Journal of Pharmaceutical Research

References

1. Novikoff AB, Shin WY. Endoplasmic reticulum and autophagy in rat hepatocytes. Proceedings of the National Academy of Sciences. 1978;75(10):5039–5042. Available from: https://www.pnas.org/doi/pdf/10.1073/pnas.75.10.5039
2. Wollert T. Autophagy. Current Biolology. 2019;29(14):671–678. Available from: https://doi.org/10.1016/j.cub.2019.06.014
3. Nakatogawa H, Ohsumi Y. Molecular mechanisms of autophagy in yeast. Tanpakushitsu Kakusan Koso. 2008;53(16):2099–2105.
4. Towers CG, Thorburn A. Autophagy in Cancer. Reference Module in Biomedical Sciences. Encyclopedia of Cancer (Third Edition). 2019;p. 112–121. Available from: http://dx.doi.org/10.1016/B978-0-12-801238-3.65812-9
5. Levine B, Kroemer G. Autophagy in the Pathogenesis of Disease. Cell. 2008;132(1):27–42. Available from: https://doi.org/10.1016/j.cell.2007.12.018
6. Wen X, Klionsky DJ. At a glance: A history of autophagy and cancer. Seminars in Cancer Biology. 2020;66:3–11. Available from: https://doi.org/10.1016/j.semcancer.2019.11.005
7. Huang F, Wang BRR, Wang YGR. Role of autophagy in tumorigenesis, metastasis, targeted therapy and drug resistance of hepatocellular carcinoma. World Journal of Gastroenterology. 2018;24(41):4643–4651. Available from: https://doi.org/10.3748/wjg.v24.i41.4643
8. Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of<i>Saccharomyces cerevisiae</i>. FEBS Letters. 1993;333(1-2):169–174. Available from: https://doi.org/10.1016/0014-5793(93)80398-e
9. Onodera J, Ohsumi Y. Autophagy Is Required for Maintenance of Amino Acid Levels and Protein Synthesis under Nitrogen Starvation. Journal of Biological Chemistry. 2005;280(36):31582–31586. Available from: https://doi.org/10.1074/jbc.m506736200
10. Filigheddu N, Gnocchi VF, Coscia M, Cappelli M, Porporato PE, Santiago TR, et al. Ghrelin and Des-Acyl Ghrelin Promote Differentiation and Fusion of C2C12 Skeletal Muscle Cells. Mol Biol Cell. 2007;18(3):986–994. Available from: https://doi.org/10.1091/mbc.e06-05-0402
11. Bergamini E. Autophagy: A cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically. Molecular Aspects of Medicine. 2006;27(5-6):403–410. Available from: https://doi.org/10.1016/j.mam.2006.08.001
12. Levine B, Klionsky DJ. Development by self-digestion: Molecular mechanisms and biological functions of autophagy. Dev Cell. 2004;6(4):463–477. Available from: https://doi.org/10.1016/s1534-5807(04)00099-1
13. Kim J, Kundu M, Viollet B, Guan KLL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nature Cell Biology. 2011;13(2):132–141. Available from: https://doi.org/10.1038/ncb2152
14. Nakamura S, Yoshimori T. New insights into autophagosome–lysosome fusion. Journal of Cell Science. 2017;130(7):1209–1225. Available from: https://doi.org/10.1242/jcs.196352
15. Kriegenburg F, Ungermann C, Reggiori F. Coordination of Autophagosome–Lysosome Fusion by Atg8 Family Members. Current Biology. 2018;28(8):R512–R518. Available from: https://doi.org/10.1016/j.cub.2018.02.034
16. Jaber N, Dou Z, Chen JSS, Catanzaro J, Jiang YPP, Ballou LM, et al. Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function. Proceedings of the National Academy of Sciences. 2012;109(6):2003–2008. Available from: https://doi.org/10.1073/pnas.1112848109
17. Piacentini M, Kroemer G. Dying to survive - apoptosis, necroptosis, autophagy as supreme experiments of nature. The International Journal of Developmental Biology. 2015;59(1-3):5–9. Available from: https://doi.org/10.1387/ijdb.150167mp
18. Ren JHH, He WSS, Nong L, Zhu QYY, Hu K, Zhang RGG, et al. Acquired Cisplatin Resistance in Human Lung Adenocarcinoma Cells Is Associated with Enhanced Autophagy. Cancer Biotherapy and Radiopharmaceuticals. 2010;25(1):75–80. Available from: https://doi.org/10.1089/cbr.2009.0701
19. Zappavigna S, Luce A, Vitale G, Merola N, Facchini S, Caraglia M. Autophagic cell death: A new frontier in cancer research. Advances in Bioscience and Biotechnology. 2013;04(02):250–262. Available from: http://dx.doi.org/10.4236/abb.2013.42034
20. Kroemer G, Mariño G, Levine B. Autophagy and the Integrated Stress Response. Molecular Cell. 2010;40(2):280–293. Available from: https://doi.org/10.1016/j.molcel.2010.09.023
21. Kocaturk NM, Akkoc Y, Kig C, Bayraktar O, Gozuacik D, Kutlu O. Autophagy as a molecular target for cancer treatment. European Journal of Pharmaceutical Sciences. 2019;134:116–137. Available from: https://doi.org/10.1016/j.ejps.2019.04.011
22. Cao Y, Luo Y, Zou J, Ouyang J, Cai Z, Zeng X, et al. Autophagy and its role in gastric cancer. Clinica Chimica Acta. 2019;489:10–20. Available from: https://doi.org/10.1016/j.cca.2018.11.028
23. Chen Y, Klionsky DJ. The regulation of autophagy – unanswered questions. Journal of Cell Science. 2011;124(2):161–170. Available from: https://doi.org/10.1242/jcs.064576
24. An H, Harper JW. Systematic analysis of ribophagy in human cells reveals bystander flux during selective autophagy. Nature Cell Biology. 2018;20(2):135–143. Available from: http://dx.doi.org/10.1038/s41556-017-0007-x
25. Feng Y, Backues SK, Baba M, Heo JMM, Harper JW, Klionsky DJ. Phosphorylation of Atg9 regulates movement to the phagophore assembly site and the rate of autophagosome formation. Autophagy. 2016;12(4):648–658. Available from: http://dx.doi.org/10.1080/15548627.2016.1157237
26. Papinski D, Kraft C. Atg1 kinase organizes autophagosome formation by phosphorylating Atg9. Autophagy. 2014;10(7):1338–1340. Available from: https://doi.org/10.4161%2Fauto.28971
27. Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N, et al. Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy. Cell. 2005;122(6):927–939. Available from: https://doi.org/10.1016/j.cell.2005.07.002
28. Mercer TJ, Gubas A, Tooze SA. A molecular perspective of mammalian autophagosome biogenesis. Journal of Biological Chemistry. 2018;293(15):5386–5395. Available from: https://doi.org/10.1074/jbc.r117.810366
29. Park JMM, Jung CH, Seo M, Otto NM, Grunwald D, Kim KH, et al. The ULK1 complex mediates MTORC1 signaling to the autophagy initiation machinery via binding and phosphorylating ATG14. Autophagy. 2016;12(3):547–564. Available from: http://dx.doi.org/10.1080/15548627.2016.1140293
30. Tsuboyama K, Koyama-Honda I, Sakamaki Y, Koike M, Morishita H, Mizushima N. The ATG conjugation systems are important for degradation of the inner autophagosomal membrane. Science. 2016;354(6315):1036–1041. Available from: https://doi.org/10.1126/science.aaf6136
31. Klionsky DJ, Schulman BA. Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins. Nature Structural & Molecular Biology. 2014;21(4):336–345. Available from: https://doi.org/10.1038%2Fnsmb.2787
32. Limpert AS, Lambert LJ, Bakas NA, Bata N, Brun SN, Shaw RJ, et al. Autophagy in Cancer: Regulation by Small Molecules. Trends in Pharmacological Sciences. 2018;39(12):1021–1032. Available from: https://doi.org/10.1016/j.tips.2018.10.004
33. Colasanti T, Vomero M, Barbati C, Finucci A, Conti F, Alessandri C, et al. Autophagy and Autoimmunity. Mosaic of Autoimmunity. 2019;p. 143–153. Available from: https://doi.org/10.1016/B978-0-12-814307-0.00016-5
34. Kriegenburg F, Ungermann C, Reggiori F. Coordination of Autophagosome–Lysosome Fusion by Atg8 Family Members. Current Biology. 2018;28(8):R512–R518. Available from: https://doi.org/10.1016/j.cub.2018.02.034
35. Jäger S, Bucci C, Tanida I, Ueno T, Kominami E, Saftig P. Role for Rab7 in maturation of late autophagic vacuoles. J Cell Sci. 2004;117(20):4837–4885. Available from: https://doi.org/10.1242/jcs.01370
36. Panda PK, Mukhopadhyay S, Das DN, Sinha N, Naik PP, Bhutia SK. Mechanism of autophagic regulation in carcinogenesis and cancer therapeutics. Seminars in Cell & Developmental Biology. 2015;39:43–55. Available from: http://dx.doi.org/10.1016/j.semcdb.2015.02.013
37. Liang XH, Jackson S, Seaman M, Brown K, Kempkes B, Hibshoosh H. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature. 1999;402(6762):672–678. Available from: https://doi.org/10.1038/45257
38. Wen L, Chen XZZ, Yang K, Chen ZXZ, Zhang B, Chen JPZ, et al. Prognostic Value of Cancer Stem Cell Marker CD133 Expression in Gastric Cancer: A Systematic Review. PLoS ONE. 2013;8(3):e59154. Available from: https://doi.org/10.1371%2Fjournal.pone.0059154
39. Galluzzi L, Pietrocola F, Pedro JMB, Amaravadi RK, Baehrecke EH, Cecconi F, et al. Autophagy in malignant transformation and cancer progression. The EMBO Journal. 2015;34(7):856–880. Available from: https://doi.org/10.15252/embj.201490784
40. Yu L, Alva A, Su H, Dutt P, Freundt E, Welsh S, et al. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science. 2004;304(5656):1500–1502. Available from: https://doi.org/10.1126/science.1096645
41. Ganley IG, Lam DH, Wang J, Ding X, Chen S, Jiang X. ULK1·ATG13·FIP200 Complex Mediates mTOR Signaling and Is Essential for Autophagy. Journal of Biological Chemistry. 2009;284(18):12297–12305. Available from: https://doi.org/10.1074/jbc.m900573200
42. Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, et al. The Crystal Structure of Atg3, an Autophagy-related Ubiquitin Carrier Protein (E2) Enzyme that Mediates Atg8 Lipidation. Journal of Biological Chemistry. 2007;282(11):8036–8043. Available from: https://doi.org/10.1074/jbc.m611473200
43. Ahlberg J, Glaumann H. Uptake-Microautophagy-and degradation of exogenous proteins by isolated rat liver lysosomes. Effects of pH, ATP, and inhibitors of proteolysis. Exp Mol Pathol. 1985;42(1):78–88. Available from: https://doi.org/10.1016/0014-4800(85)90020-6
44. Jiang H, Cheng D, Liu W, Peng J, Feng J. Protein kinase C inhibits autophagy and phosphorylates LC3. Biochemical and Biophysical Research Communications. 2010;395(4):471–476. Available from: http://dx.doi.org/10.1016/j.bbrc.2010.04.030
45. Duran A, Amanchy R, Linares JF, Joshi J, Abu-Baker S, Porollo A, et al. p62 Is a Key Regulator of Nutrient Sensing in the mTORC1 Pathway. Molecular Cell. 2011;44(1):134–146. Available from: http://dx.doi.org/10.1016/j.molcel.2011.06.038
46. Moscat J, Diaz-Meco MT. p62 at the Crossroads of Autophagy, Apoptosis, and Cancer. p62 at the Crossroads of Autophagy. 2009;137(6):1001–1004. Available from: https://doi.org/10.1016%2Fj.cell.2009.05.023
47. Chandrasekar T, Evans CP. Autophagy and urothelial carcinoma of the bladder: A review. Investigative and Clinical Urology. 2016;57(Suppl 1):S89–S97. Available from: https://doi.org/10.4111%2Ficu.2016.57.S1.S89
48. Egan D, Kim J, Shaw RJ, Guan K. The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR. Autophagy. 2011;7(6):643–644. Available from: https://doi.org/10.4161/auto.7.6.15123
49. Young ARJ, Narita M, Ferreira M, Kirschner K, Sadaie M, Darot JFJ, et al. Autophagy mediates the mitotic senescence transition. Genes & Development. 2009;23(7):798–803. Available from: https://doi.org/10.1101%2Fgad.519709
50. Chan EY. mTORC1 Phosphorylates the ULK1-mAtg13-FIP200 Autophagy Regulatory Complex. Science Signaling. 2009;2(84):13–19. Available from: https://doi.org/10.1126/scisignal.284pe51
51. Mokas S, Mills JR, Garreau C, Fournier MJ, Robert F, Arya P, et al. Uncoupling Stress Granule Assembly and Translation Initiation Inhibition. Molecular Biology of the Cell. 2009;20(11):2673–2683. Available from: https://doi.org/10.1091/mbc.e08-10-1061
52. Ronan B, Flamand O, Vescovi L, Dureuil C, Durand L, Fassy F, et al. A highly potent and selective Vps34 inhibitor alters vesicle trafficking and autophagy. Nature Chemical Biology. 2014;10(12):1013–1019. Available from: https://doi.org/10.1038/nchembio.1681
53. Dowdle WE, Nyfeler B, Nagel J, Elling RA, Liu S, Triantafellow E, et al. Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo. Nature Cell Biology. 2014;16(11):1069–1079. Available from: https://doi.org/10.1038/ncb3053
54. Takamura A, Komatsu M, Hara T, Sakamoto A, Kishi C, Waguri S, et al. Autophagy-deficient mice develop multiple liver tumors. Genes & Development. 2011;25(8):795–800. Available from: https://doi.org/10.1101/gad.2016211
55. Mariño G, Salvador-Montoliu N, Fueyo A, Knecht E, Mizushima N, López-Otín C. Withdrawal: Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3. Journal of Biological Chemistry. 2019;294(4):1435. Available from: https://doi.org/10.1074/jbc.w118.007329
56. Kashuba VI, Gizatullin RZ, Protopopov AI, Allikmets R, Korolev S, Li J, et al. NotI linking/jumping clones of human chromosome 3: mapping of the TFRC, RAB7 and HAUSP genes to regions rearranged in leukemia and deleted in solid tumors. FEBS Letters. 1997;419(2-3):181–185. Available from: https://doi.org/10.1016/s0014-5793(97)01449-x
57. Xu P, Das M, Reilly J, Davis RJ. JNK regulates FoxO-dependent autophagy in neurons. Genes & Development. 2011;25(4):310–322. Available from: https://doi.org/10.1101/gad.1984311
58. Pike LRG, Singleton DC, Buffa F, Abramczyk O, Phadwal K, Li JLL, et al. Transcriptional up-regulation of ULK1 by ATF4 contributes to cancer cell survival. Biochemical Journal. 2013;449(2):389–400. Available from: https://doi.org/10.1042/bj20120972
59. Cianfanelli V, Fuoco C, Lorente M, Salazar M, Quondamatteo F, Gherardini PF, et al. AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation. Nature Cell Biology. 2015;17(1):20–30. Available from: https://doi.org/10.1038/ncb3072
60. Chano T, Ikegawa S, Saito-Ohara F, Inazawa J, Mabuchi A, Saeki Y, et al. Isolation, characterization and mapping of the mouse and human RB1CC1 genes. Gene. 2002;291(1-2):29–34. Available from: https://doi.org/10.1016/s0378-1119(02)00585-1
61. Liang C, Lee JSS, Inn KSS, Gack MU, Li Q, Roberts EA, et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nature Cell Biology. 2008;10(7):776–787. Available from: https://doi.org/10.1038/ncb1740
62. Ahn CH, Jeong EG, Lee JW, Kim MS, Kim SH, Kim SS, et al. Expression of beclin-1, an autophagy-related protein, in gastric and colorectal cancers. APMIS. 2007;115(12):1344–1349. Available from: https://doi.org/10.1111/j.1600-0463.2007.00858.x
63. Appay V, Sauce D. Immune activation and inflammation in HIV-1 infection: causes and consequences. Journal of Pathology. 2008;214(2):231–241. Available from: https://doi.org/10.1002/path.2276
64. Lee EJJ, Tournier C. The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy. Autophagy. 2011;7(7):689–695. Available from: https://doi.org/10.4161%2Fauto.7.7.15450
65. Kundu M, Lindsten T, Yang CYY, Wu J, Zhao F, Zhang J, et al. Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood. 2008;112(4):1493–1502. Available from: https://doi.org/10.1182/blood-2008-02-137398
66. Chan EYW, Longatti A, Mcknight NC, Tooze SA. Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism. Molecular and Cellular Biology. 2009;29(1):157–171. Available from: https://doi.org/10.1128/mcb.01082-08
67. Mao T, Liang O. ULK1 Can Suppress or Promote Tumor Growth Under Different Conditions. In: Autophagy: Cancer, Other Pathologies, Inflammation, Immunity, Infection, and Aging (11). (Vol. 11, pp. 245-257) Elsevier Inc. 2017.
68. Chan EY, Tooze SA. Evolution of Atg1 function and regulation. Autophagy. 2009;5(6):758–765. Available from: https://doi.org/10.4161/auto.8709
69. Alers S, Löffler AS, Wesselborg S, Stork B. The incredible ULKs. Cell Communication and Signaling. 2012;10(1):7. Available from: https://doi.org/10.1186/1478-811x-10-7
70. Löffler AS, Alers S, Dieterle AM, Keppeler H, Franz-Wachtel M, Kundu M. Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. Autophagy. 2011;7(7):696–706. Available from: https://doi.org/10.4161/auto.7.7.15451
71. Kang R, Zeh HJ, Lotze MT, Tang D. The Beclin 1 network regulates autophagy and apoptosis. Cell Death & Differentiation. 2011;18(4):571–580. Available from: http://dx.doi.org/10.1038/cdd.2010.191
72. Mizushima N. The role of the Atg1/ULK1 complex in autophagy regulation. Current Opinion in Cell Biology. 2010;22(2):132–139. Available from: http://dx.doi.org/10.1016/j.ceb.2009.12.004
73. Wong PM, Puente C, Ganley IG, Jiang X. The ULK1 complex sensing nutrient signals for autophagy activation. Autophagy. 2013;9(2):124–137. Available from: https://doi.org/10.4161/auto.23323
74. Chan EYW, Kir S, Tooze SA. siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy. Journal of Biological Chemistry. 2007;282(35):25464–25474. Available from: https://doi.org/10.1074/jbc.m703663200
75. Wyant GA, Abu-Remaileh M, Wolfson RL, Chen WW, Freinkman E, Danai LV, et al. mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient. Cell. 2017;171(3):642–654. Available from: https://doi.org/10.1016/j.cell.2017.09.046
76. Nicklin P, Bergman P, Zhang B, Triantafellow E, Wang H, Nyfeler B, et al. Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy. Cell. 2009;136(3):521–534. Available from: http://dx.doi.org/10.1016/j.cell.2008.11.044
77. Zhang N, Yang X, Yuan F, Zhang L, Wang Y, Wang L, et al. Increased Amino Acid Uptake Supports Autophagy-Deficient Cell Survival upon Glutamine Deprivation. Cell Reports. 2018;23(10):3006–3020. Available from: https://doi.org/10.1016/j.celrep.2018.05.006
78. Huang J, Manning BD. A complex interplay between Akt, TSC2 and the two mTOR complexes. Biochemical Society Transactions. 2009;37(1):217–222. Available from: https://doi.org/10.1042/bst0370217
79. Long X, Lin Y, Ortiz-Vega S, Yonezawa K, Avruch J. Rheb Binds and Regulates the mTOR Kinase. Current Biology. 2005;15(8):702–713. Available from: https://doi.org/10.1016/j.cub.2005.02.053
80. Zhang Y, Gao X, Saucedo LJ, Ru B, Edgar BA, Pan D. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nature Cell Biology. 2003;5(6):578–581. Available from: https://doi.org/10.1038/ncb999
81. Hardie DG. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nature Reviews Molecular Cell Biology. 2007;8(10):774–785. Available from: https://doi.org/10.1038/nrm2249
82. Meley D, Bauvy C, Houben-Weerts JHPM, Dubbelhuis PF, Helmond MTJ, Codogno P, et al. AMP-activated Protein Kinase and the Regulation of Autophagic Proteolysis. Journal of Biological Chemistry. 2006;281(46):34870–34879. Available from: https://doi.org/10.1074/jbc.m605488200
83. Sodowski K, Cnota W, Czuba B, Borowski D, Wielgos M, Kaminski P. Blood flow in ductus venosus in early uncomplicated pregnancy. Neuroendocrinol Lett. 2007;28(5):713–719.
84. Gwinn DM, Shackelford DB, Egan DF, Mihaylova MM, Mery A, Vasquez DS, et al. AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint. Molecular Cell. 2008;30(2):214–226. Available from: https://doi.org/10.1016/j.molcel.2008.03.003
85. Bach M, Larance M, James DE, Ramm G. The serine/threonine kinase ULK1 is a target of multiple phosphorylation events. Biochemical Journal. 2011;440(2):283–291. Available from: https://doi.org/10.1042/bj20101894
86. Egan DF, Shackelford DB, Mihaylova MM, Gelino S, Kohnz RA, Mair W, et al. Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy. Science. 2011;331(6016):456–461. Available from: https://doi.org/10.1126/science.1196371
87. Lee JW, Park S, Takahashi Y, Wang HGG. The Association of AMPK with ULK1 Regulates Autophagy. PLoS ONE. 2010;5(11):e15394. Available from: https://doi.org/10.1371%2Fjournal.pone.0015394
88. Levine B, Abrams J. p53: The Janus of autophagy? Nature Cell Biology. 2008;10(6):637–639. Available from: https://doi.org/10.1038%2Fncb0608-637
89. Feng Z, Zhang H, Levine AJ, Jin S. The coordinate regulation of the p53 and mTOR pathways in cells. Proceedings of the National Academy of Sciences. 2005;102(23):8204–8209. Available from: https://doi.org/10.1073/pnas.0502857102
90. Feng Z, Hu W, Stanchina ED, Teresky AK, Jin S, Lowe SS, et al. The Regulation of AMPK β1, TSC2, and PTEN Expression by p53: Stress, Cell and Tissue Specificity, and the Role of These Gene Products in Modulating the IGF-1-AKT-mTOR Pathways. Cancer Research. 2007;67(7):3043–3053. Available from: https://doi.org/10.1158/0008-5472.can-06-4149
91. Budanov AV, Karin M. p53 Target Genes Sestrin1 and Sestrin2 Connect Genotoxic Stress and mTOR Signaling. Cell. 2009;134(3):451–460. Available from: https://doi.org/10.1016/j.cell.2008.06.028
92. Maiuri MC, Malik SA, Morselli E, Kepp O, Criollo A, Mouchel PLL, et al. Stimulation of autophagy by the p53 target gene Sestrin2. Cell Cycle. 2009;8(10):1571–1576. Available from: https://doi.org/10.4161/cc.8.10.8498
93. Crighton D, Wilkinson S, O&apos;prey J, Syed N, Smith P, Harrison PR, et al. DRAM, a p53-Induced Modulator of Autophagy, Is Critical for Apoptosis. Cell. 2006;126(1):121–134. Available from: https://doi.org/10.1016/j.cell.2006.05.034
94. Gao W, Shen Z, Shang L, Wang X. Upregulation of human autophagy-initiation kinase ULK1 by tumor suppressor p53 contributes to DNA-damage-induced cell death. Cell Death & Differentiation. 2011;18(10):1598–1607. Available from: http://dx.doi.org/10.1038/cdd.2011.33
95. Tasdemir E, Maiuri MC, Morselli E, Criollo A, D&apos;amelio M, Djavaheri-Mergny M, et al. A dual role of p53 in the control of autophagy. Autophagy. 2008;4(6):810–814. Available from: https://doi.org/10.4161/auto.6486
96. Tasdemir E, Maiuri MC, Galluzzi L, Vitale I, Djavaheri-Mergny M, D&apos;amelio M, et al. Regulation of autophagy by cytoplasmic p53. Nature Cell Biology. 2008;10(6):676–687. Available from: https://doi.org/10.1038/ncb1730
97. Laplante M, Sabatini DM. mTOR Signaling in Growth Control and Disease. Cell. 2012;149(2):274–293. Available from: http://dx.doi.org/10.1016/j.cell.2012.03.017
98. Petherick KJ, Conway OJL, Mpamhanga C, Osborne SA, Kamal A, Saxty B, et al. Pharmacological inhibition of ULK1 kinase blocks mammalian target of rapamycin (mTOR)-dependent autophagy. Journal of Biological Chemistry. 2015;290(48):11376–11383. Available from: https://doi.org/10.1074/jbc.c114.627778
99. Puente C, Hendrickson RC, Jiang X. Nutrient-regulated Phosphorylation of ATG13 Inhibits Starvation-induced Autophagy. Journal of Biological Chemistry. 2016;291(11):6026–6035. Available from: https://doi.org/10.1074%2Fjbc.M115.689646
100. Lazarus MB, Novotny CJ, Shokat KM. Structure of the Human Autophagy Initiating Kinase ULK1 in Complex with Potent Inhibitors. ACS Chemical Biology. 2015;10(1):257–261. Available from: https://doi.org/10.1021/cb500835z
101. Mack HID, Zheng B, Asara JM, Thomas SM. AMPK-dependent phosphorylation of ULK1 regulates ATG9 localization. Autophagy. 2012;8(8):1197–1214. Available from: https://doi.org/10.4161/auto.20586
102. Shang L, Chen S, Du F, Li S, Zhao L, Wang X. Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK. Proceedings of the National Academy of Sciences. 2011;108(12):4788–4793. Available from: https://doi.org/10.1073/pnas.1100844108
103. Mathew R, Karp CM, Beaudoin B, Vuong N, Chen G, Chen HY, et al. Autophagy Suppresses Tumorigenesis through Elimination of p62. Cell. 2009;137(6):1062–1075. Available from: http://dx.doi.org/10.1016/j.cell.2009.03.048
104. Qiu DMM, Wang GLL, Chen L, Xu YYY, He S, Cao XLL, et al. The expression of beclin-1, an autophagic gene, in hepatocellular carcinoma associated with clinical pathological and prognostic significance. BMC Cancer. 2014;14(1):1–13. Available from: https://doi.org/10.1186/1471-2407-14-327
105. Qu X, Yu J, Bhagat G, Furuya N, Hibshoosh H, Troxel A. Journal of Clinical Investigation. 2003;112(12):1809–1829. Available from: https://doi.org/10.1172/jci20039
106. Tang D, Kang R, Livesey KM, Cheh CWW, Farkas A, Loughran P, et al. Endogenous HMGB1 regulates autophagy. The Journal of Cell Biology. 2010;190(5):881–892. Available from: https://doi.org/10.1083%2Fjcb.200911078
107. Aryal P, Kim K, Park PHH, Ham S, Cho J, Song K. Baicalein induces autophagic cell death through AMPK/ULK1 activation and downregulation of mTORC1 complex components in human cancer cells. FEBS Journal. 2014;281(20):4644–4658. Available from: https://doi.org/10.1111/febs.12969
108. Egan DF, Chun MGH, Vamos M, Zou H, Rong J, Miller CJ, et al. Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates. Molecular Cell. 2015;59(2):285–297. Available from: http://dx.doi.org/10.1016/j.molcel.2015.05.031
109. Lazarus MB, Shokat KM. Discovery and structure of a new inhibitor scaffold of the autophagy initiating kinase ULK1. Bioorganic & Medicinal Chemistry. 2015;23(17):5483–5488. Available from: http://dx.doi.org/10.1016/j.bmc.2015.07.034
110. Wood SD, Grant W, Adrados I, Choi JY, Alburger JM, Duckett DR. In Silico HTS and Structure Based Optimization of Indazole-Derived ULK1 Inhibitors. ACS Med Chem Lett.. 2017;8:1258–1263. Available from: https://pubs.acs.org/doi/10.1021/acsmedchemlett.7b00344
111. Das CK, Banerjee I, Mandal M. Pro-survival autophagy: An emerging candidate of tumor progression through maintaining hallmarks of cancer. Seminars in Cancer Biology. 2020;66:59–74. Available from: https://doi.org/10.1016/j.semcancer.2019.08.020
112. Amaravadi R, Kimmelman AC, White E. Recent insights into the function of autophagy in cancer. Genes & Development. 2016;30(17):1913–1930. Available from: https://doi.org/10.1101/gad.287524.116
113. Newton PT. New insights into niclosamide action: autophagy activation in colorectal cancer. Biochemical Journal. 2019;476(5):779–781. Available from: https://doi.org/10.1042/bcj20190020
114. Hellmann MD, Paz-Ares L, Caro RB, Zurawski B, Kim SW, Costa EC, et al. Nivolumab plus Ipilimumab in Advanced Non–Small-Cell Lung Cancer. New England Journal of Medicine. 2019;381(21):2020–2031. Available from: https://doi.org/10.1056/nejmoa1910231
115. Hou J, Rao M, Zheng W, Fan J, Law BYK. Advances on Cell Autophagy and Its Potential Regulatory Factors in Renal Ischemia-Reperfusion Injury. DNA and Cell Biology. 2019;38(9):895–904. Available from: https://doi.org/10.1089/dna.2019.4767
116. Colecchia D, Dapporto F, Tronnolone S, Salvini L, Chiariello M. MAPK15 is part of the ULK complex and controls its activity to regulate early phases of the autophagic process. Journal of Biological Chemistry. 2018;293(41):15962–15976. Available from: https://doi.org/10.1074/jbc.ra118.002527
117. Huang YHH, Yang PMM, Chuah QYY, Lee YJJ, Hsieh YFF, Peng CWW, et al. Autophagy promotes radiation-induced senescence but inhibits bystander effects in human breast cancer cells. Autophagy. 2014;10(7):1212–1228. Available from: https://doi.org/10.4161%2Fauto.28772
118. Coppé J, Desprez P, Krtolica A, Campisi J. The Senescence-Associated Secretory Phenotype: The Dark Side of Tumor Suppression. Annual Review of Pathology. 2010;5:99–118. Available from: https://doi.org/10.1146%2Fannurev-pathol-121808-102144
119. Amaral C, Borges M, Melo S, Silva ETD, Correia-Da-Silva G, Teixeira N. Apoptosis and Autophagy in Breast Cancer Cells following Exemestane Treatment. PLoS ONE. 2012;7(8):e42398. Available from: https://doi.org/10.1371/journal.pone.0042398
120. Dragowska WH, Weppler SA, Wang JC, Wong LY, Kapanen AI, Rawji JS, et al. Induction of Autophagy Is an Early Response to Gefitinib and a Potential Therapeutic Target in Breast Cancer. PLoS ONE. 2013;8(10):e76503. Available from: https://doi.org/10.1371/journal.pone.0076503
121. Vazquez-Martin A, Oliveras-Ferraros C, Menendez JA. Autophagy Facilitates the Development of Breast Cancer Resistance to the Anti-HER2 Monoclonal Antibody Trastuzumab. PLoS ONE. 2009;4(7):e6251. Available from: https://doi.org/10.1371/journal.pone.0006251
122. Cufí S, Vazquez-Martin A, Oliveras-Ferraros C, Corominas-Faja B, Cuyàs E, López-Bonet E. The anti-malarial chloroquine overcomes Primary resistance and restores sensitivity to Trastuzumab in HER2-positive breast cancer. Sci Rep. 2013;3:1–13. Available from: https://doi.org/10.1038/srep02469
123. Shen M, Duan WMM, Wu MYY, Wang WJJ, Liu LU, Xu MDD, et al. Participation of autophagy in the cytotoxicity against breast cancer cells by cisplatin. Oncology Reports. 2015;34(1):359–367. Available from: https://doi.org/10.3892/or.2015.4005
124. Abedin MJ, Wang D, Mcdonnell MA, Lehmann U, Kelekar A. Autophagy delays apoptotic death in breast cancer cells following DNA damage. Cell Death & Differentiation. 2007;14(3):500–510. Available from: https://doi.org/10.1038/sj.cdd.4402039
125. Lefort S, Joffre C, Kieffer Y, Givel AMM, Bourachot B, Zago G, et al. Inhibition of autophagy as a new means of improving chemotherapy efficiency in high-LC3B triple-negative breast cancers. Autophagy. 2014;10(12):2122–2142. Available from: https://doi.org/10.4161%2F15548627.2014.981788
126. Wang C, Huo X, Wang L, Meng Q, Liu Z, Liu Q, et al. Dioscin strengthens the efficiency of adriamycin in MCF-7 and MCF-7/ADR cells through autophagy induction: More than just down-regulation of MDR1. Scientific Reports. 2016;6(1):1–12. Available from: https://doi.org/10.1038/srep28403
127. Lee YJ, Won AJ, Lee JJ, Jung JH, Yoon S, Lee BM, et al. Molecular Mechanism of SAHA on Regulation of Autophagic Cell Death in Tamoxifen-Resistant MCF-7 Breast Cancer Cells. International Journal of Medical Sciences. 2012;9(10):881–893. Available from: https://doi.org/10.7150/ijms.5011
128. Wu YHH, Hong CWW, Wang YCC, Huang WJJ, Yeh YLL, Wang BJC, et al. A novel histone deacetylase inhibitor TMU-35435 enhances etoposide cytotoxicity through the proteasomal degradation of DNA-PKcs in triple-negative breast cancer. Cancer Letters. 2017;400:79–88. Available from: http://dx.doi.org/10.1016/j.canlet.2017.04.023
129. Felzen V, Hiebel C, Koziollek-Drechsler I, Reißig S, Wolfrum U, Kögel D, et al. Estrogen receptor α regulates non-canonical autophagy that provides stress resistance to neuroblastoma and breast cancer cells and involves BAG3 function. Cell Death & Disease. 2015;6(7):e1812. Available from: https://doi.org/10.1038/cddis.2015.181
130. Cook KL, Clarke PAG, Parmar J, Hu R, Schwartz‐roberts JL, Abu‐asab M, et al. Knockdown of estrogen receptor‐α induces autophagy and inhibits antiestrogen‐mediated unfolded protein response activation, promoting ROS‐induced breast cancer cell death. The FASEB Journal. 2014;28(9):3891–3905. Available from: https://doi.org/10.1096/fj.13-247353
131. Vijayaraghavan S, Karakas C, Doostan I, Chen X, Bui T, Yi M, et al. CDK4/6 and autophagy inhibitors synergistically induce senescence in Rb positive cytoplasmic cyclin E negative cancers. Nature Communications. 2017;8(1):1–17. Available from: https://doi.org/10.1038/ncomms15916
132. Qadir MA, Kwok B, Dragowska WH, To KH, Le D, Bally MB, et al. Macroautophagy inhibition sensitizes tamoxifen-resistant breast cancer cells and enhances mitochondrial depolarization. Breast Cancer Research and Treatment. 2008;112(3):389–403. Available from: https://doi.org/10.1007/s10549-007-9873-4
133. Medina PD, Payré B, Boubekeur N, Bertrand-Michel J, Tercé F, Silvente-Poirot S, et al. Ligands of the antiestrogen-binding site induce active cell death and autophagy in human breast cancer cells through the modulation of cholesterol metabolism. Cell Death & Differentiation. 2009;16(10):1372–1384. Available from: https://doi.org/10.1038/cdd.2009.62
134. Amaral C, Varela C, Azevedo M, Silva ETD, Roleira FMF, Chen S, et al. Effects of steroidal aromatase inhibitors on sensitive and resistant breast cancer cells: Aromatase inhibition and autophagy. The Journal of Steroid Biochemistry and Molecular Biology. 2013;135(1):51–59. Available from: http://dx.doi.org/10.1016/j.jsbmb.2012.12.017
135. Ravanan P, Srikumar IF, Talwar P. Autophagy: The spotlight for cellular stress responses. Life Sciences. 2017;188:53–67. Available from: http://dx.doi.org/10.1016/j.lfs.2017.08.029
136. Picca A, Lezza A, Leeuwenburgh C, Pesce V, Calvani R, Landi F, et al. Fueling Inflamm-Aging through Mitochondrial Dysfunction: Mechanisms and Molecular Targets. International Journal of Molecular Sciences. 2017;18(5):933. Available from: https://doi.org/10.3390/ijms18050933
137. Chen P, Cescon M, Bonaldo P. Autophagy-mediated regulation of macrophages and its applications for cancer. Autophagy. 2014;10(2):192–200. Available from: https://doi.org/10.4161/auto.26927
138. Antunes F, Erustes AG, Costa AJ, Nascimento AC, Bincoletto C, Ureshino RP, et al. Autophagy and intermittent fasting: the connection for cancer therapy? Clinics. 2018;73(16):e814s. Available from: https://doi.org/10.6061%2Fclinics%2F2018%2Fe814s
139. Niekerk GV, Hattingh SM, Engelbrecht AMM. Enhanced Therapeutic Efficacy in Cancer Patients by Short-term Fasting: The Autophagy Connection. Frontiers in Oncology. 2016;6:1–7. Available from: https://doi.org/10.3389/fonc.2016.00242
140. Qiu L, Zhou G, Cao S. Targeted inhibition of ULK1 enhances daunorubicin sensitivity in acute myeloid leukemia. Life Sciences. 2020;243:117234. Available from: https://doi.org/10.1016/j.lfs.2019.117234
141. Lu J, Zhu L, Zheng LP, Cui Q, Zhu HH, Zhao H, et al. Overexpression of ULK1 Represents a Potential Diagnostic Marker for Clear Cell Renal Carcinoma and the Antitumor Effects of SBI-0206965. EBioMedicine. 2018;34:85–93. Available from: https://doi.org/10.1016/j.ebiom.2018.07.034
142. Tang F, Hu P, Yang Z, Xue C, Gong J, Sun S, et al. SBI0206965, a novel inhibitor of Ulk1, suppresses non-small cell lung cancer cell growth by modulating both autophagy and apoptosis pathways. Oncology Reports. 2017;37(6):3449–3458. Available from: https://doi.org/10.3892/or.2017.5635