This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Dohnal V, Wu Q, Kuca K. Metabolism of aflatoxins: Key enzymes and inter individual as well as interspecies differences. Arch Toxicol. 2014; 29: 155–170.DohnalVWuQKucaKMetabolism of aflatoxins: Key enzymes and inter individual as well as interspecies differences20142915517010.1007/s00204-014-1312-925027283Search in Google Scholar
Hayes JD, Pulford DJ. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev Biochem Mol. 1995; 30: 445–600.HayesJDPulfordDJThe glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance19953044560010.3109/104092395090834918770536Search in Google Scholar
Caccuri AM, Giovanni A. Proton release on the binding of glutathione to alpha Mu and Delta class glutathione transferases. Biochem J. 1999; 344: 419–425.CaccuriAMGiovanniAProton release on the binding of glutathione to alpha Mu and Delta class glutathione transferases199934441942510.1042/bj3440419Search in Google Scholar
Lee HH, Schütte D, Wulf G, Füzesi L, Radzun HJ, Schweyer S, Engel W, Nayernia K. Stem-cell protein Piwil2 is widely expressed in tumours and inhibits apoptosis through activation of Stat3/Bcl-XL pathway. Hum Mol Genet. 2006; 15: 201–211.LeeHHSchütteDWulfGFüzesiLRadzunHJSchweyerSEngelWNayerniaKStem-cell protein Piwil2 is widely expressed in tumours and inhibits apoptosis through activation of Stat3/Bcl-XL pathway20061520121110.1093/hmg/ddi43016377660Search in Google Scholar
Sasaki T, Shiohama A, Minoshima S, Shimizu N. Identification of eight members of the Argonaute family in the human genome. Genomics. 2003; 82: 323–333.SasakiTShiohamaAMinoshimaSShimizuNIdentification of eight members of the Argonaute family in the human genome20038232333310.1016/S0888-7543(03)00129-0Search in Google Scholar
Chen L, Shen R, Ye Y, Pu XA, Liu X, Duan W, Wen J, Zimmerer J, Wang Y, Liu Y, et al. Precancerous stem cells have the potential for both benign and malignant differentiation. PLoS One. 2007; 2: e293.ChenLShenRYeYPuXALiuXDuanWWenJZimmererJWangYLiuYPrecancerous stem cells have the potential for both benign and malignant differentiation20072e29310.1371/journal.pone.0000293180842517356702Search in Google Scholar
Jordan CT, Guzman ML, Noble M. Cancer stem cells. N Engl J Med. 2006; 355: 1253–1261.JordanCTGuzmanMLNobleMCancer stem cells20063551253126110.1056/NEJMra06180816990388Search in Google Scholar
Unhavaithaya Y, Hao Y, Beyret E, Yin H, Miyagawa SK, Nakano T, Lin H. PIWI-interacting RNA-binding protein, is required for germline stem cell self-renewal and appears to positively regulate translation. J Biol Chem. 2009; 284: 6507–6519.UnhavaithayaYHaoYBeyretEYinHMiyagawaSKNakanoTLinHPIWI-interacting RNA-binding protein, is required for germline stem cell self-renewal and appears to positively regulate translation20092846507651910.1074/jbc.M809104200264910619114715Search in Google Scholar
Ye Y, Yin DT, Chen L, Zhou Q, Shen R, He G, Yan Q, Ting Z, Issekutz AC, Shapiro CL, et al. Identification of Piwil2-like (PL2L) proteins that promote tumourigenesis. PLoS One. 2010; 5: e13406.YeYYinDTChenLZhouQShenRHeGYanQTingZIssekutzACShapiroCLIdentification of Piwil2-like (PL2L) proteins that promote tumourigenesis20105e1340610.1371/journal.pone.0013406295811520975993Search in Google Scholar
Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 7: 248–254.BradfordMMA rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding1976724825410.1016/0003-2697(76)90527-3Search in Google Scholar
Habig WH, Pabst MJ, Jakoby WB. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 1974; 249: 7130–7139.HabigWHPabstMJJakobyWBGlutathione S-transferases. The first enzymatic step in mercapturic acid formation19742497130713910.1016/S0021-9258(19)42083-8Search in Google Scholar
Allocati N, Masulli M, Di Ilio C, Federici L. Glutathione transferases: Substrates, inhibitors, and pro-drugs in cancer and neurodegenerative diseases. Oncogenesis. 2018; 7: 8–23.AllocatiNMasulliMDi IlioCFedericiLGlutathione transferases: Substrates, inhibitors, and pro-drugs in cancer and neurodegenerative diseases2018782310.1038/s41389-017-0025-3583387329362397Search in Google Scholar
Dong SC, Sha HH, Xu YY, Hu T, Lou R, Li H, Wu J, Dan C, Freng J. Glutathione S-transferase π: A potential role in antitumour therapy. Dove Med Press. 2018; 12: 3535–3547.DongSCShaHHXuYYHuTLouRLiHWuJDanCFrengJGlutathione S-transferase π: A potential role in antitumour therapy20181235353547Search in Google Scholar
Mahajan S, Atkins WM. The chemistry and biology of inhibitors and prodrugs targeted to glutathione S-transferases. Cell Mol Life Sci. 2005: 62; 1221–1233.MahajanSAtkinsWMThe chemistry and biology of inhibitors and prodrugs targeted to glutathione S-transferases2005621221123310.1007/s00018-005-4524-615798895Search in Google Scholar
Gate L, Tew KD. Glutathione S-transferases as emerging therapeutic targets. Expert Opin Ther Targets. 2001; 5: 477–489.GateLTewKDGlutathione S-transferases as emerging therapeutic targets2001547748910.1517/14728222.5.4.47712540261Search in Google Scholar
Hayes JD, Flanagan JU, Jowsey IR. Glutathione transferases. Annu Rev Pharmacol Toxicol. 2005; 45: 51–88.HayesJDFlanaganJUJowseyIRGlutathione transferases200545518810.1146/annurev.pharmtox.45.120403.09585715822171Search in Google Scholar
Punganuru SR, Mostofa AG, Madala HR, Basak D, Srivenugopal KS. Potent anti-proliferative actions of a non-diuretic glucosamine derivative of ethacrynic acid. Bioorg Med Chem Lett. 2016; 26: 2829–2833.PunganuruSRMostofaAGMadalaHRBasakDSrivenugopalKSPotent anti-proliferative actions of a non-diuretic glucosamine derivative of ethacrynic acid2016262829283310.1016/j.bmcl.2016.04.06227156773Search in Google Scholar
Guneidy RA, Gad AM, Zaki ER, Ibrahim FM, Shooker A. Antioxidant or pro-oxidant and glutathione transferase P1-1 inhibiting activities for Tamarindus indica seeds and their cytotoxic effect on MCF-7 cancer cell line. J Genet Eng Biotechnol. 2020; 18: 74.GuneidyRAGadAMZakiERIbrahimFMShookerAAntioxidant or pro-oxidant and glutathione transferase P1-1 inhibiting activities for Tamarindus indica seeds and their cytotoxic effect on MCF-7 cancer cell line2020187410.1186/s43141-020-00077-z767742133215267Search in Google Scholar
Aybek H, Temel Y, Ahmed BM, Ağca CA, Çiftci M. Deciphering of the effect of chemotherapeutic agents on human glutathione S-transferase enzyme and MCF-7 cell line. Protein & Pept Lett. 2020; 27: 888–894.AybekHTemelYAhmedBMAğcaCAÇiftciMDeciphering of the effect of chemotherapeutic agents on human glutathione S-transferase enzyme and MCF-7 cell line20202788889410.2174/092986652766620041310101732282293Search in Google Scholar
Zeng B, Ge C, Li R, Zhang Z, Fu Q, Zhen L, Lin Z, Liu L, Xue Y, Xu Y, et al. Knockdown of microsomal glutathione S-transferase 1 inhibits lung adenocarcinoma cell proliferation and induces apoptosis. Biomed Pharmacother. 2020; 121: 109562.ZengBGeCLiRZhangZFuQZhenLLinZLiuLXueYXuYKnockdown of microsomal glutathione S-transferase 1 inhibits lung adenocarcinoma cell proliferation and induces apoptosis202012110956210.1016/j.biopha.2019.10956231707341Search in Google Scholar
Sanaei M, Kavaoosi F, Esmi Z. The effect of 5-aza-2′-deoxycytidine in combination to and in comparison with vorinostat on DNA methyltransferases, histone deacetylase 1, glutathione S-transferase 1 and suppressor of cytokine signaling 1 genes expression, cell growth inhibition and apoptotic induction in hepatocellular LCL-PI 11 cell line. Int J Hematol Oncol Stem Cell Res. 2020; 14: 45–55.SanaeiMKavaoosiFEsmiZThe effect of 5-aza-2′-deoxycytidine in combination to and in comparison with vorinostat on DNA methyltransferases, histone deacetylase 1, glutathione S-transferase 1 and suppressor of cytokine signaling 1 genes expression, cell growth inhibition and apoptotic induction in hepatocellular LCL-PI 11 cell line202014455510.18502/ijhoscr.v14i1.2360Search in Google Scholar
Gao JX. Cancer stem cells: The lessons from pre-cancerous stem cells. J Cell Mol Med. 2008; 12: 67–96.GaoJXCancer stem cells: The lessons from pre-cancerous stem cells200812679610.1111/j.1582-4934.2007.00170.x382347318053092Search in Google Scholar
Zhang D, Li D, Shen L. Exosomes derived from Piwil2-induced cancer stem cells transform fibroblasts into cancer-associated fibroblasts. Oncol Rep. 2020; 43: 1125–1132.ZhangDLiDShenLExosomes derived from Piwil2-induced cancer stem cells transform fibroblasts into cancer-associated fibroblasts2020431125113210.3892/or.2020.7496705793632323829Search in Google Scholar
Feng D, Yan K, Liang H, Liang J, Wang W, Yu H, Zhou Y, Zhao W, Dong Z, Ling B. CBP-mediated Wnt3a/β-catenin signaling promotes cervical oncogenesis initiated by Piwil2. Neoplasia. 2021; 23: 1–11.FengDYanKLiangHLiangJWangWYuHZhouYZhaoWDongZLingBCBP-mediated Wnt3a/β-catenin signaling promotes cervical oncogenesis initiated by Piwil220212311110.1016/j.neo.2020.10.013767416133190089Search in Google Scholar
Zou GL, Zhang XR, Ma YL, Lu Q, Zhao R, Zh YZ, Wang YY. The role of Nrf2/PIWIL2/purine metabolism axis in controlling radiation-induced lung fibrosis. Am J Cancer Res. 2020; 10: 2752–2767.ZouGLZhangXRMaYLLuQZhaoRZhYZWangYYThe role of Nrf2/PIWIL2/purine metabolism axis in controlling radiation-induced lung fibrosis20201027522767Search in Google Scholar