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Increasing evidence state that Nrf2 contributes to chemoresistance in several kinds of cancer. However, its role in endometrial cancer cells remains unclarified. Immunohistochemistry staining was used to detect the expression of Nrf2 in normal patient and endometrial cancer patient. Stable transfection Ishikawa cell line with high level of Nrf2 was established to evaluate its role in chemoresistance. Dot blot assays were used to assess global hydroxymethylation level after stigmasterol treatment. Cellular growth profile was detected by CCK8 assay. Western blot was used to evaluate the changes of the target molecules after various treatments. Nrf2 is overexpressed in endometrial cancer tissues compared with the normal endometrium. Overexpression of Nrf2 resulted in decrease sensitivity to cisplatin. In addition, stigmasterol has been identified as a novel Nrf2 inhibitor. It enhanced the sensitivity of endometrial cancer cells to cisplatin, and the underlying mechanism is that stigmasterol declines the Nrf2 protein level. Our findings identified stigmasterol as a new potential inhibitor of Nrf2 and highlight a critical role of stigmasterol in overcoming chemoresistance in endometrial cancer therapy.",{"EN":142,"VI":143},"Stigmasterol sensitizes endometrial cancer cells to chemotherapy by repressing Nrf2 signal pathway","Stigmasterol làm tăng độ nhạy của tế bào ung thư nội mạc tử cung với hoá trị bằng cách ức chế con đường tín hiệu Nrf2",{"VOID":145},"Satyaswaroop PG, Clarke CL, Zaino RJ, Mortel R. Apparent resistance in human endometrial carcinoma during combination treatment with tamoxifen and progestin may result from desensitization following downregulation of tumor progesterone receptor. Cancer Lett. 1992;62(2):107–14.\nPerez-Medina T, Bajo J, Folgueira G, Haya J, Ortega P. Atypical endometrial hyperplasia treatment with progestogens and gonadotropin-releasing hormone analogues: long-term follow-up. Gynecol Oncol. 1999;73(2):299–304.\nBen-Arie A, Perlman S, Hazan Y, Solomon LA, Edwards C, Kaplan AL. High-risk endometrial cancer in young indigent women. Int J Gynecol Cancer. 2004;14(5):927–30.\nJemal A, Siegel R, Ward E, Hao Y, Xu J, Thun MJ. Cancer statistics, 2009. CA Cancer J Clin. 2009;59(4):225–49.\nZivanovic O, Carter J, Kauff ND, Barakat RR. A review of the challenges faced in the conservative treatment of young women with endometrial carcinoma and risk of ovarian cancer. Gynecol Oncol. 2009;115(3):504–9.\nChaudhry P, Asselin E. Resistance to chemotherapy and hormone therapy in endometrial cancer. Endocr Relat Cancer. 2009;16(2):363–80.\nKobayashi A, Kang MI, Okawa H, Ohtsuji M, Zenke Y, Chiba T, et al. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol Cell Biol. 2004;24(16):7130–9.\nCho JM, Manandhar S, Lee HR, Park HM, Kwak MK. Role of the Nrf2-antioxidant system in cytotoxicity mediated by anticancer cisplatin: implication to cancer cell resistance. Cancer Lett. 2008;260(1–2):96–108.\nShibata T, Kokubu A, Gotoh M, Ojima H, Ohta T, Yamamoto M, et al. Genetic alteration of Keap1 confers constitutive Nrf2 activation and resistance to chemotherapy in gallbladder cancer. Gastroenterology. 2008;135(4):1358–68.\nHomma S, Ishii Y, Morishima Y, Yamadori T, Matsuno Y, Haraguchi N, et al. Nrf2 enhances cell proliferation and resistance to anticancer drugs in human lung cancer. Clin Cancer Res. 2009;15(10):3423–32.\nWang XJ, Sun Z, Villeneuve NF, Zhang S, Zhao F, Li Y, et al. Nrf2 enhances resistance of cancer cells to chemotherapeutic drugs, the dark side of Nrf2. Carcinogenesis. 2008;29(6):1235–43.\nSingh A, Boldin-Adamsky S, Thimmulappa RK, Rath SK, Ashush H, Coulter J, et al. RNAi-mediated silencing of nuclear factor erythroid-2-related factor 2 gene expression in non-small cell lung cancer inhibits tumor growth and increases efficacy of chemotherapy. Cancer Res. 2008;68(19):7975–84.\nSingh A, Venkannagari S, Oh KH, Zhang YQ, Rohde JM, Liu L, et al. Small molecule inhibitor of NRF2 selectively intervenes therapeutic resistance in KEAP1-deficient NSCLC tumors. ACS Chem Biol. 2016;11(11):3214–25.\nWang XJ, Hayes JD, Henderson CJ, Wolf CR. Identification of retinoic acid as an inhibitor of transcription factor Nrf2 through activation of retinoic acid receptor alpha. Proc Natl Acad Sci USA. 2007;104(49):19589–94.\nXu J, Wang H, Ding K, Zhang L, Wang C, Li T, et al. Luteolin provides neuroprotection in models of traumatic brain injury via the Nrf2-ARE pathway. Free Radic Biol Med. 2014;71:186–95.\nZhong Y, Zhang F, Sun Z, Zhou W, Li ZY, You QD, et al. Drug resistance associates with activation of Nrf2 in MCF-7\u002FDOX cells, and wogonin reverses it by down-regulating Nrf2-mediated cellular defense response. Mol Carcinog. 2013;52(10):824–34.\nZhou X, Wang W, Wang C, Zheng C, Xu X, Ni X, et al. DPP4 Inhibitor Attenuates Severe Acute Pancreatitis-Associated Intestinal Inflammation via Nrf2 Signaling. Oxid Med Cell Longev. 2019;2019:6181754.\nJaramillo MC, Zhang DD. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev. 2013;27(20):2179–91.\nJiang T, Chen N, Zhao F, Wang XJ, Kong B, Zheng W, et al. High levels of Nrf2 determine chemoresistance in type II endometrial cancer. Cancer Res. 2010;70(13):5486–96.\nLu H, Ju DD, Yang GD, Zhu LY, Yang XM, Li J, et al. Targeting cancer stem cell signature gene SMOC-2 Overcomes chemoresistance and inhibits cell proliferation of endometrial carcinoma. EBioMedicine. 2019;40:276–89.\nRen D, Villeneuve NF, Jiang T, Wu T, Lau A, Toppin HA, et al. Brusatol enhances the efficacy of chemotherapy by inhibiting the Nrf2-mediated defense mechanism. Proc Natl Acad Sci USA. 2011;108(4):1433–8.\nBai M, Yang L, Liao H, Liang X, Xie B, Xiong J, et al. Metformin sensitizes endometrial cancer cells to chemotherapy through IDH1-induced Nrf2 expression via an epigenetic mechanism. Oncogene. 2018;37(42):5666–81.\nTian D, Shi Y, Chen D, Liu Q, Fan F. The Wnt inhibitor LGK-974 enhances radiosensitivity of HepG2 cells by modulating Nrf2 signaling. Int J Oncol. 2017;51(2):545–54.\nLimonciel A, Jennings P. A review of the evidence that ochratoxin A is an Nrf2 inhibitor: implications for nephrotoxicity and renal carcinogenicity. Toxins (Basel). 2014;6(1):371–9.\nTang X, Wang H, Fan L, Wu X, Xin A, Ren H, et al. Luteolin inhibits Nrf2 leading to negative regulation of the Nrf2\u002FARE pathway and sensitization of human lung carcinoma A549 cells to therapeutic drugs. Free Radic Biol Med. 2011;50(11):1599–609.\nHuang C, Xie D, Cui J, Li Q, Gao Y, Xie K. FOXM1c promotes pancreatic cancer epithelial-to-mesenchymal transition and metastasis via upregulation of expression of the urokinase plasminogen activator system. Clin Cancer Res. 2014;20(6):1477–88.\nBao LJ, Jaramillo MC, Zhang ZB, Zheng YX, Yao M, Zhang DD, et al. Nrf2 induces cisplatin resistance through activation of autophagy in ovarian carcinoma. Int J Clin Exp Pathol. 2014;7(4):1502–13.\nShibata T, Kokubu A, Saito S, Narisawa-Saito M, Sasaki H, Aoyagi K, et al. NRF2 mutation confers malignant potential and resistance to chemoradiation therapy in advanced esophageal squamous cancer. Neoplasia. 2011;13(9):864–73.\nSaygin C, Wiechert A, Rao VS, Alluri R, Connor E, Thiagarajan PS, et al. CD55 regulates self-renewal and cisplatin resistance in endometrioid tumors. J Exp Med. 2017;214(9):2715–32.\nEritja N, Chen BJ, Rodriguez-Barrueco R, Santacana M, Gatius S, Vidal A, et al. Autophagy orchestrates adaptive responses to targeted therapy in endometrial cancer. Autophagy. 2017;13(3):608–24.\nWu J, Bao L, Zhang Z, Yi X. Nrf2 induces cisplatin resistance via suppressing the iron export related gene SLC40A1 in ovarian cancer cells. Oncotarget. 2017;8(55):93502–15.\nLee JH, Rangappa S, Mohan CD, Sethi G, Lin ZX, et al. Brusatol a Nrf2 inhibitor targets STAT3 signaling cascade in head and neck squamous cell carcinoma. Biomolecules. 2019;9:550.\nOlayanju A, Copple IM, Bryan HK, Edge GT, Sison RL, Wong MW, et al. Brusatol provokes a rapid and transient inhibition of Nrf2 signaling and sensitizes mammalian cells to chemical toxicity-implications for therapeutic targeting of Nrf2. 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and ornithine decarboxylase (ODC) are essential for cell proliferation. DL-α-difluoromethylornithine (DFMO), a synthetic inhibitor of ODC, induces G1 arrest through dephosphorylation of retinoblastoma protein (pRb). The effect of DFMO on cell growth of pRb deficient cells is not known. We examined the effects of DFMO on pRb deficient human retinoblastoma Y79 cell proliferation and its molecular mechanism. Using cultured Y79 cells, the effects of DFMO were studied by using polyamine analysis, western blot, gel shift, FACS and promoter analysis. DFMO suppressed the proliferation of Y79 cells, which accumulated in the G1 and S phase. DFMO induced p27\u002FKip1 protein expression, p107 dephosphorylation and accumulation of p107\u002FE2F-4 complex in Y79 cells. These results indicate that p107 dephosphorylation and accumulation of p107\u002FE2F-4 complex is involved in G1 and S phase arrest of DFMO treated Y79 cells.",{"EN":386,"VI":387},"Polyamine depletion induces G1 and S phase arrest in human retinoblastoma Y79 cells","Cạn kiệt polyamine gây ngừng pha G1 và S ở tế bào u nguyên bào võng mạc Y79 ở người",{"VOID":389},"Pegg AE: Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res. 1988, 48: 759-774.\nTabor CW, Tabor H: Polyamines. Annu Rev Biochem. 1984, 53: 749-790. 10.1146\u002Fannurev.bi.53.070184.003533.\nLuk GD, Casero RA: Polyamines in normal and cancer cells. Adv Enzyme Regul. 1987, 26: 91-105. 10.1016\u002F0065-2571(87)90007-0.\nLuk GD, Yang P: Polyamines in intestinal and pancreatic adaptation. Gut. 1987, 28: 95-101. 10.1136\u002Fgut.28.Suppl.95.\nLuk GD, Moshier JA, Ehrinpreis MN: Ornithine decarboxylase as a marker for colorectal polyps and cancer. Prog Clin Biol Res. 1988, 279: 227-239.\nAuvinen M, Paasinen A, Andersson LC, Holtta E: Ornithine decarboxylase activity is critical for cell transformation. Nature. 1992, 360: 355-358. 10.1038\u002F360355a0.\nClifford A, Morgan D, Yuspa SH, Soler AP, Gilmour S: Role of ornithine decarboxylase in epidermal tumorigenesis. Cancer Res. 1995, 55: 1680-1686.\nRussell DH: Ornithine decarboxylase as a biological and pharmacological tool. Pharmacology. 1980, 20: 117-129.\nKubota S, Ohsawa N, Takaku F: Effects of DL-alpha-difluoromethyl-ornithine on the growth and metastasis of B16 melanoma in vivo. Int J Cancer. 1987, 39: 244-247. 10.1002\u002Fijc.2910390220.\nMcCann PP, Pegg AE: Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Ther. 1992, 54: 195-215. 10.1016\u002F0163-7258(92)90032-U.\nPegg AE, Shantz LM, Coleman CS: Ornithine decarboxylase as a target for chemoprevention. J Cell Biochem Suppl. 1995, 22: 132-138. 10.1002\u002Fjcb.240590817.\nRay RM, Zimmerman BJ, McCormack SA, Patel TB, Johnson LR: Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1\u002FCip1), p27(Kip1), and p53 in IEC-6 cells. Am J Physiol. 1999, 276: 684-691.\nChoi SH, Kim SW, Choi DH, Min BH, Chun BG: Polyamine-depletion induces p27Kip1 and enhances dexamethasone-induced G1 arrest and apoptosis in human T lymphoblastic leukemia cells. Leuk Res. 2000, 24: 119-127. 10.1016\u002FS0145-2126(99)00161-7.\nNemoto T, Kamei S, Seyama Y, Kubota S: p53 independent G (1) arrest induced by DL-alpha-difluoromethylornithine. Biochem Biophys Res Commun. 2001, 280: 848-854. 10.1006\u002Fbbrc.2000.4227.\nSheer CJ, Roberts JM: CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 1999, 13: 1501-1512.\nHarper JW, Elledge SJ: Cdk inhibitors in development and cancer. Curr Opin Genet Dev. 1996, 6: 56-66. 10.1016\u002FS0959-437X(96)90011-8.\nWeinberg RA: The retinoblastoma protein and cell cycle control. Cell. 1995, 81: 323-330. 10.1016\u002F0092-8674(95)90385-2.\nDyson N: The regulation of E2F by pRB-family proteins. Genes Dev. 1998, 12: 2245-2262.\nMulligan G, Jacks T: The retinoblastoma gene family: cousins with overlapping interests. Trends Genet. 1998, 14: 223-229. 10.1016\u002FS0168-9525(98)01470-X.\nGoodrich DW, Wang NP, Qian YW, Lee EY, Lee WH: The retinoblastoma gene product regulates progression through the G1 phase of the cell cycle. Cell. 1991, 67: 293-302. 10.1016\u002F0092-8674(91)90181-W.\nHinds PW, Mittnacht S, Dulic V, Arnold A, Reed SI, Weinberg RA: Regulation of retinoblastoma protein functions by ectopic expression of human cyclins. Cell. 1992, 70: 993-1006. 10.1016\u002F0092-8674(92)90249-C.\nZhu L, van den Heuvel S, Helin K, Fattaey A, Ewen M, Livingston D, Dyson N, Harlow E: Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein. Genes Dev. 1993, 7: 1111-1125. 10.1101\u002Fgad.7.7a.1111.\nHoshikawa Y, Mori A, Amimoto K, Iwabe K, Hatakeyama M: Control of retinoblastoma protein-independent hematopoietic cell cycle by the pRB-related p130. Proc Natl Acad Sci USA. 1998, 95: 8574-8579. 10.1073\u002Fpnas.95.15.8574.\nJiang H, Karnezis AN, Tao M, Guida PM, Zhu L: pRB and p107 have distinct effects when expressed in pRB-deficient tumor cells at physiologically relevant levels. Oncogene. 2000, 19: 3878-3887. 10.1038\u002Fsj.onc.1203722.\nSage J, Mulligan GJ, Attardi LD, Miller A, Chen S, Williams B, Theodorou E, Jacks T: Targeted disruption of the three Rb-related genes leads to loss of G (1) control and immortalization. Genes Dev. 2000, 14: 3037-3050. 10.1101\u002Fgad.843200.\nBeijersbergen RL, Hijmans EM, Zhu L, Bernards R: Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation. EMBO J. 1994, 13: 4080-4086.\nGu W, Bhatia K, Magrath IT, Dang CV, Dalla-Favera R: Binding and suppression of the Myc transcriptional activation domain by p107. Science. 1994, 264: 251-254. 10.1126\u002Fscience.8146655.\nSala A, De Luca A, Giordano A, Peschle C: The retinoblastoma family member p107 binds to B-MYB and suppresses its autoregulatory activity. J Biol Chem. 1996, 271: 28738-28740. 10.1074\u002Fjbc.271.24.14290.\nSterner JM, Dew-Knight S, Musahl C, Kornbluth S, Horowitz JM: Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7. Mol Cell Biol. 1998, 18: 2748-2757.\nAdnane J, Shao Z, Robbins PD: The retinoblastoma susceptibility gene product represses transcription when directly bound to the promoter. J Biol Chem. 1995, 270: 8837-8843. 10.1074\u002Fjbc.270.15.8837.\nBremner R, Cohen BL, Sopta M, Hamel PA, Ingles CJ, Galli BL, Phillips RA: Direct transcriptional repression by pRB and its reversal by specific cyclins. Mol Cell Biol. 1995, 15: 3256-3265.\nBrehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T: Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature. 1998, 391: 597-601. 10.1038\u002F35404.\nFerreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D: The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc Natl Acad Sci USA. 1998, 95: 10493-10498. 10.1073\u002Fpnas.95.18.10493.\nLuo RX, Postigo AA, Dean DC: Rb interacts with histone deacetylase to repress transcription. Cell. 1998, 92: 463-473. 10.1016\u002FS0092-8674(00)80940-X.\nHateboer G, Kerkhoven RM, Shvarts A, Bernards R, Beijersbergen RL: Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins. Genes Dev. 1996, 10: 2960-2970. 10.1101\u002Fgad.10.23.2960.\nRobanus-Maandag E, Dekker M, van der Valk M, Carrozza ML, Jeanny JC, Dannenberg JH, Berns A, Riele H: p107 is a suppressor of retinoblastoma development in pRb-deficient mice. Genes Dev. 1998, 12: 1599-1609.\nKondo T, Higashi H, Nishizawa H, Ishikawa S, Ashizawa S, Yamada M, Makita Z, Koike T, Hatakeyama M: Involvement of pRB-related p107 protein in the inhibition of S phase progression in response to genotoxic stress. J Biol Chem. 2001, 276: 17559-17567. 10.1074\u002Fjbc.M009911200.\nOhtani K, Iwanaga R, Arai M, Huang Y, Matsumura Y, Nakamura M: Cell type-specific E2F activation and cell cycle progression induced by the oncogene product Tax of human T-cell leukemia virus type I. J Biol Chem. 2000, 275: 11154-11163. 10.1074\u002Fjbc.275.15.11154.\nKubota S, Kiyosawa H, Nomura Y, Yamada T, Seyama Y: Ornithine decarboxylase overexpression in mouse 10T1\u002F2 fibroblasts: cellular transformation and invasion. J Natl Cancer Inst. 1997, 89: 567-571. 10.1093\u002Fjnci\u002F89.8.567.\nMorgan DM: Determination of polyamines as their benzoylated derivatives by HPLC. Methods Mol Biol. 1998, 79: 111-118.\nDignam JD, Lebovitz RM, Roeder RG: Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 1983, 11: 1475-1489. 10.1093\u002Fnar\u002F11.5.1475.",{"VOID":391},"10.1186\u002F1475-2867-8-2","2024-12-26T02:55:58.410+00:00",[153],"https:\u002F\u002Fcancerci.biomedcentral.com\u002Farticles\u002F10.1186\u002F1475-2867-8-2",[396,411,424],{"id":397,"sortIndex":21,"researcher":20,"roles":398,"affiliations":399,"properties":408,"displayName":410,"givenName":20,"familyName":20},"4897c36e-ac6d-44c7-bd1a-4c5b826625af",[159],[400],{"id":401,"sortIndex":21,"affiliation":402,"properties":20},"fc23703d-a3a2-4c24-9b19-18036b41f58d",{"id":401,"createTime":20,"updateTime":20,"relativeEntities":403,"slug":20,"properties":404,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":407,"statistic":20},[],{"title":405},{"VI":406},"Department of Ophthalmology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan",[],{"title":409},{"VI":410},"Akiko 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Exp Mol Med. 2008;40(5):514–22.",{"doi":1037},"10.3858\u002Femm.2008.40.5.514",{"id":1039,"createTime":1040,"updateTime":1041,"relativeEntities":1042,"slug":1043,"properties":1044,"entityType":148,"verifyStatus":149,"verifyTime":1055,"verifyNote":151,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1056,"fullTextUrl":20,"authors":1057,"publicationType":316,"publisherRelationship":1169,"citationCount":1224,"citationInfo":1225,"publishDate":1228,"publishYear":1226,"citationAnalyzeStatus":1229,"lastCitationAnalyze":1230,"indexDatabases":1231,"openAccess":20,"references":20,"isForceReanalyzing":375},"e74d2740-dcf5-4198-8135-0ff699887f91","2024-02-11T08:23:25.873+00:00","2026-08-24T23:43:13.107+00:00",[],"Spatial-and-single-cell-analyses-uncover-links-between-ALKBH1-and-tumor-associated-macrophages-in-gastric-cancer",{"abstract":1045,"title":1047,"gsPaper":1049,"references":1051,"doi":1053},{"EN":1046},"AlkB homolog 1, histone H2A dioxygenase (ALKBH1), a crucial enzyme involved in RNA demethylation in humans, plays a significant role in various cellular processes. While its role in tumor progression is well-established, its specific contribution to stomach adenocarcinoma (STAD) remains elusive. This study seeks to explore the clinical and pathological relevance of ALKBH1, its impact on the tumor immune microenvironment, and its potential for precision oncology in STAD. We adopted a comprehensive multi-omics approach to identify ALKBH1 as an potential diagnostic biomarker for STAD, demonstrating its association with advanced clinical stages and reduced overall survival rates. Our analysis involved the utilization of publicly available datasets from GEO and TCGA. We identified differentially expressed genes in STAD and scrutinized their relationships with immune gene expression, overall survival, tumor stage, gene mutation profiles, and infiltrating immune cells. Moreover, we employed spatial transcriptomics to investigate ALKBH1 expression across distinct regions of STAD. Additionally, we conducted spatial transcriptomic and single-cell RNA-sequencing analyses to elucidate the correlation between ALKBH1 expression and immune cell populations. Our findings were validated through immunohistochemistry and bioinformatics on 60 STAD patient samples. Our study unveiled crucial gene regulators in STAD linked with genetic variations, deletions, and the tumor microenvironment. Mutations in these regulators demonstrated a positive association with distinct immune cell populations across six immune datasets, exerting a substantial influence on immune cell infiltration in STAD. Furthermore, we established a connection between elevated ALKBH1 expression and macrophage infiltration in STAD. Pharmacogenomic analysis of gastric cancer cell lines further indicated that ALKBH1 inactivation correlated with heightened sensitivity to specific small-molecule drugs. In conclusion, our study highlights the potential role of ALKBH1 alterations in the advancement of STAD, shedding light on novel diagnostic and prognostic applications of ALKBH1 in this context. We underscore the significance of ALKBH1 within the tumor immune microenvironment, suggesting its utility as a precision medicine tool and for drug screening in the management of STAD.",{"EN":1048},"Spatial and single-cell analyses uncover links between ALKBH1 and tumor-associated macrophages in gastric cancer",{"VOID":1050},"[\"1960771502513784211\"]",{"VOID":1052},"Rawla P, Barsouk A. Epidemiology of gastric cancer: global trends, risk factors and prevention. Prz Gastroenterol. 2019;14(1):26–38.\nStahl P, Seeschaaf C, Lebok P, Kutup A, Bockhorn M, Izbicki JR, Bokemeyer C, Simon R, Sauter G, Marx AH. Heterogeneity of amplification of HER2, EGFR, CCND1 and MYC in gastric cancer. BMC Gastroenterol. 2015;15:7.\nIkeda F, Kiyohasa Y. The epidemiology of gastric cancer: the Hisayama study. 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J Transl Med. 2022;20(1):302.\nTzeng YT, Tsui KH, Tseng LM, Hou MF, Chu PY, Sheu JJ, Li CJ. Integrated analysis of pivotal biomarker of LSM1, immune cell infiltration and therapeutic drugs in breast cancer. J Cell Mol Med. 2022;26(14):4007–20.\nTsai HW, Li CJ, Lin LT, Chiang AJ, Chen SN, Wen ZH, Tsui KH. Expression status and prognostic significance of mitochondrial dynamics OPA3 in human ovarian cancer. Aging (Albany NY). 2022;14(9):3874–86.\nLee J, Kim Y, Jin S, Yoo H, Jeong S, Jeong E, Yoon S. Q-omics: smart software for assisting oncology and cancer research. Mol Cells. 2021;44(11):843–50.\nLi CJ, Lin HY, Ko CJ, Lai JC, Chu PY. A novel biomarker driving poor-prognosis liver cancer: overexpression of the mitochondrial calcium gatekeepers. Biomedicines. 2020. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fbiomedicines8110451.\nHuang Y, Yan J, Li Q, Li J, Gong S, Zhou H, Gan J, Jiang H, Jia GF, Luo C, et al. Meclofenamic acid selectively inhibits FTO demethylation of m6A over ALKBH5. Nucleic Acids Res. 2015;43(1):373–84.\nZhang M, Yang S, Nelakanti R, Zhao W, Liu G, Li Z, Liu X, Wu T, Xiao A, Li H. Mammalian ALKBH1 serves as an N(6)-mA demethylase of unpairing DNA. Cell Res. 2020;30(3):197–210.\nLin Q, Chen JW, Yin H, Li MA, Zhou CR, Hao TF, Pan T, Wu C, Li ZR, Zhu D, et al. DNA N6-methyladenine involvement and regulation of hepatocellular carcinoma development. Genomics. 2022;114(2): 110265.\nWang C, Huang Y, Zhang J, Fang Y. MiRNA-339-5p suppresses the malignant development of gastric cancer via targeting ALKBH1. Exp Mol Pathol. 2020;115: 104449.\nLi H, Zhang Y, Guo Y, Liu R, Yu Q, Gong L, Liu Z, Xie W, Wang C. ALKBH1 promotes lung cancer by regulating m6A RNA demethylation. 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Although therapeutic approaches have improved drastically in the last decades, the prognosis of lung cancer patients remains suboptimal. The canonical nuclear transcription factor kappa B (NF-κB) signalling pathway is critical in the carcinogenesis of lung cancer. The non-canonical NF-κB signalling pathway (represented by RelB) has attracted increasing attention in the pathogenesis of haematological and epithelial malignancies. However, the function of RelB in non-small cell lung cancer (NSCLC) is still unclear. Recently, high expression of RelB has been detected in NSCLC tissues. We have also demonstrated that RelB expression is an independent prognostic factor in NSCLC patients. The mRNA and protein expression of RelB in NSCLC tissues were detected by qRT-PCR and IHC assay. The cell growth of SPC-A1 cells was detected in real-time using the x-Celligence system and xenograft tumour assays. The proliferation capability of cells was detected using a CFSE assay. Cell apoptosis was measured using Annexin V\u002FPI staining, cell cycle was analyzed by the cytometry. Cell migration abilities were detected using the x-Celligence system and wound healing assays. The relative amounts of the active and inactive gelatinases MMP-2 and MMP-9 were examined using gelatin zymography experiments. Apoptosis of RelB depletion SPC-A1 cells after ionizing radiation at 8 Gy. The expression of cellular proliferation signal pathway related-proteins were examined by Western blot analysis. The expression of RelB increases in NSCLC tissues. High RelB expression was significantly correlated with advanced-metastatic stage in patients with NSCLC. RelB-silencing inhibits cell growth in vitro and in vivo. We found that RelB affected cell proliferation by regulating AKT phosphorylation. RelB silencing attenuates the migration and invasion abilities of SPC-A1 cells and is likely related to the down regulation of MMP-9 activity and Integrin β-1 expression. In addition, RelB modulated radiation-induced survival of NSCLC cells predominantly by regulating Bcl-xL expression. Given the involvement of RelB in cell proliferation, migration, invasion, and radio-resistance, RelB functions as an oncogene in NSCLC cells. 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RL, Miller KD, Jemal A. Cancer statistics, 2017. CA Cancer J Clin. 2017;67(1):7–30.",{},{"id":20,"text":1415,"url":20,"identifiers":1416},"Chen W, Zheng R, Baade PD, Zhang S, Zeng H, Bray F, Jemal A, Yu X, He J. Cancer statistics in China, 2015. CA Cancer J Clin. 2016;66(2):115–32.",{},{"id":1418,"text":1419,"url":1420,"identifiers":1421},"4c68646b-0035-4279-8000-0006b275d4fa","Cagle PT, Raparia K, Portier BP. Emerging biomarkers in personalized therapy of lung cancer. Adv Exp Med Biol. 2016;890:25–36.","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":1422},"10.1007\u002Fs10440-022-00541-7",{"id":1418,"text":1424,"url":1420,"identifiers":1425},"Abe Y, Tanaka N. The Hedgehog signaling networks in lung cancer: the mechanisms and roles in tumor progression and implications for cancer therapy. Biomed Res Int. 2016;2016:7969286.",{"doi":1422},{"id":1418,"text":1427,"url":1420,"identifiers":1428},"Ghosh S, Dass JF. 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Mol Cell Biol. 2009;29(14):3832–44.",{"doi":1422},{"id":1418,"text":1448,"url":1420,"identifiers":1449},"Rojo F, Gonzalez-Perez A, Furriol J, Nicolau MJ, Ferrer J, Burgués O, Sabbaghi M, González-Navarrete I, Cristobal I, Serrano L, Zazo S, Madoz J, Servitja S, Tusquets I, Albanell J, Lluch A, Rovira A, Eroles P. Non-canonical NF-kappaB pathway activation predicts outcome in borderline oestrogen receptor positive breast carcinoma. Br J Cancer. 2016;115(3):322–31.",{"doi":1422},{"id":1418,"text":1451,"url":1420,"identifiers":1452},"Guo F, Kang S, Zhou P, Guo L, Ma L, Hou J. Maspin expression is regulated by the non-canonical NF-kappaB subunit in androgen-insensitive prostate cancer cell lines. Mol Immunol. 2011;49(1–2):8–17.",{"doi":1422},{"id":1418,"text":1454,"url":1420,"identifiers":1455},"Chen W, Li Z, Bai L, Lin Y. NF-kappaB in lung cancer, a carcinogenesis mediator and a prevention and therapy target. Front Biosci (Landmark Ed). 2011;16:1172–85.",{"doi":1422},{"id":1418,"text":1457,"url":1420,"identifiers":1458},"Meylan E, Dooley AL, Feldser DM, Shen L, Turk E, Ouyang C, Jacks T. Requirement for NF-kappaB signalling in a mouse model of lung adenocarcinoma. Nature. 2009;462(7269):104–7.",{"doi":1422},{"id":1418,"text":1460,"url":1420,"identifiers":1461},"Basseres DS, Ebbs A, Levantini E, Baldwin AS. Requirement of the NF-kappaB subunit p65\u002FRelA for K-Ras-induced lung tumorigenesis. Cancer Res. 2010;70(9):3537–46.",{"doi":1422},{"id":1418,"text":1463,"url":1420,"identifiers":1464},"Li D, Beisswenger C, Herr C, Hellberg J, Han G, Zakharkina T, Voss M, Wiewrodt R, Bohle RM, Menger MD, Schmid RM, Stöckel D, Lenhof HP, Bals R. Myeloid cell RelA\u002Fp65 promotes lung cancer proliferation through Wnt\u002Fbeta-catenin signaling in murine and human tumor cells. Oncogene. 2014;33(10):1239–48.",{"doi":1422},{"id":1418,"text":1466,"url":1420,"identifiers":1467},"Dimitrakopoulos FI, Antonacopoulou AG, Kottorou A, Vlotinou H, Panagopoulos ND, Dougenis D, Scopa C, Papadaki H, Kalofonos HP. NSCLC and the alternative pathway of NF-kappaB: uncovering an unknown relation. Virchows Arch. 2012;460(5):515–23.",{"doi":1422},{"id":1418,"text":1469,"url":1420,"identifiers":1470},"Giopanou I, Lilis I, Papaleonidopoulos V, Marazioti A, Spella M, Vreka M, Papadaki H, Stathopoulos GT. Comprehensive evaluation of nuclear factor-kappaBeta expression patterns in non-small cell lung cancer. PLoS ONE. 2015;10(7):e0132527.",{"doi":1422},{"id":1418,"text":1472,"url":1420,"identifiers":1473},"Qin H, Zhou J, Zhou P, Xu J, Tang Z, Ma H, Guo F. Prognostic significance of RelB overexpression in non-small cell lung cancer patients. Thorac Cancer. 2016;7(4):415–21.",{"doi":1422},{"id":1418,"text":1475,"url":1420,"identifiers":1476},"Ge QL, Liu SH, Ai ZH, Tao MF, Ma L, Wen SY, Dai M, Liu F, Liu HS, Jiang RZ, Xue ZW, Jiang YH, Sun XH, Hu YM, Zhao YX, Chen X, Tao Y, Zhu XL, Ding WJ, Yang BQ, Liu DD, Zhang XR, Teng YC. RelB\u002FNF-kappaB links cell cycle transition and apoptosis to endometrioid adenocarcinoma tumorigenesis. Cell Death Dis. 2016;7(10):e2402.",{"doi":1422},{"id":1478,"text":1479,"url":1480,"identifiers":1481},"f423c909-85a7-4e82-8649-107fa17acfc1","Labouba I, Poisson A, Lafontaine J, Delvoye N, Gannon PO, Le Page C, Saad F, Mes-Masson AM. The RelB alternative NF-kappaB subunit promotes autophagy in 22Rv1 prostate cancer cells in vitro and affects mouse xenograft tumor growth in vivo. Cancer Cell Int. 2014;14:67.","https:\u002F\u002Fcancerci.biomedcentral.com\u002Farticles\u002F10.1186\u002F1475-2867-14-67",{"doi":1482},"10.1186\u002F1475-2867-14-67",{"id":1418,"text":1484,"url":1420,"identifiers":1485},"Yip PY. Phosphatidylinositol 3-kinase–AKT–mammalian target of rapamycin (PI3K–Akt–mTOR) signaling pathway in non-small cell lung cancer. Transl Lung Cancer Res. 2015;4(2):165–76.",{"doi":1422},{"id":1418,"text":1487,"url":1420,"identifiers":1488},"Xu Y, Fang F, Sun Y, Clair DKS, Clair WHS. RelB-dependent differential radiosensitization effect of STI571 on prostate cancer cells. Mol Cancer Ther. 2010;9(4):803–12.",{"doi":1422},{"id":1418,"text":1490,"url":1420,"identifiers":1491},"Demchenko YN, Glebov OK, Zingone A, Keats JJ, Bergsagel PL, Kuehl WM. Classical and\u002For alternative NF-kappaB pathway activation in multiple myeloma. Blood. 2010;115(17):3541–52.",{"doi":1422},{"id":1418,"text":1493,"url":1420,"identifiers":1494},"Vallabhapurapu SD, Noothi SK, Pullum DA, Lawrie CH, Pallapati R, Potluri V, Kuntzen C, Khan S, Plas DR, Orlowski RZ, Chesi M, Kuehl WM, Bergsagel PL, Karin M, Vallabhapurapu S. Transcriptional repression by the HDAC4–RelB–p52 complex regulates multiple myeloma survival and growth. Nat Commun. 2015;6:8428.",{"doi":1422},{"id":1418,"text":1496,"url":1420,"identifiers":1497},"Lee DW, Ramakrishnan D, Valenta J, Parney IF, Bayless KJ, Sitcheran R. The NF-kappaB RelB protein is an oncogenic driver of mesenchymal glioma. PLoS ONE. 2013;8(2):e57489.",{"doi":1422},{"id":1418,"text":1499,"url":1420,"identifiers":1500},"Wang J, Yi S, Zhou J, Zhang Y, Guo F. The NF-kappaB subunit RelB regulates the migration and invasion abilities and the radio-sensitivity of prostate cancer cells. Int J Oncol. 2016;49(1):381–92.",{"doi":1422},{"id":1418,"text":1502,"url":1420,"identifiers":1503},"Wang XM, Li J, Yan MX, Liu L, Jia DS, Geng Q, Lin HC, He XH, Li JJ, Yao M. Integrative analyses identify osteopontin, LAMB3 and ITGB1 as critical pro-metastatic genes for lung cancer. PLoS ONE. 2013;8(2):e55714.",{"doi":1422},{"id":1418,"text":1505,"url":1420,"identifiers":1506},"Ju L, Zhou C. Integrin beta 1 enhances the epithelial–mesenchymal transition in association with gefitinib resistance of non-small cell lung cancer. Cancer Biomark. 2013;13(5):329–36.",{"doi":1422},{"id":1418,"text":1508,"url":1420,"identifiers":1509},"Saito T, Sasaki CY, Rezanka LJ, Ghosh P, Longo DL. p52-Independent nuclear translocation of RelB promotes LPS-induced attachment. Biochem Biophys Res Commun. 2010;391(1):235–41.",{"doi":1422},{"id":1418,"text":1511,"url":1420,"identifiers":1512},"Jiang S, Wang R, Yan H, Jin L, Dou X, Chen D. MicroRNA-21 modulates radiation resistance through upregulation of hypoxia-inducible factor-1alpha-promoted glycolysis in non-small cell lung cancer cells. Mol Med Rep. 2016;13(5):4101–7.",{"doi":1422},{"id":1418,"text":1514,"url":1420,"identifiers":1515},"Rhodes A, Hillen T. Mathematical modeling of the role of survivin on dedifferentiation and radioresistance in cancer. Bull Math Biol. 2016;78(6):1162–88.",{"doi":1422},{"id":1418,"text":1517,"url":1420,"identifiers":1518},"Wei X, Xu Y, Xu FF, Chaiswing L, Schnell D, Noel T, Wang C, Chen JF, Clair DKS, Clair WHS. RelB expression determines the differential effects of ascorbic acid in normal and cancer cells. Cancer Res. 2017;77(6):1345–56.",{"doi":1422},{"id":1418,"text":1520,"url":1420,"identifiers":1521},"Zhu L, Zhu B, Yang L, Zhao X, Jiang H, Ma F. RelB regulates Bcl-xl expression and the irradiation-induced apoptosis of murine prostate cancer cells. Biomed Rep. 2014;2(3):354–8.",{"doi":1422},{"id":1418,"text":1523,"url":1420,"identifiers":1524},"Zhu HC, Qiu T, Dan C, Liu XH, Hu CH. Blockage of RelB expression by gene silencing enhances the radiosensitivity of androgen-independent prostate cancer cells. Mol Med Rep. 2015;11(2):1167–73.",{"doi":1422},{"id":1418,"text":1526,"url":1420,"identifiers":1527},"Braun F, de Carne Trecesson S, Bertin-Ciftci J, Juin P. Protect and serve: Bcl-2 proteins as guardians and rulers of cancer cell survival. Cell Cycle. 2013;12(18):2937–47.",{"doi":1422},{"id":1529,"text":1530,"url":1531,"identifiers":1532},"efd7a036-1ea9-48ab-b786-5e02d5185f17","Llambi F, Green DR. Apoptosis and oncogenesis: give and take in the BCL-2 family. Curr Opin Genet Dev. 2011;21(1):12–20.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0959437X10001966",{"doi":1533},"10.1016\u002Fj.gde.2010.12.001",{"id":1535,"createTime":1536,"updateTime":1537,"relativeEntities":1538,"slug":1539,"properties":1540,"entityType":148,"verifyStatus":149,"verifyTime":1551,"verifyNote":151,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1552,"fullTextUrl":20,"authors":1553,"publicationType":316,"publisherRelationship":1660,"citationCount":20,"citationInfo":20,"publishDate":1714,"publishYear":1405,"citationAnalyzeStatus":1715,"lastCitationAnalyze":1716,"indexDatabases":1717,"openAccess":20,"references":20,"isForceReanalyzing":375},"94fdda93-2f53-4230-8173-375596455744","2023-12-19T09:54:25.226+00:00","2026-08-20T01:51:18.990+00:00",[],"The-experimental-study-of-shunt-decompression-arterialized-vein-flap",{"abstract":1541,"title":1543,"gsPaper":1545,"references":1547,"doi":1549},{"EN":1542},"Arterialized vein flap is a kind of unphysiological flap. Unphysiological reconstruction of blood circulation leads to higher load than that supported by physiological flap and is the culprit of flap swelling, blood stasis, skin blistering, and necrosis after flap grafting. To resolve the multiple disadvantages of traditional flap grafting, by introducing the principles of fluid mechanics, shunt-decompression surgery is prepared to decline the circulation preload and improve the prognosis of arterialized vein flap grafting. By introducing the principles of fluid mechanics, we established the model of shunt-decompression arterialized vein flap, which satisfied the common properties of general fluid that the interface pressure between object and fluid is reduced when the velocity of fluid is increased and vice versa—the effect of Bernoulli. Under this rule, we anastomose the arterialized vein to the branch of main artery of recipient region or make end-to-side anastomosis, which can maintain the blood flow of main artery, decrease the perfusion of flap, and preserve the decompressive effect of main artery to branches. From March, 2016 to September, 2016, we performed animal experiments on ten male bama mini pigs with average weight of 28 ± 2.35 kg. Superior epigastric artery of pig was used for feeding artery to arterialize the superficial epigastric veins. The total area of flap is 8 cm × 6 cm. End-to-side anastomosis and end-to-end anastomosis were established in experimental group and control group, respectively. Doppler speckle perfusion imaging apparatus was used to monitor the alterations of flap perfusion, blood flow of flap, tissue swelling and survival of flaps. The average flap perfusion (PU) at 1 week after surgery is 83.62 ± 3.14 in experimental group and 98.14 ± 6.54 in control group, respectively (P \u003C 0.05), indicating the significant reduction of flap blood perfusion in experimental group as compared with control group. As to the survival of flaps, 7 flaps completely survived, 3 showed partial necrosis, and no one was found as complete necrosis in experimental group, while only 3 flaps survived, and 4 flaps and 3 flaps showed partial necrosis and complete necrosis in control group, respectively (P \u003C 0.05). Based on the physiological features of arterialized vein flap and its problems in clinical application, we improved the anastomosis strategy of flap grafting and obtained excellent experimental outcomes, which provides an insight for the clinical application of arterialized vein flaps.",{"EN":1544},"The experimental study of shunt-decompression arterialized vein flap",{"VOID":1546},"[]",{"VOID":1548},"Tsai TM, Jupiter JB, Serratoni F, Seki T, Okubo K. The effect of hypothermia and tissue perfusion on extended myocutaneous flap viability. Plast Reconstr Surg. 1982;70:444–54.\nYan H, Kolkin J, Zhao B, Li Z, Jiang S, Wang W, Xia Z, Fan C. The effect of hemodynamic remodeling on the survival of arterialized venous flaps. PLoS ONE. 2013;8:e79608.\nKayalar M, Kucuk L, Sugun TS, Gurbuz Y, Savran A, Kaplan I. Clinical applications of free arterialized venous flaps. J Plast Reconstr Aesthetic Surg. 2014;67:1548–56.\nPittet B, Quinodoz P, Alizadeh N, Schlaudraff KU, Mahajan AL. Optimizing the arterialized venous flap. Plast Reconstr Surg. 2008;122:1681–9.\nTay SC, Teoh LC, Tan SH, Yong FC. Extending the reach of the heterodigital arterialized flap by vein division and repair. Plast Reconstr Surg. 2004;114:1450–6.\nYan H, Zhang F, Akdemir O, Songcharoen S, Jones NI, Angel M, Brook D. Clinical applications of venous flaps in the reconstruction of hands and fingers. Arch Orthop Trauma Surg. 2011;131:65–74.\nReynoso R, Haddad JL, Sastre N. A few considerations regarding enhancement of arterialized skin flap survival. Microsurgery. 2000;20:176–80.\nKruse AL, Luebbers HT, Gratz KW, Obwegeser JA. Factors influencing survival of free-flap in reconstruction for cancer of the head and neck: a literature review. Microsurgery. 2010;30:242–8.\nOrganek AJ, Klebuc MJ, Zuker RM. Indications and outcomes of free tissue transfer to the lower extremity in children: review. J Reconstr Microsurg. 2006;22:173–81.\nSaydam FA, Basaran K, Ceran F, Mert B. Foot ischemia after a free fibula flap harvest: immediate salvage with an interpositional sapheneous vein graft. J Craniofac Surg. 2014;25:1784–6.\nSchmidt Y, Bannasch H, Eisenhardt SU. Ischemia-reperfusion injury leads to significant tissue damage in free flap surgery. Plast Reconstr Surg. 2012;129:174e–5e.\nYuen QM, Leung PC. Some factors affecting the survival of venous flaps: an experimental study. Microsurgery. 1991;12:60–4.\nMundy JC, Panje WR. Creation of free flaps by arterialization of the venous system. Arch Otolaryngol. 1984;110:221–3.\nNakayama Y, Soeda S, Kasai Y. Flaps nourished by arterial inflow through the venous system: an experimental investigation. Plast Reconstr Surg. 1981;67:328–34.\nGoldschlager R, Rozen WM, Ting JW, Leong J. The nomenclature of venous flow-through flaps: updated classification and review of the literature. Microsurgery. 2012;32:497–501.\nFrick AF, Baumhauer A, Baumeister RG, Wiebecke B. Experimental studies of the no-reflow phenomenon with prostacyclin. Handchir Mikrochir Plast Chir. 1993;25:296–9.\nKerrigan CL, Zelt RG, Thomson JG, Diano E. The pig as an experimental animal in plastic surgery research for the study of skin flaps, myocutaneous flaps and fasciocutaneous flaps. Lab Anim Sci. 1986;36:408–12.\nSun Z, Wang G, Yang X, Yang J, Teng X, Yin G. Experimental study on effect of natural hirudin on vein congestion of random skin flap in porcine models. Zhongguo Xiu Fu Chong Jian Wai Ke Za Zhi. 2008;22:1296–300.",{"VOID":1550},"10.1186\u002Fs12935-018-0622-z","2024-09-04T15:56:13.038+00:00","https:\u002F\u002Fcancerci.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12935-018-0622-z",[1554,1569,1582,1595,1608,1621,1634,1647],{"id":1555,"sortIndex":21,"researcher":20,"roles":1556,"affiliations":1557,"properties":1566,"displayName":1568,"givenName":20,"familyName":20},"ba792ce8-ec09-4c3b-a6d5-1a46a82ea784",[159],[1558],{"id":1559,"sortIndex":21,"affiliation":1560,"properties":20},"b8a6bc48-db32-4251-9d39-9107a33c333d",{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1561,"slug":20,"properties":1562,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1565,"statistic":20},[],{"title":1563},{"VI":1564},"Department of Hand Surgery, Shenzhen Baoan Shajing People’s Hospital, Shenzhen, People’s Republic of China",[],{"title":1567},{"VI":1568},"Zheng Li",{"id":1570,"sortIndex":96,"researcher":20,"roles":1571,"affiliations":1572,"properties":1579,"displayName":1581,"givenName":20,"familyName":20},"efaf2469-020e-477a-b09a-d4fca8d5a2e6",[159],[1573],{"id":1559,"sortIndex":21,"affiliation":1574,"properties":20},{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1575,"slug":20,"properties":1576,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1578,"statistic":20},[],{"title":1577},{"VI":1564},[],{"title":1580},{"VI":1581},"Zhen-wei Zhang",{"id":1583,"sortIndex":99,"researcher":20,"roles":1584,"affiliations":1585,"properties":1592,"displayName":1594,"givenName":20,"familyName":20},"4781f1d1-937a-4dd1-8e86-f773d398f2ee",[159],[1586],{"id":1559,"sortIndex":21,"affiliation":1587,"properties":20},{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1588,"slug":20,"properties":1589,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1591,"statistic":20},[],{"title":1590},{"VI":1564},[],{"title":1593},{"VI":1594},"Shao-xiao Yu",{"id":1596,"sortIndex":213,"researcher":20,"roles":1597,"affiliations":1598,"properties":1605,"displayName":1607,"givenName":20,"familyName":20},"d1491668-d3de-40b5-9907-24731a896997",[159],[1599],{"id":1559,"sortIndex":21,"affiliation":1600,"properties":20},{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1601,"slug":20,"properties":1602,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1604,"statistic":20},[],{"title":1603},{"VI":1564},[],{"title":1606},{"VI":1607},"Jia-chuan Zhuang",{"id":1609,"sortIndex":227,"researcher":20,"roles":1610,"affiliations":1611,"properties":1618,"displayName":1620,"givenName":20,"familyName":20},"5d05b39d-5ac7-4af5-bc59-feb18f6feb22",[159],[1612],{"id":1559,"sortIndex":21,"affiliation":1613,"properties":20},{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1614,"slug":20,"properties":1615,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1617,"statistic":20},[],{"title":1616},{"VI":1564},[],{"title":1619},{"VI":1620},"Yu-hai Ke",{"id":1622,"sortIndex":241,"researcher":20,"roles":1623,"affiliations":1624,"properties":1631,"displayName":1633,"givenName":20,"familyName":20},"e385de85-1e82-4d2d-b062-6fa9d1a99392",[159],[1625],{"id":1559,"sortIndex":21,"affiliation":1626,"properties":20},{"id":1559,"createTime":20,"updateTime":20,"relativeEntities":1627,"slug":20,"properties":1628,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1630,"statistic":20},[],{"title":1629},{"VI":1564},[],{"title":1632},{"VI":1633},"Yi 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a core member of the FA complex, in the Fanconi anemia pathway, FAAP24 plays an important role in DNA damage repair. However, the association between FAAP24 and patient prognosis in AML and immune infiltration remains unclear. The purpose of this study was to explore its expression characteristics, immune infiltration pattern, prognostic value and biological function using TCGA-AML and to verify it in the Beat AML cohort. In this study, we examined the expression and prognostic value of FAAP24 across cancers using data from TCGA, TARGET, GTEx, and GEPIA2. To further investigate the prognosis in AML, development and validation of a nomogram containing FAAP24 were performed. GO\u002FKEGG, ssGSEA, GSVA and xCell were utilized to explore the functional enrichment and immunological features of FAAP24 in AML. Drug sensitivity analysis used data from the CellMiner website, and the results were confirmed in vitro. Integrated analysis of the TCGA, TARGET and GTEx databases showed that FAAP24 is upregulated in AML; meanwhile, high FAAP24 expression was associated with poor prognosis according to GEPIA2. Gene set enrichment analysis revealed that FAAP24 is implicated in pathways involved in DNA damage repair, the cell cycle and cancer. Components of the immune microenvironment using xCell indicate that FAAP24 shapes an immunosuppressive tumor microenvironment (TME) in AML, which helps to promote AML progression. Drug sensitivity analysis showed a significant correlation between high FAAP24 expression and chelerythrine resistance. In conclusion, FAAP24 could serve as a novel prognostic biomarker and play an immunomodulatory role in AML. \n                           In summary, FAAP24 is a promising prognostic biomarker in AML that requires further exploration and confirmation.",{"EN":1728},"High FAAP24 expression reveals poor prognosis and an immunosuppressive microenvironment shaping in AML",{"VOID":1730},"[\"6429317546864030835\"]",{"EN":1732},"",{"VOID":1734},"Rubnitz JE, Gibson B, Smith FO. Acute myeloid leukemia. Hematol Oncol Clin N Am. 2010;24(1):35–63.\nWelsh J. Acute Myeloid Leukemia Survival Rates and Outlook 2021. Available from: https:\u002F\u002Fwww.verywellhealth.com\u002Facute-myeloid-leukemia-survival-rates-5208865.\nSteffen B, Müller-Tidow C, Schwäble J, Berdel WE, Serve H. The molecular pathogenesis of acute myeloid leukemia. Crit Rev Oncol\u002FHematol. 2005;56(2):195–221.\nTan Y, Zheng L, Du Y, Zhong Q, Zhu Y, Liu ZML, Shuang, et al. Identification of the hub genes and pathways involved in acute myeloid leukemia using bioinformatics analysis. Medicine. 2020;99(35):e22047.\nDonehower L, Soussi T, Korkut A, Liu Y, Schultz A, Cardenas M et al. Integrated Analysis of TP53 Gene and Pathway Alterations in The Cancer Genome Atlas. Cell Reports. 2019;28:1370-84.e5.\nWang C, Zhang S, Ma B, Fu Y, Luo Y. TP53 mutations upregulate RCP expression via Sp1\u002F3 to drive lung cancer progression. Oncogene. 2022;41.\nPrada J, Arroyave Ospina J, Rothlisberger S. Molecular Biomarkers in Acute Myeloid Leukemia. Blood Rev. 2016;31.\nCiccia A, Ling C, Coulthard R, Yan Z, Xue Y, Meetei AR, et al. Identification of FAAP24, a Fanconi Anemia Core Complex protein that interacts with FANCM. Mol Cell. 2007;25(3):331–43.\nde Winter JP, Joenje H. Fanconi Anemia. In: Maloy S, Hughes K, editors. Brenner’s Encyclopedia of Genetics (Second Edition). San Diego: Academic Press; 2013. p. 17–20.\nWang Y, Han X, Wu F, Leung JW, Lowery MG, Do H, et al. Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response. Cell Res. 2013;23(10):1215–28.\nGhosal K, Agatemor C, Han RI, Ku ATT, Sabu MS. Fanconi Anemia DNA Repair Pathway as a New Mechanism to Exploit Cancer Drug Resistance. Mini Rev Med Chem. 2020;20(9):pp. 779 – 87(9).\nWang Y, Leung Justin W, Jiang Y, Lowery Megan G, Do H, Vasquez Karen M, et al. FANCM and FAAP24 maintain Genome Stability via Cooperative as Well as Unique Functions. Mol Cell. 2013;49(5):997–1009.\nGoldman MJ, Craft B, Hastie M, Repečka K, McDade F, Kamath A, et al. Visualizing and interpreting cancer genomics data via the Xena platform. Nat Biotechnol. 2020;38(6):675–8.\nTyner JW, Tognon CE, Bottomly Dea. Functional genomic landscape of acute myeloid leukaemia. Nature. 2018;562(7728):526–31.\nGao J, Aksoy BA, Dogrusoz U, Dresdner G, Gross B, Sumer SO, et al. Integrative analysis of Complex Cancer Genomics and Clinical Profiles using the cBioPortal. Sci Signal. 2013;6(269):pl1–pl.\nReinhold WC, Sunshine M, Liu H, Varma S, Kohn KW, Morris J, et al. CellMiner: a web-based suite of genomic and pharmacologic tools to explore transcript and drug patterns in the NCI-60 Cell Line Set. Cancer Res. 2012;72(14):3499–511.\nTang Z, Kang B, Li C, Chen T, Zhang Z. GEPIA2: an enhanced web server for large-scale expression profiling and interactive analysis. Nucleic Acids Res. 2019;47:W556 - W60.\nVasaikar S, Straub P, Wang J, Zhang B, LinkedOmics. Analyzing multi-omics data within and across 32 cancer types. Nucleic Acids Res. 2017;46.\nChen DS, Mellman I. Oncology meets immunology: the cancer-immunity cycle. Immunity. 2013;39 1:1–10.\nAran D, Hu Z, Butte AJ. xCell: Digitally portraying the tissue cellular heterogeneity landscape. bioRxiv. 2017:114165.\nLi Y, Xiao J, Bai J, et al. Molecular characterization and clinical relevance of m6A regulators across 33 cancer types. Mol Cancer. 2019;18:137. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs12943-019-1066-322.\nTsvetkov P, Coy S, Petrova B, Dreishpoon M, Verma A, Abdusamad M, et al. Copper induces cell death by targeting lipoylated TCA cycle proteins. Sci (New York NY). 2022;375(6586):1254–61.\nXu X, Liu R, Zhou X, Zhang Z, Zhu T, Huang Y et al. Characterization of exosomes derived from IPEC-J2 treated with probiotic Bacillus amyloliquefaciens SC06 and its regulation of macrophage functions. Front Immunol. 2022;13.\nXu X-g, Hu J-f, Ma J-x, Nie L, Shao T, Xiang L-x, et al. Essential roles of TIM-1 and TIM-4 homologs in adaptive humoral immunity in a zebrafish model. J Immunol. 2016;196(4):1686–99.\nEsposito MT, So CWE. DNA damage accumulation and repair defects in acute myeloid leukemia: implications for pathogenesis, disease progression, and chemotherapy resistance. Chromosoma. 2014;123(6):545–61.\nCeccaldi R, Sarangi P, D’Andrea AD. The fanconi anaemia pathway: new players and new functions. Nat Rev Mol Cell Biol. 2016;17(6):337–49.\nHořejší Z, Collis SJ, Boulton SJ. FANCM-FAAP24 and HCLK2: roles in ATR signalling and the Fanconi Anemia pathway. Cell Cycle. 2009;8(8):1133–7.\nSendker S, Reinhardt D, Niktoreh N. Redirecting the Immune Microenvironment in Acute Myeloid Leukemia. Cancers [Internet]. 2021; 13(6).\nHyun SY, Na EJ, Jang JE, Chung H, Kim SJ, Kim JS, et al. Immunosuppressive role of CD11b + CD33 + HLA-DR – myeloid-derived suppressor cells-like blast subpopulation in acute myeloid leukemia. Cancer Med. 2020;9(19):7007–17.\nSumitomo R, Hirai T, Fujita M, Murakami H, Otake Y, Huang CL. M2 tumor–associated macrophages promote tumor progression in non–small–cell lung cancer. Exp Ther Med. 2019;18(6):4490–8.\nJunhua Lv YZ, Suwei Gao C, Zhang Y, Chen W, Li Y-G, Yang Q, Zhou. Feng Liu endothelial-specific m6A modulates mouse hematopoietic stem and progenitor cell development via notch signaling. Cell Res. 2018;28(2):249–52.\nLi Z, Weng H, Su R, Weng X, Zuo Z, Li C, et al. FTO Plays an Oncogenic Role in Acute Myeloid Leukemia as a N6-Methyladenosine RNA Demethylase. Cancer Cell. 2017;31(1):127 – 41.\nXiulin Jiang BL, Zhi Nie L, Duan QX, Jin Z, Yang C. Yongbin Chen. The role of m6A modification in the biological functions and diseases. Signal Transduction and Targeted Therapy 2021;6(74).\nCheng Y, Gao Z, Zhang T, Wang Y, Xie X, Han G et al. Decoding m6A RNA methylome identifies PRMT6-regulated lipid transport promoting AML stem cell maintenance. Cell Stem Cell. 2022;30.\nXuan Zhou ZX, Hehua M et al. A novel cuproptosis-related gene signature can predict prognosis in acute myeloid leukemia. Res Square. 2022.\nYang T, Xu R, Su Q, Wang H, Liu F, Dai B et al. Chelerythrine hydrochloride inhibits proliferation and induces mitochondrial apoptosis in cervical cancer cells via PI3K\u002FBAD signaling pathway. Toxicol In Vitro. 2020;68(104965).\nKang K, Jiang H, Zhang S, Cheng B. Antitumor Effects of Chelerythrine: A literature review. 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Both taxanes induced apoptosis in SK-BR-3 as well as MCF-7 cells. Caspase-2 activity in SK-BR-3 cells increased approximately 15-fold within 48 h after the application of both taxanes at the death-inducing concentration (100 nM). In MCF-7 cells, caspase-2 activity increased approximately 11-fold within 60 h after the application of taxanes (300 nM). Caspase-2 activation was confirmed by decreasing levels of procaspase-2, increasing levels of cleaved caspase-2 and the cleavage of caspase-2 substrate golgin-160. The inhibition of caspase-2 expression using siRNA increased the number of surviving cells more than 2-fold in MCF-7 cells, and at least 4-fold in SK-BR-3 cells, 96 h after the application of death-inducing concentration of taxanes. The inhibition of caspase-2 expression also resulted in decreased cleavage of initiator caspases (caspase-8, caspase-9) as well as executioner caspases (caspase-3, caspase-7) in both cell lines after the application of taxanes. 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Cell Physiol Biochem. 2011, 27: 525-538. 10.1159\u002F000329954.","https:\u002F\u002Fdoi.org\u002F10.1159\u002F000329954",{"mag":2531,"openalex":2532,"pm":2533,"doi":2534},"2051509548","W2051509548","21691070","10.1159\u002F000329954",{"id":2536,"createTime":2537,"updateTime":2538,"relativeEntities":2539,"slug":2540,"properties":2541,"entityType":148,"verifyStatus":149,"verifyTime":2554,"verifyNote":151,"languages":2555,"translateLanguages":20,"viewCount":21,"primaryUrl":2556,"fullTextUrl":20,"authors":2557,"publicationType":316,"publisherRelationship":2641,"citationCount":101,"citationInfo":2696,"publishDate":2699,"publishYear":2697,"citationAnalyzeStatus":1997,"lastCitationAnalyze":2700,"indexDatabases":2701,"openAccess":20,"references":2702,"isForceReanalyzing":375},"3e1eff9f-222d-4440-8056-f589db2a859b","2024-04-19T07:26:05.644+00:00","2026-07-25T21:02:12.773+00:00",[],"Microarray-analysis-of-breast-cancer-gene-expression-profiling-in-response-to-2-deoxyglucose-metformin-and-glucose-starvation",{"openalex":2542,"abstract":2544,"title":2546,"gsPaper":2548,"pm":2550,"doi":2552},{"VOID":2543},"W4220939801",{"EN":2545},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:sec>\n                \u003Cjats:title>Background\u003C\u002Fjats:title>\n                \u003Cjats:p>Breast cancer (BC) is the most frequently diagnosed cancer in women. Altering glucose metabolism and its effects on cancer progression and treatment resistance is an emerging interest in BC research. For instance, combining chemotherapy with glucose-lowering drugs (2-deoxyglucose (2-DG), metformin (MET)) or glucose starvation (GS) has shown better outcomes than with chemotherapy alone. However, the genes and molecular mechanisms that govern the action of these glucose deprivation conditions have not been fully elucidated. Here, we investigated the differentially expressed genes in MCF-7 and MDA-MB-231 BC cell lines upon treatment with glucose-lowering drugs (2-DG, MET) and GS using microarray analysis to study the difference in biological functions between the glucose challenges and their effect on the vulnerability of BC cells.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Methods\u003C\u002Fjats:title>\n                \u003Cjats:p>MDA-MB-231 and MCF-7 cells were treated with 20 mM MET or 4 mM 2-DG for 48 h. GS was performed by gradually decreasing the glucose concentration in the culture medium to 0 g\u002FL, in which the cells remained with fetal bovine serum for one week. Expression profiling was carried out using Affymetrix Human Clariom S microarrays. Differentially expressed genes were obtained from the Transcriptome Analysis Console and enriched using DAVID and R packages.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Results\u003C\u002Fjats:title>\n                \u003Cjats:p>Our results showed that MDA-MB-231 cells were more responsive to glucose deprivation than MCF-7 cells. Endoplasmic reticulum stress response and cell cycle inhibition were detected after all three glucose deprivations in MDA-MB-231 cells and only under the metformin and GS conditions in MCF-7 cells. Induction of apoptosis and inhibition of DNA replication were observed with all three treatments in MDA-MB-231 cells and metformin-treated MCF-7 cells. Upregulation of cellular response to reactive oxygen species and inhibition of DNA repair mechanisms resulted after metformin and GS administration in MDA-MB-231 cell lines and metformin-treated MCF-7 cells. Autophagy was induced after 2-DG treatment in MDA-MB-231 cells and after metformin in MCF-7 cells. Finally, inhibition of DNA methylation were observed only with GS in MDA-MB-231 cells.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>\u003Cjats:sec>\n                \u003Cjats:title>Conclusion\u003C\u002Fjats:title>\n                \u003Cjats:p>The procedure used to process cancer cells and analyze their expression data distinguishes our study from others. GS had the greatest effect on breast cancer cells compared to 2-DG and MET. Combining MET and GS could restrain both cell lines, making them more vulnerable to conventional chemotherapy.\u003C\u002Fjats:p>\n              \u003C\u002Fjats:sec>",{"EN":2547},"Microarray analysis of breast cancer gene expression profiling in response to 2-deoxyglucose, metformin, and glucose starvation",{"VOID":2549},"[\"14951439444369695460\"]",{"VOID":2551},"35305635",{"VOID":2553},"10.1186\u002Fs12935-022-02542-w","2024-05-02T07:54:59.197+00:00",[521],"https:\u002F\u002Fcancerci.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12935-022-02542-w",[2558,2575,2594,2609,2624],{"id":2559,"sortIndex":21,"researcher":20,"roles":2560,"affiliations":2561,"properties":2570,"displayName":2572,"givenName":20,"familyName":20},"c2d8ac00-b19c-46de-8dfb-695428644c3f",[],[2562],{"id":2563,"sortIndex":21,"affiliation":2564,"properties":20},"fe6d1396-a1e4-4a58-9930-562d51dd017e",{"id":2563,"createTime":20,"updateTime":20,"relativeEntities":2565,"slug":20,"properties":2566,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2569,"statistic":20},[],{"title":2567},{"EN":2568},"Cancer and Metabolism Laboratory, Faculty of Medicine, Saint-Joseph University, Beirut, Lebanon",[],{"title":2571,"openalex":2573},{"EN":2572},"Rita Aoun",{"VOID":2574},"A5010071154",{"id":2576,"sortIndex":96,"researcher":20,"roles":2577,"affiliations":2578,"properties":2587,"displayName":2591,"givenName":20,"familyName":20},"11c09cc2-0425-453b-9d66-d95e84bf3a79",[],[2579],{"id":2580,"sortIndex":21,"affiliation":2581,"properties":20},"b4938489-0b0c-4edc-9450-1ef277aaba07",{"id":2580,"createTime":20,"updateTime":20,"relativeEntities":2582,"slug":20,"properties":2583,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2586,"statistic":20},[],{"title":2584},{"VI":2585},"Faculty of Medicine, Saint-Joseph University, Beirut, Lebanon",[],{"orcid":2588,"title":2590,"openalex":2592},{"VOID":2589},"https:\u002F\u002Forcid.org\u002F0000-0003-4167-4944",{"EN":2591},"Christopher El 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Oncotarget. 2016;7:30119–32.",{"doi":3041},"10.18632\u002Foncotarget.8798",{"id":3043,"createTime":3044,"updateTime":3045,"relativeEntities":3046,"slug":3047,"properties":3048,"entityType":148,"verifyStatus":149,"verifyTime":3058,"verifyNote":151,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":3059,"fullTextUrl":20,"authors":3060,"publicationType":316,"publisherRelationship":3184,"citationCount":20,"citationInfo":20,"publishDate":3238,"publishYear":373,"citationAnalyzeStatus":1715,"lastCitationAnalyze":3239,"indexDatabases":3240,"openAccess":20,"references":20,"isForceReanalyzing":375},"65e28254-8e82-4742-8158-8802c6f704ce","2024-01-15T14:09:52.685+00:00","2026-07-23T16:43:20.960+00:00",[],"Multi-dimensional-omics-characterization-in-glioblastoma-identifies-the-purity-associated-pattern-and-prognostic-gene-signatures",{"abstract":3049,"title":3051,"gsPaper":3053,"references":3054,"doi":3056},{"EN":3050},"The presence of tumor-associated stroma and tumor-infiltrated immune cells have been largely reported across glioblastomas. Tumor purity, defined as the proportion of tumor cells in the tumor, was associated with the genomic and clinicopathologic features of the tumor and may alter the interpretation of glioblastoma biology. We use an integrative approach to infer tumor purity based on multi-omic data and comprehensively evaluate the impact of tumor purity on glioblastoma (GBM) prognosis, genomic profiling, and the immune microenvironment in the Cancer Genome Atlas Consortium (TCGA) cohort. We found that low tumor purity was significantly associated with reduced survival time. Additionally, we established a purity-relevant 5-gene signature that was an independent prognostic biomarker and validated it in the TCGA, CGGA and GSE4412 cohort. Moreover, we correlated tumor purity with genomic characteristics and tumor microenvironment. We identified that gamma delta T cells in glioblastoma microenvironment were positively correlated with purity and served as a marker for favorable prognosis, which was validated in both TCGA and CGGA dataset. We observe the potential confounding effects of tumor purity on GBM clinical and molecular information interpretation. GBM microenvironment could be purity-dependent, which provides new insights into the clinical implications of glioblastoma.",{"EN":3052},"Multi-dimensional omics characterization in glioblastoma identifies the purity-associated pattern and prognostic gene signatures",{"VOID":1546},{"VOID":3055},"Jiang T, Mao Y, Ma W, Mao Q, You Y, Yang X, et al. CGCG clinical practice guidelines for the management of adult diffuse gliomas. Cancer Lett. 2016;375(2):263–73.\nHanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell. 2011;144(5):646–74.\nQuail DF, Joyce JA. Microenvironmental regulation of tumor progression and metastasis. 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Nat Rev Immunol. 2015;15(11):683–91.",{"VOID":3057},"10.1186\u002Fs12935-020-1116-3","2024-06-25T00:26:47.101+00:00","https:\u002F\u002Fcancerci.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12935-020-1116-3",[3061,3084,3104,3124,3144,3164],{"id":3062,"sortIndex":21,"researcher":20,"roles":3063,"affiliations":3064,"properties":3082,"displayName":1633,"givenName":20,"familyName":20},"b583da03-9a68-4370-b1b0-b5de50b863f8",[159],[3065,3073],{"id":3066,"sortIndex":21,"affiliation":3067,"properties":20},"3afa9263-8e99-415c-9265-8071f2735dfb",{"id":3066,"createTime":20,"updateTime":20,"relativeEntities":3068,"slug":20,"properties":3069,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":3072,"statistic":20},[],{"title":3070},{"VI":3071},"Department of Neurosurgery, Xiangya Hospital, Central South University, Changsha, 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