. Clouthier, M.S. Wicha, Regulation of mammary stem\u002Fprogenitor cells by PTEN\u002FAkt\u002Fbeta-catenin signaling. PLoS Biol 7, e1000121 (2009)",{"doi":922},{"id":1950,"text":1951,"url":1952,"identifiers":1953},"cbdc2876-d249-45b6-b062-9c382350a69b","A.K. Gupta, G.J. Cerniglia, R. Mick, M.S. Ahmed, V.J. Bakanauskas, R.J. Muschel, W.G. McKenna, Radiation sensitization of human cancer cells in vivo by inhibiting the activity of PI3K using LY294002. Int J Radiat Oncol Biol Phys 56, 846–853 (2003)","https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS0360301603002141",{"doi":1954},"10.1016\u002Fs0360-3016(03)00214-1",{"id":918,"text":1956,"url":920,"identifiers":1957},"Z. Jiang, N. Pore, G.J. Cerniglia, R. Mick, M.M. Georgescu, E.J. Bernhard, S.M. Hahn, A.K. Gupta, A. Maity, Phosphatase and tensin homologue deficiency in glioblastoma confers resistance to radiation and temozolomide that is reversed by the protease inhibitor nelfinavir. Cancer Res 67, 4467–4473 (2007)",{"doi":922},{"id":918,"text":1959,"url":920,"identifiers":1960},"L. de la Pena, W.E. Burgan, D.J. Carter, M.G. Hollingshead, M. Satyamitra, K. Camphausen, P.J. Tofilon, Inhibition of Akt by the alkylphospholipid perifosine does not enhance the radiosensitivity of human glioma cells. Mol Cancer Ther 5, 1504–1510 (2006)",{"doi":922},{"id":1962,"text":1963,"url":1964,"identifiers":1965},"571380cd-d767-4959-874e-d532359687c7","H.F. Li, J.S. Kim, T. Waldman, Radiation-induced Akt activation modulates radioresistance in human glioblastoma cells. Radiat Oncol 4, 43 (2009)","https:\u002F\u002Fro-journal.biomedcentral.com\u002Farticles\u002F10.1186\u002F1748-717X-4-43",{"doi":1966},"10.1186\u002F1748-717X-4-43",{"id":1968,"createTime":1969,"updateTime":1970,"relativeEntities":1971,"slug":1972,"properties":1973,"entityType":189,"verifyStatus":190,"verifyTime":1984,"verifyNote":191,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1985,"fullTextUrl":20,"authors":1986,"publicationType":425,"publisherRelationship":2056,"citationCount":20,"citationInfo":20,"publishDate":2115,"publishYear":1567,"citationAnalyzeStatus":19,"lastCitationAnalyze":2116,"indexDatabases":2117,"openAccess":20,"references":20,"isForceReanalyzing":732},"af2e7ca1-249f-4dcf-80eb-ef6359f93cb4","2024-02-10T16:18:39.385+00:00","2026-03-26T21:16:13.476+00:00",[],"The-emerging-role-of-lncRNAs-in-the-regulation-of-cancer-stem-cells",{"abstract":1974,"title":1976,"gsPaper":1978,"references":1980,"doi":1982},{"EN":1975},"Tumors contain a functional subpopulation of cells that exhibit stem cell properties. These cells, named cancer stem cells (CSCs), play significant roles in the initiation and progression of cancer. Long non-coding RNAs (lncRNAs) can act at the transcriptional, posttranscriptional and translational level. As such, they may be involved in various biological processes such as DNA damage repair, inflammation, metabolism, cell survival, cell signaling, cell growth and differentiation. Accumulating evidence indicates that lncRNAs are key regulators of the CSC subpopulation, thereby contributing to cancer progression. The aim of this review is to overview current knowledge about the functional role and the mechanisms of action of lncRNAs in the initiation, maintenance and regulation of CSCs derived from different neoplasms. These lncRNAs include CTCF7, ROR, DILC, HOTAIR, H19, HOTTIP, ATB, HIF2PUT, SOX2OT, MALAT-1, CUDR, Lnc34a, Linc00617, DYNC2H1–4, PVT1, SOX4 and ARSR Uc.283-plus. Furthermore, we will illustrate how lncRNAs may regulate asymmetric CSC division and contribute to self-renewal, drug resistance and EMT, thus affecting the metastasis and recurrence of different cancers. In addition, we will highlight the implications of targeting lncRNAs to improve the efficacy of conventional drug therapies and to hamper CSC survival and proliferation. lncRNAs are valuable tools in the search for new targets to selectively eliminate CSCs and improve clinical outcomes. LncRNAs may serve as excellent therapeutic targets because they are stable, easily detectable and expressed in tissue-specific contexts.",{"EN":1977},"The emerging role of lncRNAs in the regulation of cancer stem cells",{"VOID":1979},"[\"13749814914276793293\"]",{"VOID":1981},"S. Djebali, C.A. Davis, A. Merkel, A. Dobin, T. Lassmann, A. Mortazavi, A. Tanzer, J. Lagarde, W. Lin, F. Schlesinger, C. Xue, G.K. Marinov, J. Khatun, B.A. Williams, C. Zaleski, J. Rozowsky, M. Roder, F. Kokocinski, R.F. 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Cell Rep e212, 297–312 (2018)",{"VOID":1983},"10.1007\u002Fs13402-018-0406-4","2024-05-16T07:05:27.707+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13402-018-0406-4",[1987,2002,2019,2034],{"id":1988,"sortIndex":21,"researcher":20,"roles":1989,"affiliations":1990,"properties":1999,"displayName":2001,"givenName":20,"familyName":20},"b4de053d-2df8-434e-bc60-d8545b21242c",[754],[1991],{"id":1992,"sortIndex":21,"affiliation":1993,"properties":20},"e453b436-e5dc-49a0-b248-1ca0f25806fb",{"id":1992,"createTime":20,"updateTime":20,"relativeEntities":1994,"slug":20,"properties":1995,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1998,"statistic":20},[],{"title":1996},{"VI":1997},"Epigenetics, Instituto Nacional de Medicina Genomica, Mexico City, Mexico",[],{"title":2000},{"VI":2001},"Rosario 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drug uptake has not been well studied, compared to the deeper understanding of drug resistance mediated by the cellular efflux system such as MDR1 proteins. It has been suggested that many drugs need active or defined transporters to pass the cell membrane. In contrast to efflux components induced after anti-cancer drugs reach the intracellular compartment, drug importers are required for initial drug responses. Furthermore, tissue-specific uptake of anti-cancer drugs may directly impact the side effects of many drugs when they accumulate in healthy tissues. Therefore, linking anti-cancer drugs to their respective drug import transporters would directly help to predict drug responses, whilst minimizing side effects. To identify drug transporters of the commonly used anti-cancer drug doxorubicin, we performed focused CRISPR activation and knockout genetic screens targeting all potential membrane-associated transporters and proteins. We monitored the direct uptake of doxorubicin by fluorescence-activated cell sorting (FACS) as the screening readout for identifying transporters\u002Fproteins directly involved in doxorubicin uptake. Integrating the data from these comprehensive CRISPR screenings, we confirmed previously indicated doxorubicin exporters such as ABCB1 and ABCG2 genes, and identified novel doxorubicin importer gene SLC2A3 (GLUT3). Upregulation of SLC2A3 led to higher doxorubicin uptake and better cell killing, indicating SLC2A3 could be a new marker to predict doxorubicin drug response and minimize side effects for the personalized application of this conventional chemotherapeutic drug. Our study provides a comprehensive way for identifying drug transporters, as exemplified by the commonly used anti-cancer drug doxorubicin. The newly identified importers may have direct clinical implications for the personalized application of doxorubicin in treating distinct tumors. Our results also highlight the necessity of combining both CRISPR knockout and CRISPR activation genetic screens to identify drug transporters.",{"EN":2128},"Targeted CRISPR activation and knockout screenings identify novel doxorubicin transporters",{"VOID":2130},"[]",{"VOID":2132},"P. Cohen, D. Cross, P.A. Jänne, Kinase drug discovery 20 years after imatinib: progress and future directions. Nat. Rev. Drug Discovery. 20(7), 551–569 (2021)\nR.H. Wijdeven et al., Old drugs, novel ways out: Drug resistance toward cytotoxic chemotherapeutics. Drug Resistance Updates 28(Supplement C), 65?81 (2016)\nP. Borst et al., The multidrug resistance protein family. Biochim. et Biophys. Acta (BBA) - Biomembr. 1461(2), 347–357 (1999)\nA. Prahallad et al., Unresponsiveness of colon cancer to BRAF(V600E) inhibition through feedback activation of EGFR. Nature 483. 100–103 (2012)\nC. Sun et al., Reversible and adaptive resistance to BRAF(V600E) inhibition in melanoma. Nature 508(7494), 118–122 (2014)\nK. 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Thompson, Glucose transporter 3 (GLUT3) protein is present in human myocardium. Biochim. Biophys. 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Xiao",{"VOID":2561},"A5041816259",{"id":2563,"sortIndex":133,"researcher":20,"roles":2564,"affiliations":2565,"properties":2574,"displayName":2578,"givenName":20,"familyName":20},"f01856b2-4d46-4371-befe-851fa207591a",[],[2566],{"id":2567,"sortIndex":21,"affiliation":2568,"properties":20},"6b55bdb5-a6d0-4463-a758-d0f1a26f4b90",{"id":2567,"createTime":20,"updateTime":20,"relativeEntities":2569,"slug":20,"properties":2570,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2573,"statistic":20},[],{"title":2571},{"EN":2572},"Department of General Surgery, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, 200025, Shanghai, China",[],{"orcid":2575,"title":2577,"openalex":2579},{"VOID":2576},"https:\u002F\u002Forcid.org\u002F0000-0003-3534-9205",{"EN":2578},"Jing Sun",{"VOID":2580},"A5060972491",{"id":2582,"sortIndex":2583,"researcher":20,"roles":2584,"affiliations":2585,"properties":2594,"displayName":2598,"givenName":20,"familyName":20},"b73ba3e7-9627-4254-929d-d10a209898be",17,[],[2586],{"id":2587,"sortIndex":21,"affiliation":2588,"properties":20},"e39a9bfc-5fbe-4b59-85c5-98905ef7f687",{"id":2587,"createTime":20,"updateTime":20,"relativeEntities":2589,"slug":20,"properties":2590,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2593,"statistic":20},[],{"title":2591},{"EN":2592},"Department of Oncology, the Sixth People’s Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, PRC, China",[],{"orcid":2595,"title":2597,"openalex":2599},{"VOID":2596},"https:\u002F\u002Forcid.org\u002F0000-0001-6442-3975",{"EN":2598},"Aina He",{"VOID":2600},"A5056438877",{"id":2602,"sortIndex":2603,"researcher":20,"roles":2604,"affiliations":2605,"properties":2612,"displayName":2616,"givenName":20,"familyName":20},"ac444fbe-46d9-41b3-81c9-e52214f73b23",18,[],[2606],{"id":2292,"sortIndex":21,"affiliation":2607,"properties":20},{"id":2292,"createTime":20,"updateTime":20,"relativeEntities":2608,"slug":20,"properties":2609,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2611,"statistic":20},[],{"title":2610},{"EN":2297},[],{"orcid":2613,"title":2615,"openalex":2617},{"VOID":2614},"https:\u002F\u002Forcid.org\u002F0000-0002-5270-5921",{"EN":2616},"Zhi Li",{"VOID":2618},"A5090560783",{"url":20,"publisher":2620,"properties":20},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":2621,"slug":10,"properties":2622,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":2626,"manageAffiliations":2643,"indexDatabases":2654,"url":20,"thumbnailPath":20,"statistic":2669,"gsStatistic":20,"type":20,"analyzePriority":20},[],{"issn":2623,"title":2624,"eissn":2625},{"VOID":13},{"EN":15},{"VOID":17},[2627,2631,2635,2639],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":2628,"label":2629,"description":2630,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":2632,"label":2633,"description":2634,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":2636,"label":2637,"description":2638,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":2640,"label":2641,"description":2642,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[2644,2649],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":2645,"slug":20,"properties":2646,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2648,"statistic":20},[],{"title":2647},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":2650,"slug":20,"properties":2651,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2653,"statistic":20},[],{"title":2652},{"EN":61},[],[2655,2662],{"id":65,"indexDatabase":2656,"url":78,"indexYears":20,"academicFieldIds":2661,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":2657,"label":2658,"description":2659,"key":74,"publicationTags":2660,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[80,81,82],{"id":84,"indexDatabase":2663,"url":95,"indexYears":96,"academicFieldIds":2668,"indexDatabaseRanking":102},{"id":86,"createTime":20,"updateTime":20,"relativeEntities":2664,"label":2665,"description":2666,"key":92,"publicationTags":2667,"standard":20},[],{"EN":89,"VI":89},{"EN":89,"VI":91},[94],[98,99,100,101],{"impactFactor":21,"impactFactorByYear":2670,"i10Index":117,"i10IndexLast5Year":118,"totalPublication":119,"totalPublicationByYear":2671,"totalCitation":134,"totalCitationByYear":2672,"totalCitationPerPublication":149,"totalCitationPerPublicationByYear":2673,"hindexLast5Year":118,"hindex":118},{"2012":105,"2013":106,"2014":107,"2015":108,"2016":109,"2017":110,"2018":111,"2019":112,"2020":113,"2021":114,"2022":115,"2023":116},{"2011":121,"2012":122,"2013":118,"2014":123,"2015":124,"2016":125,"2017":126,"2018":127,"2019":128,"2020":129,"2021":130,"2022":131,"2023":132,"2024":133},{"2011":136,"2012":137,"2013":138,"2014":139,"2015":140,"2016":141,"2017":142,"2018":143,"2019":144,"2020":145,"2021":146,"2022":147,"2023":148},{"2011":151,"2012":152,"2013":153,"2014":154,"2015":155,"2016":156,"2017":157,"2018":158,"2019":159,"2020":160,"2021":161,"2022":162,"2023":163},{"total":237,"publishYear":2675,"statisticByYear":2676},2022,{"2023":237},"2022-12-01","2024-04-15T03:19:00.222+00:00",[76,102],[],{"id":2682,"createTime":2683,"updateTime":2684,"relativeEntities":2685,"slug":2686,"properties":2687,"entityType":189,"verifyStatus":190,"verifyTime":2684,"verifyNote":191,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":2696,"fullTextUrl":20,"authors":2697,"publicationType":425,"publisherRelationship":2811,"citationCount":20,"citationInfo":20,"publishDate":2870,"publishYear":905,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":2871,"openAccess":20,"references":20,"isForceReanalyzing":732},"7c54c95d-915e-4c8c-b53a-c120016e8f8a","2023-12-18T18:41:00.686+00:00","2025-02-26T22:39:53.235+00:00",[],"The-PI3K-mTOR-dual-inhibitor-GSK458-potently-impedes-ovarian-cancer-tumorigenesis-and-metastasis",{"abstract":2688,"title":2690,"references":2692,"doi":2694},{"EN":2689},"The PI3K\u002FAKT\u002FmTOR pathway is one of the most highly activated cellular signaling pathways in advanced ovarian cancer. Although several PI3K\u002FAKT\u002FmTOR inhibitors have been developed to treat various types of cancer, the antitumor efficacy of many of these compounds against ovarian cancer has remained unclear. Here, we tested and compared a panel of 16 PI3K\u002FAKT\u002FmTOR inhibitors (XL765, Miltefosine, Rapamycin, CCI-779, RAD001, FK506, XL147, GSK2110183, IPI-145, GSK2141795, BYL719, GSK458, CAL-101, XL765 analogue SAR245409, Triciribine, and GDC0941) that have entered clinical trials for antitumor activity against ovarian cancer, as well as the front line drug, paclitaxel. Antitumor efficacy was measured in both ovarian cancer cell lines and patient-derived ovarian primary tumor cell lines in vitro and in vivo. We identified the PI3K\u002FmTOR dual inhibitor GSK458 as a potent inhibitor of proliferation in all cell lines tested at half maximal inhibitory concentrations (IC50) of approximately 0.01-1 µM, a range tens to hundreds fold lower than that of the other PI3K\u002FAKT\u002FmTOR inhibitors tested. Additionally, GSK458 showed the highest inhibitory efficacy against ovarian cancer cell migration. GSK458 also inhibited tumor growth and metastasis in nude mice intraperitoneally engrafted with SKOV3 cells or a patient-derived tumor cell xenograft (PDCX). Importantly, the inhibitory efficiency of GSK458 on cell proliferation and migration both in vitro and in vivo was comparable to that of paclitaxel. Mechanistically, the anti-tumor activity of GSK458 was found to be associated with inactivation of AKT and mTOR, and induction of cell cycle arrest at the G0\u002FG1 phase. Based on our results, we conclude that GSK458 may serve as an attractive candidate to treat ovarian cancer.",{"EN":2691},"The PI3K\u002FmTOR dual inhibitor GSK458 potently impedes ovarian cancer tumorigenesis and metastasis",{"VOID":2693},"F. Bray, J. Ferlay, I. Soerjomataram, R.L. Siegel, L.A. Torre, A. Jemal, Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J. Clin. 68, 394–424 (2018)\nR.L. Siegel, K.D. Miller, A. Jemal, Cancer statistics, 2018. CA Cancer J. Clin. 68, 7–30 (2018)\nL.A. Torre, F. Bray, R.L. Siegel, J. Ferlay, J. Lortet-Tieulent, A. Jemal, Global cancer statistics, 2012. CA Cancer J. Clin. 65, 87–108 (2015)\nX. Li, M. Tang, Q. Zhu, X. Wang, Y. Lin, X. Wang, The exosomal integrin alpha5beta1\u002FAEP complex derived from epithelial ovarian cancer cells promotes peritoneal metastasis through regulating mesothelial cell proliferation and migration. Cell. Oncol. 43, 263–277 (2020)\nS. 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Ferretti, MiRNAs and their interplay with PI3K\u002FAKT\u002FmTOR pathway in ovarian cancer cells: a potential role in platinum resistance. J. Cancer Res. Clin. Oncol. 144, 2313–2318 (2018)",{"VOID":2695},"10.1007\u002Fs13402-020-00514-8","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13402-020-00514-8",[2698,2742,2755,2770,2785,2798],{"id":2699,"sortIndex":21,"researcher":20,"roles":2700,"affiliations":2701,"properties":2739,"displayName":2741,"givenName":20,"familyName":20},"69a0c3b9-8f1d-4882-abb2-f6bcd6ce4753",[754],[2702,2710,2719,2730],{"id":2703,"sortIndex":21,"affiliation":2704,"properties":20},"486d0e8e-19f3-41c9-9369-227d71f0969d",{"id":2703,"createTime":20,"updateTime":20,"relativeEntities":2705,"slug":20,"properties":2706,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2709,"statistic":20},[],{"title":2707},{"VI":2708},"Department of Obstetrics and Gynecology, Shanghai Fengxian District Central Hospital, Southern Medical University, Shanghai, 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thyroid cancer (PTC) is more common in women than in men. It has been suggested that estrogen may be involved in its development, as has previously been shown for breast, endometrial and ovarian cancer. The purpose of this study was to assess correlations between the expression of the estrogen receptor alpha36 (ERα36) and the glucose regulated proteins GRP78 and GRP94 (chaperones involved in glycoprotein folding) and various PTC clinicopathological features, as well as to evaluate the potential usefulness of these three potential oncogenic proteins in the prediction of aggressive PTC behavior. ERα36, GRP78 and GRP94 protein expression in 218 primary PTC tissues and PTC-derived BCPAP cells was examined using immunohistochemistry, Western blotting and immunocytochemistry. The proliferative, invasive and migrative capacities of BCPAP cells in which the respective genes were either exogenously over-expressed or silenced were assessed using BrdU incorporation and Transwell assays, respectively. We found that ERα36, GRP78 and GRP94 protein expression was upregulated in the primary PTC tissues tested. We also found that ERα36, GRP78 and GRP94 expression modulation affected the proliferation, invasion and migration of PTC-derived BCPAP cells. A positive correlation and a positive feedback loop were noted between ERα36, GRP78 and GRP94 protein expression in the primary PTC tissues and in BCPAP cells, respectively. High ERα36 expression in combination with a high GRP78\u002F GRP94 expression was found to have a stronger correlation with extrathyroid extension (ETE), lymph node metastasis (LNM), distant metastasis (DM) and high TNM stage than high ERα36 expression in combination with either high GRP78 or high GRP94 expression (p = 0.028 for ETE, p = 0.002 for DM and p ≤ 0.001 for LNM and high TNM stage) or high ERα36 expression alone (p \u003C 0.001 for ETE, LNM, DM and high TNM stage). From our data we conclude that a concomitant high expression of ERα36, GRP78 and GRP94 is strongly associated with aggressive PTC behavior and may be used as a predictor for ETE, LNM, DM and high TNM stage.",{"EN":2882},"Concomitant high expression of ERα36, GRP78 and GRP94 is associated with aggressive papillary thyroid cancer behavior",{"VOID":2884},"H. Li, J. Li, Thyroid disorders in women. Minerva Med. 106, 109–114 (2015)\nS. Hima, S. Sreeja, Modulatory role of 17β-estradiol in the tumor microenvironment of thyroid cancer. IUBMB Life 68, 85–96 (2016). https:\u002F\u002Fdoi.org\u002F10.1002\u002Fiub.1462\nE. Przybylik-Mazurek, A. Hubalewska-Dydejczyk, A. Fedorowicz, D. Pach, Factors connected with the female sex seem to play an important role in differentiated thyroid cancer. Gynecol. Endocrinol. 28, 150–155 (2012). https:\u002F\u002Fdoi.org\u002F10.3109\u002F09513590.2011.563909\nS. Caini, B. Gibelli, D. Palli, C. Saieva, M. Ruscica, S. Gandini, Menstrual and reproductive history and use of exogenous sex hormones and risk of thyroid cancer among women: A meta-analysis of prospective studies. Cancer Causes Control 26, 511–518 (2015). https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10552-015-0546-z\nM.C. Pike, C.L. Pearce, A.H. Wu, Prevention of cancers of the breast, endometrium and ovary. Oncogene 23, 6379–6391 (2004). https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsj.onc.1207899\nC. Busonero, S. Leone, F. Acconcia, Emetine induces estrogen receptor alpha degradation and prevents 17β-estradiol-induced breast cancer cell proliferation. Cell. Oncol. 40, 299–301 (2017). https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs13402-017-0322-z\nZ. Wang, X. Zhang, P. Shen, B.W. Loggie, Y. Chang, T.F. Deuel, Identification, cloning, and expression of human estrogen receptor-alpha36, a novel variant of human estrogen receptor-alpha66. Biochem. Biophys. Res. Commun. 336, 1023–1027 (2005). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bbrc.2005.08.226\nZ.Y. Wang, L. Yin, Estrogen receptor alpha-36 (ER-α36): A new player in human breast cancer. Mol. Cell. Endocrinol. 418, 193–206 (2015). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.mce.2015.04.017\nS.L. Lin, L.Y. Yan, X.W. Liang, Z.B. Wang, Z.Y. Wang, J. Qiao, H. Schatten, Q.Y. Sun, A novel variant of ER-alpha, ER-alpha36 mediates testosterone-stimulated ERK and Akt activation in endometrial cancer Hec1A cells. Reprod. Biol. Endocrinol. 7, 1–8 (2009)\nX. Zhang, Z.Y. Wang, Estrogen receptor-α variant, ER-α36, is involved in tamoxifen resistance and estrogen hypersensitivity. Endocrinology 154, 1990–1998 (2013). https:\u002F\u002Fdoi.org\u002F10.1210\u002Fen.2013-1116\nJ. Cao, L. Teng, Estrogen receptor-α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells. Mol. Oncol. 7, 611–624 (2013)\nZ. Wang, X. Zhang, P. Shen, B.W. Loggie, Y. Chang, T.F. Deuel, A variant of estrogen receptor-{alpha}, hER-{alpha}36: Transduction of estrogen- and antiestrogen-dependent membrane-initiated mitogenic signaling. Proc. Natl. Acad. Sci. U. S. A. 103, 9063–9068 (2006). https:\u002F\u002Fdoi.org\u002F10.1073\u002Fpnas.0603339103\nS.L. Lin, L.Y. Yan, X.T. Zhang, J. Yuan, M. Li, J. Qiao, Z.Y. Wang, Q.Y. Sun, ER-alpha36, a variant of ER-alpha, promotes tamoxifen agonist action in endometrial cancer cells via the MAPK\u002FERK and PI3K\u002FAkt pathways. PLoS One 5, e9013 (2010). https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0009013\nJ.S. Tong, Q.H. Zhang, Z.B. Wang, S. Li, C.R. Yang, X.Q. Fu, Y. Hou, Z.Y. Wang, J. Sheng, Q.Y. Sun, ER-α36, a novel variant of ER-α, mediates estrogen-stimulated proliferation of endometrial carcinoma cells via the PKCδ\u002FERK pathway. PLoS One 5, e15408 (2010). https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0015408\nX.T. Zhang, L. Ding, L.G. Kang, Z.Y. Wang, Involvement of ER-α36, Src, EGFR and STAT5 in the biphasic estrogen signaling of ER-negative breast cancer cells. Oncol. Rep. 27, 2057–2065 (2012). https:\u002F\u002Fdoi.org\u002F10.3892\u002For.2012.1722\nX.T. Zhang, L.G. Kang, L. Ding, S. Vranic, Z. Gatalica, Z.Y. Wang, A positive feedback loop of ER-α36\u002FEGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30, 770–780 (2011). https:\u002F\u002Fdoi.org\u002F10.1038\u002Fonc.2010.458\nL.M. Lee, J. Cao, H. Deng, P. Chen, Z. Gatalica, Z.Y. Wang, ER-alpha36, a novel variant of ER-alpha, is expressed in ER-positive and -negative human breast carcinomas. Anticancer Res. 28, 479–483 (2008)\nB.B. Tu, S.L. Lin, L.Y. Yan, Z.Y. Wang, Q.Y. Sun, J. Qiao, ER-α36, a novel variant of estrogen receptor α, is involved in EGFR-related carcinogenesis in endometrial cancer. Am. J. Obstet. Gynecol. 205, e1–e6 (2011)\nH. Deng, X. Huang, J. Fan, L. Wang, Q. Xia, X. Yang, Z. Wang, L. Liu, A variant of estrogen receptor-alpha, ER-alpha36 is expressed in human gastric cancer and is highly correlated with lymph node metastasis. Oncol. Rep. 24, 171–176 (2010)\nA.S. Lee, The glucose-regulated proteins: Stress induction and clinical applications. Trends Biochem. Sci. 26, 504–510 (2001). https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0968-0004(01)01908-9\nA.S. Lee, Glucose-regulated proteins in cancer: Molecular mechanisms and therapeutic potential. Nat. Rev. Cancer 14, 263–276 (2014). https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnrc3701\nA. Altmeyer, R.G. Maki, A.M. Feldweg, M. Heike, V.P. Protopopov, S.K. Masur, P.K. Srivastava, Tumor-specific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96. Int. J. Cancer 69, 340–349 (1996). https:\u002F\u002Fdoi.org\u002F10.1002\u002F(SICI)1097-0215(19960822)69:4\u003C340::AID-IJC18>3.0.CO;2-9\nK. Melendez, E.S. Wallen, B.S. Edwards, C.D. Mobarak, D.G. Bear, P.L. Moseley, Heat shock protein 70 and glycoprotein 96 are differentially expressed on the surface of malignant and nonmalignant breast cells. Cell Stress Chaperones 11, 334–342 (2006). https:\u002F\u002Fdoi.org\u002F10.1379\u002FCSC-187.1\nJ.G. Kiang, I.D. Gist, G.C. Tsokos, 17 beta-estradiol-induced increases in glucose-regulated protein 78kD and 94kD protect human breast cancer T47-D cells from thermal injury. Chin. J. Phys. 40, 213–219 (1997)\nP. Scriven, S. Coulson, R. Haines, S. Balasubramanian, S. Cross, L. Wyld, Activation and clinical significance of the unfolded protein response in breast cancer. Br. J. Cancer 101, 1692–1698 (2009). https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsj.bjc.6605365\nY.Z. Zheng, Z.G. Cao, X. Hu, Z.M. Shao, The endoplasmic reticulum stress markers GRP78 and CHOP predict disease-free survival and responsiveness to chemotherapy in breast cancer. Breast Cancer Res. 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Investig. 94, 906–916 (2014). https:\u002F\u002Fdoi.org\u002F10.1038\u002Flabinvest.2014.63\nZ. Fu, H. Zhen, F. Zou, X. Wang, Y. Chen, L. Liu, Involvement of the Akt signaling pathway in ER-α36\u002FGRP94-mediated signaling in gastric cancer. Oncol. Lett. 8, 2077–2080 (2014). https:\u002F\u002Fdoi.org\u002F10.3892\u002Fol.2014.2514\nZ. Fu, H. Deng, X. Wang, X. Yang, Z. Wang, L. Liu, Involvement of ER-α36 in the malignant growth of gastric carcinoma cells is associated with GRP94 overexpression. Histopathology 63, 325–333 (2013). https:\u002F\u002Fdoi.org\u002F10.1111\u002Fhis.12171",{"VOID":2886},"10.1007\u002Fs13402-017-0368-y","2025-02-26T15:58:11.312+00:00","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs13402-017-0368-y",[2890,2905,2918,2933,2946,2959,2974],{"id":2891,"sortIndex":21,"researcher":20,"roles":2892,"affiliations":2893,"properties":2902,"displayName":2904,"givenName":20,"familyName":20},"299e8151-cb59-42da-a9fe-96f542bae8df",[754],[2894],{"id":2895,"sortIndex":21,"affiliation":2896,"properties":20},"5ca3ca43-0f5a-4001-a174-9901ef7967b6",{"id":2895,"createTime":20,"updateTime":20,"relativeEntities":2897,"slug":20,"properties":2898,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2901,"statistic":20},[],{"title":2899},{"VI":2900},"Department of Biochemistry and Molecular Biology, Molecular Medicine and Cancer Research Center, Chongqing Medical University, Chongqing, China",[],{"title":2903},{"VI":2904},"Yu-Jie Dai",{"id":2906,"sortIndex":219,"researcher":20,"roles":2907,"affiliations":2908,"properties":2915,"displayName":2917,"givenName":20,"familyName":20},"a45d6385-adf3-48d9-aedb-aec2d1ffca88",[754],[2909],{"id":2895,"sortIndex":21,"affiliation":2910,"properties":20},{"id":2895,"createTime":20,"updateTime":20,"relativeEntities":2911,"slug":20,"properties":2912,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2914,"statistic":20},[],{"title":2913},{"VI":2900},[],{"title":2916},{"VI":2917},"Yi-Bo Qiu",{"id":2919,"sortIndex":237,"researcher":20,"roles":2920,"affiliations":2921,"properties":2930,"displayName":2932,"givenName":20,"familyName":20},"15f69318-be99-4cd9-8319-910abd0edf8f",[754],[2922],{"id":2923,"sortIndex":21,"affiliation":2924,"properties":20},"2bf648d5-bd4d-4036-88df-f930e3ecd3c2",{"id":2923,"createTime":20,"updateTime":20,"relativeEntities":2925,"slug":20,"properties":2926,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2929,"statistic":20},[],{"title":2927},{"VI":2928},"Department of Pathology, Molecular Medicine and Cancer Research Center, Chongqing Medical University, Chongqing, China",[],{"title":2931},{"VI":2932},"Rong Jiang",{"id":2934,"sortIndex":253,"researcher":20,"roles":2935,"affiliations":2936,"properties":2943,"displayName":2945,"givenName":20,"familyName":20},"abb585b0-0d6f-4c59-b413-500c6b754edb",[754],[2937],{"id":2923,"sortIndex":21,"affiliation":2938,"properties":20},{"id":2923,"createTime":20,"updateTime":20,"relativeEntities":2939,"slug":20,"properties":2940,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2942,"statistic":20},[],{"title":2941},{"VI":2928},[],{"title":2944},{"VI":2945},"Man Xu",{"id":2947,"sortIndex":271,"researcher":20,"roles":2948,"affiliations":2949,"properties":2956,"displayName":2958,"givenName":20,"familyName":20},"f45c65e5-291a-4671-8692-44289b95d0a9",[754],[2950],{"id":2895,"sortIndex":21,"affiliation":2951,"properties":20},{"id":2895,"createTime":20,"updateTime":20,"relativeEntities":2952,"slug":20,"properties":2953,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2955,"statistic":20},[],{"title":2954},{"VI":2900},[],{"title":2957},{"VI":2958},"Ling-Yao Liao",{"id":2960,"sortIndex":287,"researcher":20,"roles":2961,"affiliations":2962,"properties":2971,"displayName":2973,"givenName":20,"familyName":20},"d1e36e27-3e4b-40ef-ac2b-0e0ef7ce92e9",[754],[2963],{"id":2964,"sortIndex":21,"affiliation":2965,"properties":20},"2b5d5e68-41ed-4c5f-bb55-4db3e5980f7a",{"id":2964,"createTime":20,"updateTime":20,"relativeEntities":2966,"slug":20,"properties":2967,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2970,"statistic":20},[],{"title":2968},{"VI":2969},"Department of Surgery, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong, China",[],{"title":2972},{"VI":2973},"George G. 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Previously, we found that the acetylation levels of chloride intracellular channel 1 (CLIC1) at lysine 131 were increased in cervical cancer tissues using a label-free proteomics approach. The aim of this study was to further determine the role of CLIC1 expression and its acetylation in cervical cancer. CLIC1 expression and its implications for the prognosis of cervical cancer were analyzed using primary patient samples and cells, and the Gene Expression Profiling Interactive Analysis (GEPIA) database (gepia.cancer-pku.cn). The effect of CLIC1 on cervical cancer cells was evaluated using Cell Counting Kit (CCK)-8, flow cytometry, scratch wound healing, transwell, Western blotting and co-immunoprecipitation (Co-IP) assays. In vivo tumor growth was assessed using mouse xenograft models. We found that CLIC1 expression was increased in cervical cancer tissues and cells and that patients with a high CLIC1 expression tended to have a shorter overall survival time. Knockdown of CLIC1 significantly reduced in vitro cervical cancer cell proliferation, migration and invasion, and in vivo tumorigenesis. At the molecular level, we found that nuclear factor kappa B (NF-κB) activity was positively regulated by CLIC1. Pyrrolidine dithiocarbamate (PDTC), an inhibitor of NF-κB, attenuated the tumor-promoting effect of CLIC1. Moreover, we found that CLIC1 acetylation at K131 was upregulated in cervical cancer cells, which stabilized CLIC1 by inhibiting its ubiquitynation. Substitution of K131 inhibited CLIC1 ubiquitynation and promoted in vitro cervical cancer cell proliferation, migration and invasion, and in vivo tumor growth. In addition, we found that acetyltransferase HAT1 was responsible for CLIC1 acetylation at K131. Our data indicate that CLIC1 acts as a tumor promoter in cervical cancer, suggesting a potential treatment strategy for cervical cancer by regulating CLIC1 expression and\u002For acetylation.",{"EN":3058},"Acetylation-stabilized chloride intracellular channel 1 exerts a tumor-promoting effect on cervical cancer cells by activating NF-κB",{"VOID":3060},"F. Bray, J. Ferlay, I. Soerjomataram, R.L. Siegel, L.A. Torre, A. Jemal, Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 68, 394–424 (2018)\nP.A. Cohen, A. Jhingran, A. Oaknin, L. Denny, Cervical cancer. Lancet 393, 169–182 (2019)\nR. Wei, G. Jiang, M. Lv, S. Tan, X. Wang, Y. Zhou, T. Cheng, X. Gao, X. Chen, W. Wang, C. Zou, F. Li, X. Ma, J. Hu, D. Ma, D. Luo, L. Xi, TMTP1-modified indocyanine green-loaded polymeric micelles for targeted imaging of cervical cancer and metastasis sentinel lymph node in vivo. Theranostics 9, 7325–7344 (2019)\nS. Averaimo, R.H. Milton, M.R. Duchen, M. Mazzanti, Chloride intracellular channel 1 (CLIC1): Sensor and effector during oxidative stress. FEBS Lett 584, 2076–2084 (2010)\nP. Samaras, T. Schmidt, M. Frejno, S. Gessulat, M. Reinecke, A. Jarzab, J. Zecha, J. Mergner, P. Giansanti, H.C. Ehrlich, S. Aiche, J. Rank, H. Kienegger, H. Krcmar, B. Kuster, M. Wilhelm, ProteomicsDB: A multi-omics and multi-organism resource for life science research. Nucleic Acids Res 48, D1153–D1163 (2020)\nJ.Y. Yang, J.Y. Jung, S.W. Cho, H.J. Choi, S.W. Kim, S.Y. Kim, H.J. Kim, C.H. Jang, M.G. Lee, J. Han, C.S. Shin, Chloride intracellular channel 1 regulates osteoblast differentiation. Bone 45, 1175–1185 (2009)\nG. Novarino, C. Fabrizi, R. Tonini, M.A. Denti, F. Malchiodi-Albedi, G.M. Lauro, B. Sacchetti, S. Paradisi, A. Ferroni, P.M. Curmi, S.N. Breit, M. Mazzanti, Involvement of the intracellular ion channel CLIC1 in microglia-mediated beta-amyloid-induced neurotoxicity. J Neurosci 24, 5322–5330 (2004)\nS. Averaimo, M. Gritti, E. Barini, L. Gasparini, M. Mazzanti, CLIC1 functional expression is required for cAMP-induced neurite elongation in post-natal mouse retinal ganglion cells. J Neurochem 131, 444–456 (2014)\nX. Jiang, Y. Liu, G. Wang, Y. Yao, C. Mei, X. Wu, W. Ma, Y. Yuan, Up-regulation of CLIC1 activates MYC signaling and forms a positive feedback regulatory loop with MYC in hepatocellular carcinoma. Am J Cancer Res 10, 2355–2370 (2020)\nQ. Ding, M. Li, X. Wu, L. Zhang, W. Wu, Q. Ding, H. Weng, X. Wang, Y. Liu, CLIC1 overexpression is associated with poor prognosis in gallbladder cancer. Tumour Biol 36, 193–198 (2015)\nJ. Lu, Q. Dong, B. Zhang, X. Wang, B. Ye, F. Zhang, X. Song, G. Gao, J. Mu, Z. Wang, F. Ma, J. Gu, Chloride intracellular channel 1 (CLIC1) is activated and functions as an oncogene in pancreatic cancer. Med Oncol 32, 616 (2015)\nM. Setti, N. Savalli, D. Osti, C. Richichi, M. Angelini, P. Brescia, L. Fornasari, M.S. Carro, M. Mazzanti, G. Pelicci, Functional role of CLIC1 ion channel in glioblastoma-derived stem\u002Fprogenitor cells. J Natl Cancer Inst 105, 1644–1655 (2013)\nA. Nesiu, A.M. Cimpean, R.A. Ceausu, A. Adile, I. Ioiart, C. Porta, M. Mazzanti, T.C. Camerota, M. Raica, Intracellular chloride ion channel protein-1 expression in clear cell renal cell carcinoma. Cancer Genomics Proteomics 16, 299–307 (2019)\nB. Singha, S.L. Harper, A.R. Goldman, B.G. Bitler, K.M. Aird, M.E. Borowsky, M.G. Cadungog, Q. Liu, R. Zhang, S. Jean, R. Drapkin, D.W. Speicher, CLIC1 and CLIC4 complement CA125 as a diagnostic biomarker panel for all subtypes of epithelial ovarian cancer. Sci Rep 8, 14725 (2018)\nL. Kong, Q. Wu, L. Zhao, J. Ye, N. Li, H. Yang, Upregulated lncRNA-UCA1 contributes to metastasis of bile duct carcinoma through regulation of miR-122\u002FCLIC1 and activation of the ERK\u002FMAPK signaling pathway. Cell Cycle 18, 1212–1228 (2019)\nH. Katayama, P. Tsou, M. Kobayashi, M. Capello, H. Wang, F. Esteva, M.L. 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