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Volumn 8, Issue 2, 2018, Pages

P53-mediated molecular control of autophagy in tumor cells

Author keywords

Autophagy; Histone deacetylase inhibitor; MTOR; P53; Suberoylanilide hydroxamic acid; Tumor

Indexed keywords

DOXORUBICIN; HISTONE DEACETYLASE 1; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAMMALIAN TARGET OF RAPAMYCIN; PROTEIN P53; TUMOR SUPPRESSOR PROTEIN;

EID: 85044591563     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom8020014     Document Type: Review
Times cited : (137)

References (153)
  • 2
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • [CrossRef] [PubMed]
    • Yang, Z.; Klionsky, D.J. Mammalian autophagy: Core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 2010, 22, 124–131. [CrossRef] [PubMed]
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 3
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • [CrossRef] [PubMed]
    • Mizushima, N.; Komatsu, M. Autophagy: Renovation of cells and tissues. Cell 2011, 147, 728–741. [CrossRef] [PubMed]
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 4
    • 84859161154 scopus 로고    scopus 로고
    • Microautophagy: Lesser-known self-eating. Cell. Mol
    • [CrossRef] [PubMed]
    • Li, W.W.; Li, J.; Bao, J. Microautophagy: lesser-known self-eating. Cell. Mol. Life Sci. 2012, 69, 1125–1136. [CrossRef] [PubMed]
    • (2012) Life Sci , vol.69 , pp. 1125-1136
    • Li, W.W.1    Li, J.2    Bao, J.3
  • 5
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • [CrossRef] [PubMed]
    • Kaushik, S.; Cuervo, A.M. Chaperone-mediated autophagy: A unique way to enter the lysosome world. Trends Cell Biol. 2012, 22, 305–309. [CrossRef] [PubMed]
    • (2012) Trends Cell Biol , vol.22 , pp. 305-309
    • Kaushik, S.1    Cuervo, A.M.2
  • 6
    • 78650467974 scopus 로고    scopus 로고
    • Mechanisms of mitophagy
    • [CrossRef] [PubMed]
    • Youle, R.; Narendra, D. Mechanisms of mitophagy. Nat. Rev. Mol. Cell Biol. 2011, 12, 9–14. [CrossRef] [PubMed]
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 9-14
    • Youle, R.1    Narendra, D.2
  • 7
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • [CrossRef] [PubMed]
    • Levine, B.; Mizushima, N.; Virgin, H.W. Autophagy in immunity and inflammation. Nature 2011, 469, 323–335. [CrossRef] [PubMed]
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 8
    • 77950501014 scopus 로고    scopus 로고
    • MTOR regulation of autophagy
    • [CrossRef] [PubMed]
    • Jung, C.H.; Ro, S.-H.; Cao, J.; Otto, N.M.; Kim, D.-H. mTOR regulation of autophagy. FEBS Lett. 2010, 584, 1287–1295. [CrossRef] [PubMed]
    • (2010) FEBS Lett , vol.584 , pp. 1287-1295
    • Jung, C.H.1    Ro, S.-H.2    Cao, J.3    Otto, N.M.4    Kim, D.-H.5
  • 9
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • [CrossRef] [PubMed]
    • Takeshige, K.; Baba, M.; Tsuboi, S.; Noda, T.; Ohsumi, Y. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 1992, 119, 301–311. [CrossRef] [PubMed]
    • (1992) J. Cell Biol , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 10
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M.; Ohsumi, Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 1992, 333, 169–174. [CrossRef]
    • (1992) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 12
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • [CrossRef] [PubMed]
    • Harding, T.; Morano, K.; Scott, S.; Klionsky, D. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J. Cell Biol. 1995, 131, 591–602. [CrossRef] [PubMed]
    • (1995) J. Cell Biol , vol.131 , pp. 591-602
    • Harding, T.1    Morano, K.2    Scott, S.3    Klionsky, D.4
  • 13
    • 50249183899 scopus 로고    scopus 로고
    • Autophagy revisited: A conversation with Christian de Duve
    • [CrossRef] [PubMed]
    • Klionsky, D.J. Autophagy revisited: A conversation with Christian de Duve. Autophagy 2008, 4, 740–743. [CrossRef] [PubMed]
    • (2008) Autophagy , vol.4 , pp. 740-743
    • Klionsky, D.J.1
  • 14
    • 84865302358 scopus 로고    scopus 로고
    • Mechanisms and regulation of autophagosome formation
    • [CrossRef] [PubMed]
    • Kraft, C.; Martens, S. Mechanisms and regulation of autophagosome formation. Curr. Opin. Cell Biol. 2012, 24, 496–501. [CrossRef] [PubMed]
    • (2012) Curr. Opin. Cell Biol , vol.24 , pp. 496-501
    • Kraft, C.1    Martens, S.2
  • 15
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • [CrossRef] [PubMed]
    • Choi, A.M.; Ryter, S.W.; Levine, B. Autophagy in human health and disease. N. Engl. J. Med. 2013, 368, 651–662. [CrossRef] [PubMed]
    • (2013) N. Engl. J. Med. , vol.368 , pp. 651-662
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 16
    • 84894565195 scopus 로고    scopus 로고
    • Self consumption: The interplay between autophagy and apoptosis
    • [CrossRef] [PubMed]
    • Mariño, G.; Niso-Santano, M.; Baehrecke, E.H.; Kroemer, G. Self consumption: The interplay between autophagy and apoptosis. Nat. Rev. Mol. Cell Biol. 2014, 15, 81–94. [CrossRef] [PubMed]
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 81-94
    • Mariño, G.1    Niso-Santano, M.2    Baehrecke, E.H.3    Kroemer, G.4
  • 17
    • 50349098812 scopus 로고    scopus 로고
    • Involvement of protective autophagy in TRAIL resistance of apoptosis-defective tumor cells
    • [CrossRef] [PubMed]
    • Han, J.; Hou, W.; Goldstein, L.A.; Lu, C.; Stolz, D.B.; Yin, X.-M.; Rabinowich, H. Involvement of protective autophagy in TRAIL resistance of apoptosis-defective tumor cells. J. Biol. Chem. 2008, 283, 19665–19677. [CrossRef] [PubMed]
    • (2008) J. Biol. Chem. , vol.283 , pp. 19665-19677
    • Han, J.1    Hou, W.2    Goldstein, L.A.3    Lu, C.4    Stolz, D.B.5    Yin, X.-M.6    Rabinowich, H.7
  • 21
    • 84941218863 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce autophagy through FOXO1-dependent pathways
    • [CrossRef] [PubMed]
    • Zhang, J.; Ng, S.; Wang, J.; Zhou, J.; Tan, S.; Yang, N.; Lin, Q.; Xia, D.; Shen, H.; Zhang, J. et al. Histone deacetylase inhibitors induce autophagy through FOXO1-dependent pathways. Autophagy 2015, 11, 629–642. [CrossRef] [PubMed]
    • (2015) Autophagy , vol.11 , pp. 629-642
    • Zhang, J.1    Ng, S.2    Wang, J.3    Zhou, J.4    Tan, S.5    Yang, N.6    Lin, Q.7    Xia, D.8    Shen, H.9    Zhang, J.10
  • 22
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • [CrossRef] [PubMed]
    • He, C.; Klionsky, D.J. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 2009, 43, 67–93. [CrossRef] [PubMed]
    • (2009) Annu. Rev. Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 23
    • 77951649035 scopus 로고    scopus 로고
    • The role of autophagy in tumour development and cancer therapy
    • [CrossRef] [PubMed]
    • Rosenfeldt, M.T.; Ryan, K.M. The role of autophagy in tumour development and cancer therapy. Expert Rev. Mol. Med. 2009, 11, e36. [CrossRef] [PubMed]
    • (2009) Expert Rev. Mol. Med , vol.11
    • Rosenfeldt, M.T.1    Ryan, K.M.2
  • 24
    • 79953659370 scopus 로고    scopus 로고
    • Autophagy blockade enhances HDAC inhibitors’ pro-apoptotic: Effects potential implications for the treatment of a therapeutic-resistant malignancy
    • Lopez, G.; Torres, K.; Lev, D. Autophagy blockade enhances HDAC inhibitors’ pro-apoptotic: Effects potential implications for the treatment of a therapeutic-resistant malignancy. Autophagy 2011, 7, 40–41. [CrossRef]
    • (2011) Autophagy , vol.7 , pp. 40-41
    • Lopez, G.1    Torres, K.2    Lev, D.3
  • 26
    • 85009485546 scopus 로고    scopus 로고
    • Autophagosome Maturation and Fusion
    • [CrossRef] [PubMed]
    • Reggiori, F.; Ungermann, C. Autophagosome Maturation and Fusion. J. Mol. Biol. 2017, 429, 486–496. [CrossRef] [PubMed]
    • (2017) J. Mol. Biol , vol.429 , pp. 486-496
    • Reggiori, F.1    Ungermann, C.2
  • 27
    • 84855645313 scopus 로고    scopus 로고
    • Mechanisms of autophagosome biogenesis
    • [CrossRef] [PubMed]
    • Rubinsztein, D.C.; Shpilka, T.; Elazar, Z. Mechanisms of autophagosome biogenesis. Curr. Biol. 2012, 22, R29–R34. [CrossRef] [PubMed]
    • (2012) Curr. Biol , vol.22 , pp. R29-R34
    • Rubinsztein, D.C.1    Shpilka, T.2    Elazar, Z.3
  • 28
    • 84891748139 scopus 로고    scopus 로고
    • A current perspective of autophagosome biogenesis
    • [CrossRef] [PubMed]
    • Shibutani, S.; Yoshimori, T. A current perspective of autophagosome biogenesis. Cell Res. 2014, 24, 58–68. [CrossRef] [PubMed]
    • (2014) Cell Res , vol.24 , pp. 58-68
    • Shibutani, S.1    Yoshimori, T.2
  • 29
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • [CrossRef] [PubMed]
    • Mizushima, N.; Yoshimori, T.; Ohsumi, Y. The role of Atg proteins in autophagosome formation. Annu. Rev. Cell Dev. Biol. 2011, 27, 107–132. [CrossRef] [PubMed]
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 30
    • 85005769276 scopus 로고    scopus 로고
    • Emerging mechanisms in initiating and terminating autophagy
    • [CrossRef] [PubMed]
    • Antonioli, M.; Di Rienzo, M.; Piacentini, M.; Fimia, G. Emerging mechanisms in initiating and terminating autophagy. Trends Biochem. Sci. 2017, 42, 28–41. [CrossRef] [PubMed]
    • (2017) Trends Biochem. Sci , vol.42 , pp. 28-41
    • Antonioli, M.1    Di Rienzo, M.2    Piacentini, M.3    Fimia, G.4
  • 31
    • 84884820821 scopus 로고    scopus 로고
    • Autophagy regulation and its role in cancer
    • [CrossRef] [PubMed]
    • Lorin, S.; Hamaï, A.; Mehrpour, M.; Codogno, P. Autophagy regulation and its role in cancer. Semin. Cancer Biol. 2013, 23, 361–379. [CrossRef] [PubMed]
    • (2013) Semin. Cancer Biol. , vol.23 , pp. 361-379
    • Lorin, S.1    Hamaï, A.2    Mehrpour, M.3    Codogno, P.4
  • 33
    • 84857802958 scopus 로고    scopus 로고
    • Molecules and their functions in autophagy
    • [CrossRef] [PubMed]
    • Pyo, J.O.; Nah, J.; Jung, Y.K. Molecules and their functions in autophagy. Exp. Mol. Med. 2012, 44, 73–80. [CrossRef] [PubMed]
    • (2012) Exp. Mol. Med , vol.44 , pp. 73-80
    • Pyo, J.O.1    Nah, J.2    Jung, Y.K.3
  • 35
    • 85023764965 scopus 로고    scopus 로고
    • Regulation of autophagy through TORC1 and mTORC1
    • [CrossRef] [PubMed]
    • Noda, T. Regulation of autophagy through TORC1 and mTORC1. Biomolecules 2017, 7, 52. [CrossRef] [PubMed]
    • (2017) Biomolecules , vol.7 , pp. 52
    • Noda, T.1
  • 36
    • 34250894388 scopus 로고    scopus 로고
    • BH3-only proteins and BH3 mimetics induce autophagy by competively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L)
    • [CrossRef] [PubMed]
    • Maiuri, M.; Criollo, A.; Tasdemir, E.; Vicencio, J.M.; Tajeddine, N.; Hickmann, J.; Geneste, O.; Kroemer, G. BH3-only proteins and BH3 mimetics induce autophagy by competively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L). Autophagy 2007, 3, 374–376. [CrossRef] [PubMed]
    • (2007) Autophagy , vol.3 , pp. 374-376
    • Maiuri, M.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.M.4    Tajeddine, N.5    Hickmann, J.6    Geneste, O.7    Kroemer, G.8
  • 37
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • [CrossRef] [PubMed]
    • Liang, X.H.; Jackson, S.; Seaman, M.; Brown, K.; Kempkes, B.; Hibshoosh, H.; Levine, B. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 1999, 402, 672–676. [CrossRef] [PubMed]
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3    Brown, K.4    Kempkes, B.5    Hibshoosh, H.6    Levine, B.7
  • 38
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim, D.; Sarbassov, D.; Ali, S.; King, J.; Latek, R.; Erdjument-Bromage, H.; Tempst, P.; Sabatini, D. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 2002, 110, 163–175. [CrossRef]
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.1    Sarbassov, D.2    Ali, S.3    King, J.4    Latek, R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.8
  • 40
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • [CrossRef] [PubMed]
    • Zoncu, R.; Efeyan, A.; Sabatini, D. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell Biol. 2011, 12, 21–35. [CrossRef] [PubMed]
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.3
  • 41
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • [CrossRef] [PubMed]
    • Kim, J.; Kundu, M.; Viollet, B.; Kun-Liang, G. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 2011, 13, 132–141. [CrossRef] [PubMed]
    • (2011) Nat. Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Kun-Liang, G.4
  • 42
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
    • [CrossRef] [PubMed]
    • Jung, C.H.; Jun, C.B.; Ro, S.; Kim, Y.; Otto, N.M.; Cao, J.; Kundu, M.; Kim, D. ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery. Mol. Biol. Cell. 2009, 20, 1992–2003. [CrossRef] [PubMed]
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.3    Kim, Y.4    Otto, N.M.5    Cao, J.6    Kundu, M.7    Kim, D.8
  • 43
    • 66449083078 scopus 로고    scopus 로고
    • ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. Autophagy
    • [CrossRef] [PubMed]
    • Ganley, I.G.; Lam, D.H.; Wang, J.; Ding, X.; Chen, S.; Jiang, X. ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. Autophagy. J. Biol. Chem. 2009, 284, 12297–12305. [CrossRef] [PubMed]
    • (2009) J. Biol. Chem , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam, D.H.2    Wang, J.3    Ding, X.4    Chen, S.5    Jiang, X.6
  • 44
    • 52649137098 scopus 로고    scopus 로고
    • A Gene Signature-Based Approach Identifies mTOR as a Regulator of p73
    • [CrossRef] [PubMed]
    • Rosenbluth, J.M.; Mays, D.J.; Pino, M.F.; Tang, L.J.; Pietenpol, J.A. A Gene Signature-Based Approach Identifies mTOR as a Regulator of p73. Mol. Cell. Biol. 2008, 28, 5951–5964. [CrossRef] [PubMed]
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5951-5964
    • Rosenbluth, J.M.1    Mays, D.J.2    Pino, M.F.3    Tang, L.J.4    Pietenpol, J.A.5
  • 45
    • 85028717398 scopus 로고    scopus 로고
    • MTOR regulates autophagy-associated genes downstream of p73
    • Rosenbluth, J.M.; Pietenpol, J.A. mTOR regulates autophagy-associated genes downstream of p73. Autophagy 2009, 2, 1–7. [CrossRef]
    • (2009) Autophagy , vol.2 , pp. 1-7
    • Rosenbluth, J.M.1    Pietenpol, J.A.2
  • 46
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • [CrossRef] [PubMed]
    • He, C.; Levine, B. The Beclin 1 interactome. Curr. Opin. Cell Biol. 2010, 22, 140–149. [CrossRef] [PubMed]
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 140-149
    • He, C.1    Levine, B.2
  • 47
    • 76349098949 scopus 로고    scopus 로고
    • Crosstalk between apoptosis and autophagy within the Beclin 1 interactome
    • [CrossRef] [PubMed]
    • Maiuri, M.; Criollo, A.; Kroemer, G. Crosstalk between apoptosis and autophagy within the Beclin 1 interactome. EMBO J. 2010, 29, 515–516. [CrossRef] [PubMed]
    • (2010) EMBO J , vol.29 , pp. 515-516
    • Maiuri, M.1    Criollo, A.2    Kroemer, G.3
  • 48
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • [CrossRef] [PubMed]
    • Zalckvar, E.; Berissi, H.; Mizrachy, L.; Idelchuk, Y.; Koren, I.; Eisenstein, M.; Sabanay, H.; Pinkas-Kramarski, R.; Kimchi, A. DAP-kinase mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep. 2009, 10, 285–292. [CrossRef] [PubMed]
    • (2009) EMBO Rep , vol.10 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3    Idelchuk, Y.4    Koren, I.5    Eisenstein, M.6    Sabanay, H.7    Pinkas-Kramarski, R.8    Kimchi, A.9
  • 49
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and ATG12 ubiquitin-like conjugation systems in macroautophagy. ´Protein modifications: Beyond the usual suspects´ review series
    • [CrossRef] [PubMed]
    • Geng, J.; Klionsky, D.J. The Atg8 and ATG12 ubiquitin-like conjugation systems in macroautophagy. ´Protein modifications: Beyond the usual suspects´ review series. EMBO Rep. 2008, 9, 859–864. [CrossRef] [PubMed]
    • (2008) EMBO Rep , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 50
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy
    • [CrossRef] [PubMed]
    • Mizushima, N.; Sugita, H.; Yoshimori, T.; Ohsumi, Y. A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy. J. Biol. Chem. 1998, 273, 33889–33892. [CrossRef] [PubMed]
    • (1998) J. Biol. Chem , vol.273 , pp. 33889-33892
    • Mizushima, N.1    Sugita, H.2    Yoshimori, T.3    Ohsumi, Y.4
  • 51
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • [CrossRef] [PubMed]
    • Polson, H.E.; de Lartigue, J.; Ridgen, D.J.; Reedijk, M.; Urbe, S.; Clague, M.J.; Tooze, S.A. Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation. Autophagy 2010, 6, 506–522. [CrossRef] [PubMed]
    • (2010) Autophagy , vol.6 , pp. 506-522
    • Polson, H.E.1    De Lartigue, J.2    Ridgen, D.J.3    Reedijk, M.4    Urbe, S.5    Clague, M.J.6    Tooze, S.A.7
  • 52
    • 33846240526 scopus 로고    scopus 로고
    • Sequestosome 1/p62—More than just a scaffold
    • [CrossRef] [PubMed]
    • Seibenhener, M.L.; Geetha, T.; Wooten, M.W. Sequestosome 1/p62—More than just a scaffold. FEBS Lett. 2007, 581, 175–179. [CrossRef] [PubMed]
    • (2007) FEBS Lett , vol.581 , pp. 175-179
    • Seibenhener, M.L.1    Geetha, T.2    Wooten, M.W.3
  • 56
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • [CrossRef] [PubMed]
    • Xie, Z.; Klionsky, D.J. Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 2007, 9, 1102–1109. [CrossRef] [PubMed]
    • (2007) Nat. Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 57
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
    • [CrossRef] [PubMed]
    • Simonsen, A.; Tooze, S. Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes. J. Cell Biol. 2009, 186, 773–782. [CrossRef] [PubMed]
    • (2009) J. Cell Biol , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.2
  • 58
    • 33947534030 scopus 로고    scopus 로고
    • P53 in health and disease
    • [CrossRef] [PubMed]
    • Vousden, K.H.; Lane, D.P. p53 in health and disease. Nat. Rev. Mol. Cell Biol. 2007, 8, 275–283. [CrossRef] [PubMed]
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 275-283
    • Vousden, K.H.1    Lane, D.P.2
  • 59
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • [CrossRef] [PubMed]
    • Toledo, F.; Wahl, G.M. Regulating the p53 pathway: In vitro hypotheses, in vivo veritas. Nat. Rev. Cancer 2006, 6, 909–923. [CrossRef] [PubMed]
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 60
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks, C.L.; Gu, W. Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation. Curr. Opin. Cell Biol. 2003, 15, 164–171. [CrossRef]
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 61
    • 80053064491 scopus 로고    scopus 로고
    • The impact of acetylation and deacetylation on the p53 pathway
    • [CrossRef] [PubMed]
    • Brooks, C.L.; Gu, W. The impact of acetylation and deacetylation on the p53 pathway. Protein Cell 2011, 2, 456–462. [CrossRef] [PubMed]
    • (2011) Protein Cell , vol.2 , pp. 456-462
    • Brooks, C.L.1    Gu, W.2
  • 62
    • 70349459599 scopus 로고    scopus 로고
    • P53 and metabolism
    • [CrossRef] [PubMed]
    • Vousden, K.; Ryan, K. p53 and metabolism. Nat. Rev. Cancer 2009, 9, 691–700. [CrossRef] [PubMed]
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 691-700
    • Vousden, K.1    Ryan, K.2
  • 63
    • 74949138902 scopus 로고    scopus 로고
    • Defective autophagy control by the p53 rheostat in cancer
    • [CrossRef] [PubMed]
    • Galluzzi, L.; Morselli, E.; Kepp, O.; Maiuri, M.C.; Kroemer, G. Defective autophagy control by the p53 rheostat in cancer. Cell Cycle 2010, 9, 250–255. [CrossRef] [PubMed]
    • (2010) Cell Cycle , vol.9 , pp. 250-255
    • Galluzzi, L.1    Morselli, E.2    Kepp, O.3    Maiuri, M.C.4    Kroemer, G.5
  • 65
    • 77955345508 scopus 로고    scopus 로고
    • P53 At a Glance
    • [CrossRef] [PubMed]
    • Brady, C.A.; Attardi, L.D. P53 At a Glance. J. Cell Sci. 2010, 123, 2527–2532. [CrossRef] [PubMed]
    • (2010) J. Cell Sci , vol.123 , pp. 2527-2532
    • Brady, C.A.1    Attardi, L.D.2
  • 66
    • 0025784539 scopus 로고
    • Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6
    • [CrossRef] [PubMed]
    • Yonish-Rouach, E.; Resnitzky, D.; Lotem, J.; Sachs, L.; Kimchi, A.; Oren, M. Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6. Nature 1991, 352, 345–347. [CrossRef] [PubMed]
    • (1991) Nature , vol.352 , pp. 345-347
    • Yonish-Rouach, E.1    Resnitzky, D.2    Lotem, J.3    Sachs, L.4    Kimchi, A.5    Oren, M.6
  • 67
    • 77952163120 scopus 로고    scopus 로고
    • P53 regulation of the IGF-1/AKT/mTOR pathways and the endosomal compartment
    • [CrossRef] [PubMed]
    • Feng, Z. p53 regulation of the IGF-1/AKT/mTOR pathways and the endosomal compartment. Cold Spring Harb. Perspect. Biol. 2010, 2, 1–10. [CrossRef] [PubMed]
    • (2010) Cold Spring Harb. Perspect. Biol , vol.2 , pp. 1-10
    • Feng, Z.1
  • 68
    • 0035929650 scopus 로고    scopus 로고
    • The Tumor Suppressor PTEN Positively Regulates Macroautophagy by Inhibiting the Phosphatidylinositol 3-Kinase/Protein Kinase B Pathway
    • [CrossRef] [PubMed]
    • Arico, S.; Petiot, A.; Bauvy, C.; Dubbelhuis, P.F.; Meijer, A.J.; Codogno, P.; Ogier-Denis, E. The Tumor Suppressor PTEN Positively Regulates Macroautophagy by Inhibiting the Phosphatidylinositol 3-Kinase/Protein Kinase B Pathway. J. Biol. Chem. 2001, 276, 35243–35246. [CrossRef] [PubMed]
    • (2001) J. Biol. Chem , vol.276 , pp. 35243-35246
    • Arico, S.1    Petiot, A.2    Bauvy, C.3    Dubbelhuis, P.F.4    Meijer, A.J.5    Codogno, P.6    Ogier-Denis, E.7
  • 69
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and mTOR pathways in cells
    • [CrossRef] [PubMed]
    • Feng, Z.; Zhang, H.; Levine, A.J.; Jin, S. The coordinate regulation of the p53 and mTOR pathways in cells. Proc. Natl. Acad. Sci. USA 2005, 102, 8204–8209. [CrossRef] [PubMed]
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3    Jin, S.4
  • 71
    • 48449101433 scopus 로고    scopus 로고
    • P53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling
    • [CrossRef] [PubMed]
    • Budanov, A.V.; Karin, M. p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. Cell 2008, 134, 451–460. [CrossRef] [PubMed]
    • (2008) Cell , vol.134 , pp. 451-460
    • Budanov, A.V.1    Karin, M.2
  • 73
    • 33846260837 scopus 로고    scopus 로고
    • DRAM links autophagy to p53 and programmed cell death
    • [CrossRef] [PubMed]
    • Crighton, D.; Wilkinson, S.; Ryan, K. DRAM links autophagy to p53 and programmed cell death. Autophagy 2007, 3, 72–74. [CrossRef] [PubMed]
    • (2007) Autophagy , vol.3 , pp. 72-74
    • Crighton, D.1    Wilkinson, S.2    Ryan, K.3
  • 74
    • 84880729896 scopus 로고    scopus 로고
    • Kirshenbaum, L.A. P53 mediates autophagy and cell death by a mechanism contingent on Bnip3
    • [CrossRef] [PubMed]
    • Wang, E.Y.; Gang, H.; Aviv, Y.; Dhingra, R.; Margulets, V.; Kirshenbaum, L.A. p53 mediates autophagy and cell death by a mechanism contingent on Bnip3. Hypertension 2013, 62, 70–77. [CrossRef] [PubMed]
    • (2013) Hypertension , vol.62 , pp. 70-77
    • Wang, E.Y.1    Gang, H.2    Aviv, Y.3    Dhingra, R.4    Margulets, V.5
  • 75
    • 67650745428 scopus 로고    scopus 로고
    • PUMA and Bax-induced autophagy contributes to apoptosis
    • [CrossRef] [PubMed]
    • Yee, K.S.; Wilkinson, S.; James, J.; Ryan, K.M.; Vousden, K.H. PUMA and Bax-induced autophagy contributes to apoptosis. Cell Death Differ. 2010, 16, 1135–1145. [CrossRef] [PubMed]
    • (2010) Cell Death Differ , vol.16 , pp. 1135-1145
    • Yee, K.S.1    Wilkinson, S.2    James, J.3    Ryan, K.M.4    Vousden, K.H.5
  • 77
    • 59149096565 scopus 로고    scopus 로고
    • ARF induces autophagy by virtue of interaction with Bcl-xl
    • [CrossRef] [PubMed]
    • Pimkina, J.; Humbey, O.; Zilfou, J.; Jarnik, M.; Murphy, M. ARF induces autophagy by virtue of interaction with Bcl-xl. J. Biol. Chem. 2009, 284, 2803–2810. [CrossRef] [PubMed]
    • (2009) J. Biol. Chem , vol.284 , pp. 2803-2810
    • Pimkina, J.1    Humbey, O.2    Zilfou, J.3    Jarnik, M.4    Murphy, M.5
  • 78
    • 67650270918 scopus 로고    scopus 로고
    • Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL
    • [CrossRef] [PubMed]
    • Zalckvar, E.; Berissi, H.; Eisenstein, M.; A. K. Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL. Autophagy 2009, 5, 720–722. [CrossRef] [PubMed]
    • (2009) Autophagy , vol.5 , pp. 720-722
    • Zalckvar, E.1    Berissi, H.2    Eisenstein, M.3
  • 79
    • 43949145220 scopus 로고    scopus 로고
    • DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing
    • [CrossRef] [PubMed]
    • Harrison, B.; Kraus, M.; Burch, L.; Stevens, C.; Craig, A.; Gordon-Weeks, P.; Hupp, T. DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing. J. Biol. Chem. 2008, 283, 9999–10014. [CrossRef] [PubMed]
    • (2008) J. Biol. Chem , vol.283 , pp. 9999-10014
    • Harrison, B.1    Kraus, M.2    Burch, L.3    Stevens, C.4    Craig, A.5    Gordon-Weeks, P.6    Hupp, T.7
  • 80
    • 84877311822 scopus 로고    scopus 로고
    • Global genomic profiling reveals an extensive p53-regulated autophagy program contributing to key p53 responses
    • [CrossRef] [PubMed]
    • Kenzelmann Broz, D.; Mello, S.S.; Bieging, K.T.; Jiang, D.; Dusek, R.L.; Brady, C.A.; Sidow, A.; Attardi, L.D. Global genomic profiling reveals an extensive p53-regulated autophagy program contributing to key p53 responses. Genes Dev. 2013, 27, 1016–1031. [CrossRef] [PubMed]
    • (2013) Genes Dev , vol.27 , pp. 1016-1031
    • Kenzelmann Broz, D.1    Mello, S.S.2    Bieging, K.T.3    Jiang, D.4    Dusek, R.L.5    Brady, C.A.6    Sidow, A.7    Attardi, L.D.8
  • 84
    • 84911376426 scopus 로고    scopus 로고
    • Beclin-1—p53 interaction is crucial for cell fate determination in embryonal carcinoma cells
    • [CrossRef] [PubMed]
    • Tripathi, R.; Ash, D.; Shaha, C. Beclin-1—p53 interaction is crucial for cell fate determination in embryonal carcinoma cells. J. Cell Mol. Med. 2014, 18, 2275–2286. [CrossRef] [PubMed]
    • (2014) J. Cell Mol. Med , vol.18 , pp. 2275-2286
    • Tripathi, R.1    Ash, D.2    Shaha, C.3
  • 85
    • 80053501671 scopus 로고    scopus 로고
    • Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13
    • [CrossRef] [PubMed]
    • Liu, J.; Xia, H.; Kim, M.; Xu, L.; Li, Y.; Zhang, L.; Cai, Y.; Norberg, H.V.; Zhang, T.; Furuya, T. et al. Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13. Cell 2011, 147, 223–234. [CrossRef] [PubMed]
    • (2011) Cell , vol.147 , pp. 223-234
    • Liu, J.1    Xia, H.2    Kim, M.3    Xu, L.4    Li, Y.5    Zhang, L.6    Cai, Y.7    Norberg, H.V.8    Zhang, T.9    Furuya, T.10
  • 86
    • 77953621745 scopus 로고    scopus 로고
    • P53 and ARF: Unexpected players in autophagy
    • [CrossRef] [PubMed]
    • Balaburski, G.M.; Hontz, R.D.; Murphy, M.E. P53 and ARF: Unexpected players in autophagy. Trends Cell Biol. 2010, 20, 363–369. [CrossRef] [PubMed]
    • (2010) Trends Cell Biol , vol.20 , pp. 363-369
    • Balaburski, G.M.1    Hontz, R.D.2    Murphy, M.E.3
  • 87
    • 33646523798 scopus 로고    scopus 로고
    • A Short Mitochondrial Form of p19ARF Induces Autophagy and Caspase-Independent Cell Death
    • [CrossRef] [PubMed]
    • Reef, S.; Zalckvar, E.; Shifman, O.; Bialik, S.; Sabanay, H.; Oren, M.; Kimchi, A. A Short Mitochondrial Form of p19ARF Induces Autophagy and Caspase-Independent Cell Death. Mol. Cell 2006, 22, 463–475. [CrossRef] [PubMed]
    • (2006) Mol. Cell , vol.22 , pp. 463-475
    • Reef, S.1    Zalckvar, E.2    Shifman, O.3    Bialik, S.4    Sabanay, H.5    Oren, M.6    Kimchi, A.7
  • 88
    • 39049144417 scopus 로고    scopus 로고
    • P53-dependent and p53-independent activation of autophagy by ARF
    • [CrossRef] [PubMed]
    • Abida, W.M.; Gu, W. p53-dependent and p53-independent activation of autophagy by ARF. Cancer Res. 2008, 68, 352–357. [CrossRef] [PubMed]
    • (2008) Cancer Res , vol.68 , pp. 352-357
    • Abida, W.M.1    Gu, W.2
  • 89
    • 84885611579 scopus 로고    scopus 로고
    • A conserved domain in exon 2 coding for the human and murine ARF tumor suppressor protein is required for autophagy induction
    • [CrossRef] [PubMed]
    • Budina-Kolomets, A.; Hontz, R.D.; Pimkina, J.; Murphy, M.E. A conserved domain in exon 2 coding for the human and murine ARF tumor suppressor protein is required for autophagy induction. Autophagy 2013, 9, 1553–1565. [CrossRef] [PubMed]
    • (2013) Autophagy , vol.9 , pp. 1553-1565
    • Budina-Kolomets, A.1    Hontz, R.D.2    Pimkina, J.3    Murphy, M.E.4
  • 90
    • 42049120932 scopus 로고    scopus 로고
    • Small mitochondrial ARF (SmARF) is located in both the nucleus and cytoplasm, induces cell death, and activates p53 in mouse fibroblasts
    • [CrossRef] [PubMed]
    • Ueda, Y.; Koya, T.; Yoneda-Kato, N.; Kato, J.Y. Small mitochondrial ARF (smARF) is located in both the nucleus and cytoplasm, induces cell death, and activates p53 in mouse fibroblasts. FEBS Lett. 2008, 582, 1459–1464. [CrossRef] [PubMed]
    • (2008) FEBS Lett , vol.582 , pp. 1459-1464
    • Ueda, Y.1    Koya, T.2    Yoneda-Kato, N.3    Kato, J.Y.4
  • 91
    • 65949083750 scopus 로고    scopus 로고
    • Cytoplasmic functions of the tumour suppressor p53
    • [CrossRef] [PubMed]
    • Green, D.R.; Kroemer, G. Cytoplasmic functions of the tumour suppressor p53. Nature 2009, 458, 1127–1130. [CrossRef] [PubMed]
    • (2009) Nature , vol.458 , pp. 1127-1130
    • Green, D.R.1    Kroemer, G.2
  • 92
    • 84905108850 scopus 로고    scopus 로고
    • The cytoplasmic side of p53´s oncosuppressive activities
    • [CrossRef] [PubMed]
    • Comel, A.; Sorrentino, G.; Capaci, V.; Del Sal, G. The cytoplasmic side of p53´s oncosuppressive activities. FEBS Lett. 2014, 588, 2600–2609. [CrossRef] [PubMed]
    • (2014) FEBS Lett , vol.588 , pp. 2600-2609
    • Comel, A.1    Sorrentino, G.2    Capaci, V.3    Del Sal, G.4
  • 94
    • 70350575440 scopus 로고    scopus 로고
    • Modulation of intracellular ROS levels by TIGAR controls autophagy
    • [CrossRef] [PubMed]
    • Bensaad, K.; Cheung, E.C.; Vousden, K.H. Modulation of intracellular ROS levels by TIGAR controls autophagy. EMBO J. 2009, 28, 3015–3026. [CrossRef] [PubMed]
    • (2009) EMBO J , vol.28 , pp. 3015-3026
    • Bensaad, K.1    Cheung, E.C.2    Vousden, K.H.3
  • 96
    • 84871830221 scopus 로고    scopus 로고
    • P53 Mutations in Cancer
    • [CrossRef] [PubMed]
    • Muller, P.A.J.; Vousden, K.H. P53 Mutations in Cancer. Nat. Cell Biol. 2013, 15, 2–8. [CrossRef] [PubMed]
    • (2013) Nat. Cell Biol , vol.15 , pp. 2-8
    • Muller, P.A.J.1    Vousden, K.H.2
  • 97
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell´s response to p53
    • [CrossRef] [PubMed]
    • Vousden, K.H.; Lu, X. Live or let die: the cell´s response to p53. Nat. Rev. Cancer 2002, 2, 594–604. [CrossRef] [PubMed]
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 99
    • 84922391998 scopus 로고    scopus 로고
    • Transcriptional regulation bymutant p53 and oncogenesis
    • [CrossRef] [PubMed]
    • Santoro, R.; Strano, S.; Blandino, G. Transcriptional regulation bymutant p53 and oncogenesis. Subcell. Biochem. 2014, 85, 91–103. [CrossRef] [PubMed]
    • (2014) Subcell. Biochem , vol.85 , pp. 91-103
    • Santoro, R.1    Strano, S.2    Blandino, G.3
  • 100
    • 84866740163 scopus 로고    scopus 로고
    • Alterations of TP53 are associated with a poor outcome for patients with hepatocellular carcinoma: Evidence from a systematic review and metaanalysis
    • [CrossRef] [PubMed]
    • Liu, J.; Ma, Q.; Zhang, M.; Wang, X.; Zhang, D.; Li, W.; Wang, F.; Wu, E. Alterations of TP53 are associated with a poor outcome for patients with hepatocellular carcinoma: evidence from a systematic review and metaanalysis. Eur. J. Cancer 2012, 48, 2328–2338. [CrossRef] [PubMed]
    • (2012) Eur. J. Cancer , vol.48 , pp. 2328-2338
    • Liu, J.1    Ma, Q.2    Zhang, M.3    Wang, X.4    Zhang, D.5    Li, W.6    Wang, F.7    Wu, E.8
  • 101
    • 84998850009 scopus 로고    scopus 로고
    • Molecular interplay between mutant p53 proteins and autophagy in cancer cells
    • [CrossRef] [PubMed]
    • Cordani, M.; Butera, G.; Pacchiana, R.; Donadelli, M. Molecular interplay between mutant p53 proteins and autophagy in cancer cells. Biochim. Biophys. Acta Rev. Cancer 2017, 1867, 19–28. [CrossRef] [PubMed]
    • (2017) Biochim. Biophys. Acta Rev. Cancer , vol.1867 , pp. 19-28
    • Cordani, M.1    Butera, G.2    Pacchiana, R.3    Donadelli, M.4
  • 102
    • 84985006578 scopus 로고    scopus 로고
    • Molecular mechanism leading to SAHA-induced autophagy in tumor cells: Evidence for a p53-dependent pathway
    • [CrossRef] [PubMed]
    • Fröhlich, L.F.; Mrakovcic, M.; Smole, C.; Zatloukal, K. Molecular mechanism leading to SAHA-induced autophagy in tumor cells: evidence for a p53-dependent pathway. Cancer Cell Int. 2016, 16. [CrossRef] [PubMed]
    • (2016) Cancer Cell Int , pp. 16
    • Fröhlich, L.F.1    Mrakovcic, M.2    Smole, C.3    Zatloukal, K.4
  • 105
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • [CrossRef] [PubMed]
    • Yue, Z.; Jin, S.; Yang, C.; Levine, A.J.; Heintz, N. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl. Acad. Sci. USA 2003, 100, 15077–15082. [CrossRef] [PubMed]
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 106
    • 84877283682 scopus 로고    scopus 로고
    • The family that eats together stays together: New p53 family transcriptional targets in autophagy
    • [CrossRef] [PubMed]
    • Napoli, M.; Flores, E.R. The family that eats together stays together: New p53 family transcriptional targets in autophagy. Genes Dev. 2013, 27, 971–974. [CrossRef] [PubMed]
    • (2013) Genes Dev , vol.27 , pp. 971-974
    • Napoli, M.1    Flores, E.R.2
  • 107
    • 36048958965 scopus 로고    scopus 로고
    • Histone Deacetylase Inhibitors: Overview and Perspectives
    • [CrossRef] [PubMed]
    • Dokmanovic, M.; Clarke, C.; Marks, P.A. Histone Deacetylase Inhibitors: Overview and Perspectives. Mol. Cancer Res. 2007, 5, 981–989. [CrossRef] [PubMed]
    • (2007) Mol. Cancer Res , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 108
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • [CrossRef] [PubMed]
    • Bolden, J.; Peart, M.; Johnstone, R. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 2006, 5, 769–784. [CrossRef] [PubMed]
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.1    Peart, M.2    Johnstone, R.3
  • 109
    • 84903581670 scopus 로고    scopus 로고
    • Targeting Histone Deacetylases for Cancer Therapy: From Molecular Mechanisms to Clinical Implications
    • [CrossRef] [PubMed]
    • Li, Z.; Zhu, W.-G. Targeting Histone Deacetylases for Cancer Therapy: From Molecular Mechanisms to Clinical Implications. Int. J. Biol. Sci. 2014, 10, 757–770. [CrossRef] [PubMed]
    • (2014) Int. J. Biol. Sci , vol.10 , pp. 757-770
    • Li, Z.1    Zhu, W.-G.2
  • 110
    • 1442330508 scopus 로고    scopus 로고
    • Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo
    • Luo, J.; Li, M.; Tang, Y.; Laszkowska, M.; Roeder, R.G.; Gu, W. Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo. Proc. Natl. Acad. Sci. USA 2003, 101, 2259–2264. [CrossRef]
    • (2003) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2259-2264
    • Luo, J.1    Li, M.2    Tang, Y.3    Laszkowska, M.4    Roeder, R.G.5    Gu, W.6
  • 111
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • [CrossRef] [PubMed]
    • Bali, P.; Pranpat, M.; Bradner, J.; Balasis, M.; Fiskus, W.; Guo, F.; Rocha, K.; Kumaraswamy, S.; Boyapalle, S.; Atadja, P. et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 2005, 280, 26729–26734. [CrossRef] [PubMed]
    • (2005) J. Biol. Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10
  • 112
    • 84966604775 scopus 로고    scopus 로고
    • How do tumor cells respond to HDAC inhibition?
    • [CrossRef] [PubMed]
    • Newbold, A.; Falkenberg, K.J.; Prince, H.M.; Johnstone, R.W. How do tumor cells respond to HDAC inhibition? FEBS J. 2016, 283, 4032–4046. [CrossRef] [PubMed]
    • (2016) FEBS J , vol.283 , pp. 4032-4046
    • Newbold, A.1    Falkenberg, K.J.2    Prince, H.M.3    Johnstone, R.W.4
  • 113
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA binding domain regulates apoptosis induction. Mol
    • [CrossRef] [PubMed]
    • Sykes, S.M.; Mellert, H.S.; Holbert, M.A.; Li, K.; Lane, W.S.; Mcmahon, S.B. Acetylation of the p53 DNA binding domain regulates apoptosis induction. Mol. Cell 2007, 24, 841–851. [CrossRef] [PubMed]
    • (2007) Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Lane, W.S.5    McMahon, S.B.6
  • 114
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-Dependent Acetylation of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis
    • [CrossRef] [PubMed]
    • Tang, Y.; Luo, J.; Zhang, W. Tip60-Dependent Acetylation of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis. Mol. Cell 2006, 24, 827–839. [CrossRef] [PubMed]
    • (2006) Mol. Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3
  • 115
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases
    • Barlev, N.A.; Liu, L.; Chehab, N.H.; Mansfield, K.; Harris, K.G.; Halazonetis, T.D.; Berger, S.L. Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases. Mol. Cell 2001, 8, 1243–1254. [CrossRef]
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfield, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 117
    • 35648968035 scopus 로고    scopus 로고
    • An Acetylation Switch in p53 Mediates Holo-TFIID Recruitment
    • [CrossRef] [PubMed]
    • Li, A.G.; Piluso, L.G.; Cai, X.; Gadd, B.J.; Ladurner, A.G.; Liu, X. An Acetylation Switch in p53 Mediates Holo-TFIID Recruitment. Mol. Cell 2007, 28, 408–421. [CrossRef] [PubMed]
    • (2007) Mol. Cell , vol.28 , pp. 408-421
    • Li, A.G.1    Piluso, L.G.2    Cai, X.3    Gadd, B.J.4    Ladurner, A.G.5    Liu, X.6
  • 118
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W.; Roeder, R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997, 90, 595–606. [CrossRef]
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 119
    • 33645230001 scopus 로고    scopus 로고
    • Acetylation of p53 at Lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21Waf1/Cip1
    • [CrossRef] [PubMed]
    • Zhao, Y.; Lu, S.; Wu, L.; Chai, G.; Wang, H.; Chen, Y.; Sun, J.; Yu, Y.; Zhou, W.; Zheng, Q. et al. Acetylation of p53 at Lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21Waf1/Cip1. Mol. Cell Biol. 2006, 26, 2782–2790. [CrossRef] [PubMed]
    • (2006) Mol. Cell Biol , vol.26 , pp. 2782-2790
    • Zhao, Y.1    Lu, S.2    Wu, L.3    Chai, G.4    Wang, H.5    Chen, Y.6    Sun, J.7    Yu, Y.8    Zhou, W.9    Zheng, Q.10
  • 120
    • 84910019636 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and cell death
    • [CrossRef] [PubMed]
    • Zhang, J.; Zhong, Q. Histone deacetylase inhibitors and cell death. Cell. Mol. Life Sci. 2014, 71, 3885–3901. [CrossRef] [PubMed]
    • (2014) Cell. Mol. Life Sci , vol.71 , pp. 3885-3901
    • Zhang, J.1    Zhong, Q.2
  • 121
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato, R.; Almenara, J.; Dai, Y.; Grant, S. Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol. Cancer Ther. 2003, 2, 1273–1284. [PubMed]
    • (2003) Mol. Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.1    Almenara, J.2    Dai, Y.3    Grant, S.4
  • 122
    • 67349285731 scopus 로고    scopus 로고
    • Enhancing the apoptotic and therapeutic effects of HDAC inhibitors
    • [CrossRef] [PubMed]
    • Frew, A.J.; Johnstone, R.W.; Bolden, J.E. Enhancing the apoptotic and therapeutic effects of HDAC inhibitors. Cancer Lett. 2009, 280, 125–133. [CrossRef] [PubMed]
    • (2009) Cancer Lett , vol.280 , pp. 125-133
    • Frew, A.J.1    Johnstone, R.W.2    Bolden, J.E.3
  • 123
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • [CrossRef] [PubMed]
    • Shao, Y.; Gao, Z.; Marks, P.A.; Jiang, X. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc. Natl. Acad. Sci. USA 2004, 101, 18030–18035. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 124
    • 57149105528 scopus 로고    scopus 로고
    • Induces caspase-independent, autophagic cell death of endometrial stromal sarcoma cells by influencing the mTOR pathway
    • [CrossRef] [PubMed]
    • Hrzenjak, A.; Kremser, M.; Strohmeier, B.; Moinfar, F.; Zatloukal, K.; Denk, H. SAHA induces caspase-independent, autophagic cell death of endometrial stromal sarcoma cells by influencing the mTOR pathway. J. Pathol. 2008, 216, 495–504. [CrossRef] [PubMed]
    • (2008) J. Pathol , vol.216 , pp. 495-504
    • Hrzenjak, A.1    Kremser, M.2    Strohmeier, B.3    Moinfar, F.4    Zatloukal, K.5    Denk, H.6
  • 126
    • 84860135029 scopus 로고    scopus 로고
    • Role of autophagy in histone deacetylase inhibitor-induced apoptotic and nonapoptotic cell death
    • [CrossRef] [PubMed]
    • Gammoh, N.; Lam, D.; Puente, C.; Ganley, I.; Marks, P.A.; Jiang, X. Role of autophagy in histone deacetylase inhibitor-induced apoptotic and nonapoptotic cell death. Proc. Natl. Acad. Sci. USA 2012, 109, 6561–6565. [CrossRef] [PubMed]
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6561-6565
    • Gammoh, N.1    Lam, D.2    Puente, C.3    Ganley, I.4    Marks, P.A.5    Jiang, X.6
  • 127
    • 84978006453 scopus 로고    scopus 로고
    • HDAC family members intertwined in the regulation of autophagy: A druggable vulnerability in aggressive tumor entities
    • [CrossRef] [PubMed]
    • Koeneke, E.; Witt, O.; Oehme, I. HDAC family members intertwined in the regulation of autophagy: A druggable vulnerability in aggressive tumor entities. Cells 2015, 4, 135–168. [CrossRef] [PubMed]
    • (2015) Cells , vol.4 , pp. 135-168
    • Koeneke, E.1    Witt, O.2    Oehme, I.3
  • 128
    • 45949083938 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) induces apoptosis or autophagy-associated cell death in chondrosarcoma cell lines
    • Yamamoto, S.; Tanaka, K.; Sakimura, R.; Okada, T.; Nakamura, T.; Li, Y.; Takasaki, M.; Nakabeppu, Y.; Iwamoto, Y. Suberoylanilide hydroxamic acid (SAHA) induces apoptosis or autophagy-associated cell death in chondrosarcoma cell lines. Anticancer Res. 2008, 28, 1585–1591. [PubMed]
    • (2008) Anticancer Res , vol.28 , pp. 1585-1591
    • Yamamoto, S.1    Tanaka, K.2    Sakimura, R.3    Okada, T.4    Nakamura, T.5    Li, Y.6    Takasaki, M.7    Nakabeppu, Y.8    Iwamoto, Y.9
  • 130
    • 36248982150 scopus 로고    scopus 로고
    • Autophagy induced by suberoylanilide hydroxamic acid in Hela S3 cells involves inhibition of protein kinase B and up-regulation of Beclin 1
    • [CrossRef] [PubMed]
    • Cao, Q.; Yu, C.; Xue, R.; Hsueh, W.; Pan, P.; Chen, Z.; Wang, S.; McNutt, M.; Gu, J. Autophagy induced by suberoylanilide hydroxamic acid in Hela S3 cells involves inhibition of protein kinase B and up-regulation of Beclin 1. Int. J. Biochem. Cell Biol. 2008, 40, 272–283. [CrossRef] [PubMed]
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 272-283
    • Cao, Q.1    Yu, C.2    Xue, R.3    Hsueh, W.4    Pan, P.5    Chen, Z.6    Wang, S.7    McNutt, M.8    Gu, J.9
  • 131
    • 78649299438 scopus 로고    scopus 로고
    • Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma
    • [CrossRef] [PubMed]
    • Liu, Y.-L.; Yang, P.-M.; Shun, C.-T.; Wu, M.-S.; Weng, J.-R.; Chen, C.-C. Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma. Autophagy 2010, 6, 1057–1065. [CrossRef] [PubMed]
    • (2010) Autophagy , vol.6 , pp. 1057-1065
    • Liu, Y.-L.1    Yang, P.-M.2    Shun, C.-T.3    Wu, M.-S.4    Weng, J.-R.5    Chen, C.-C.6
  • 133
    • 77955884095 scopus 로고    scopus 로고
    • Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells
    • [CrossRef] [PubMed]
    • Li, J.; Liu, R.; Lei, Y.; Wang, K.; Lau, Q.C.; Xie, N.; Zhou, S.; Nie, C.; Chen, L.; Wei, Y. et al. Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells. Autophagy 2010, 6, 711–724. [CrossRef] [PubMed]
    • (2010) Autophagy , vol.6 , pp. 711-724
    • Li, J.1    Liu, R.2    Lei, Y.3    Wang, K.4    Lau, Q.C.5    Xie, N.6    Zhou, S.7    Nie, C.8    Chen, L.9    Wei, Y.10
  • 135
    • 84885639981 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) causes tumor growth slowdown and triggers autophagy in glioblastoma stem cells
    • [CrossRef] [PubMed]
    • Chiao, M.; Cheng, W.; Yang, Y.; Shen, C.; Chiao, M.; Cheng, W.; Yang, Y.; Shen, C.; Ko, J. Suberoylanilide hydroxamic acid (SAHA) causes tumor growth slowdown and triggers autophagy in glioblastoma stem cells. Autophagy 2013, 9, 1509–1526. [CrossRef] [PubMed]
    • (2013) Autophagy , vol.9 , pp. 1509-1526
    • Chiao, M.1    Cheng, W.2    Yang, Y.3    Shen, C.4    Chiao, M.5    Cheng, W.6    Yang, Y.7    Shen, C.8    Ko, J.9
  • 136
    • 34347394714 scopus 로고    scopus 로고
    • Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl—Mediated drug resistance
    • [CrossRef] [PubMed]
    • Carew, J.S.; Nawrocki, S.T.; Kahue, C.N.; Zhang, H.; Yang, C.; Chung, L.; Houghton, J.A.; Huang, P.; Giles, F.J.; Cleveland, J.L. Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl—Mediated drug resistance. Blood 2007, 110, 313–323. [CrossRef] [PubMed]
    • (2007) Blood , vol.110 , pp. 313-323
    • Carew, J.S.1    Nawrocki, S.T.2    Kahue, C.N.3    Zhang, H.4    Yang, C.5    Chung, L.6    Houghton, J.A.7    Huang, P.8    Giles, F.J.9    Cleveland, J.L.10
  • 137
    • 33749572938 scopus 로고    scopus 로고
    • Denk, H. Valproate inhibiton of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells
    • [CrossRef] [PubMed]
    • Hrzenjak, A.; Moinfar, F.; Kremser, M.; Strohmeier, B.; Staber, P.; Zatloukal, K.; Denk, H. Valproate inhibiton of histone deacetylase 2 affects differentiation and decreases proliferation of endometrial stromal sarcoma cells. Mol. Cancer Ther. 2006, 5, 2203–2210. [CrossRef] [PubMed]
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2203-2210
    • Hrzenjak, A.1    Moinfar, F.2    Kremser, M.3    Strohmeier, B.4    Staber, P.5    Zatloukal, K.6
  • 138
    • 77951237809 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor vorinostat suppresses the growth of uterine sarcomas in vitro and in vivo
    • [CrossRef] [PubMed]
    • Hrzenjak, A.; Moinfar, F.; Kremser, M.-L.; Strohmeier, B.; Petru, E.; Zatloukal, K.; Denk, H. Histone deacetylase inhibitor vorinostat suppresses the growth of uterine sarcomas in vitro and in vivo. Mol. Cancer 2010, 9. [CrossRef] [PubMed]
    • (2010) Mol. Cancer , pp. 9
    • Hrzenjak, A.1    Moinfar, F.2    Kremser, M.-L.3    Strohmeier, B.4    Petru, E.5    Zatloukal, K.6    Denk, H.7
  • 139
    • 84897564727 scopus 로고    scopus 로고
    • Epigenetic silencing of apoptosis-inducing gene expression can be efficiently overcome by combined SAHA and TRAIL treatment in uterine sarcoma cells
    • [CrossRef] [PubMed]
    • Fröhlich, L.F.; Mrakovcic, M.; Smole, C.; Lahiri, P.; Zatloukal, K. Epigenetic silencing of apoptosis-inducing gene expression can be efficiently overcome by combined SAHA and TRAIL treatment in uterine sarcoma cells. PLoS ONE 2014, 9, e91558. [CrossRef] [PubMed]
    • (2014) Plos ONE , vol.9
    • Fröhlich, L.F.1    Mrakovcic, M.2    Smole, C.3    Lahiri, P.4    Zatloukal, K.5
  • 140
    • 78649833334 scopus 로고    scopus 로고
    • P53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation
    • [CrossRef] [PubMed]
    • Scherz-Shouval, R.; Weidberg, H.; Gonen, C.; Wilder, S.; Elazar, Z.; Oren, M. p53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation. Proc. Natl. Acad. Sci. USA 2010, 107, 18511–18516. [CrossRef] [PubMed]
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18511-18516
    • Scherz-Shouval, R.1    Weidberg, H.2    Gonen, C.3    Wilder, S.4    Elazar, Z.5    Oren, M.6
  • 141
    • 85028732285 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor-induced autophagy in tumor cells: Implications for p53
    • Mrakovcic, M.; Kleinheinz, J.; Fröhlich, L.F. Histone deacetylase inhibitor-induced autophagy in tumor cells: Implications for p53. Int. J. Mol. Sci. 2017, 18, 1883. [CrossRef]
    • (2017) Int. J. Mol. Sci , vol.18 , pp. 1883
    • Mrakovcic, M.1    Kleinheinz, J.2    Fröhlich, L.F.3
  • 142
    • 85028718290 scopus 로고    scopus 로고
    • Mutational and Epimutational Analysis of Cell Death- Resistant Tumor Cells: Clues to Molecular Carcinogenesis and Cancer Therapy
    • Mrakovcic, M.; Fröhlich, L.F. Mutational and Epimutational Analysis of Cell Death- Resistant Tumor Cells: Clues to Molecular Carcinogenesis and Cancer Therapy. Ann. Mutagen. 2017, 1, 1–2.
    • (2017) Ann. Mutagen , vol.1 , pp. 1-2
    • Mrakovcic, M.1    Fröhlich, L.F.2
  • 143
    • 38749130035 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce in human hepatoma HepG2 cells acetylation of p53 and histones in correlation with apoptotic effects
    • [CrossRef] [PubMed]
    • Carlisi, D.; Vassallo, B.; Lauricella, M.; Emanuele, S.; D’Anneo, A.; Di Leonardo, E.; Di Fazio, P.; Vento, R.; Tesoriere, G. Histone deacetylase inhibitors induce in human hepatoma HepG2 cells acetylation of p53 and histones in correlation with apoptotic effects. Int. J. Oncol. 2008, 32, 177–184. [CrossRef] [PubMed]
    • (2008) Int. J. Oncol. , vol.32 , pp. 177-184
    • Carlisi, D.1    Vassallo, B.2    Lauricella, M.3    Emanuele, S.4    D’Anneo, A.5    Di Leonardo, E.6    Di Fazio, P.7    Vento, R.8    Tesoriere, G.9
  • 144
    • 85007480781 scopus 로고    scopus 로고
    • Anticancer effects of a new SIRT inhibitor, MHY2256, against human breast cancer MCF-7 cells via regulation of MDM2-p53 binding
    • [CrossRef] [PubMed]
    • Park, E.Y.; Woo, Y.; Kim, S.J.; Kim, D.H.; Lee, E.K.; De, U.; Kim, K.S.; Lee, J.; Jung, J.H.; Ha, K.T. et al. Anticancer effects of a new SIRT inhibitor, MHY2256, against human breast cancer MCF-7 cells via regulation of MDM2-p53 binding. Int. J. Biol. Sci. 2016, 12, 1555–1567. [CrossRef] [PubMed]
    • (2016) Int. J. Biol. Sci , vol.12 , pp. 1555-1567
    • Park, E.Y.1    Woo, Y.2    Kim, S.J.3    Kim, D.H.4    Lee, E.K.5    De, U.6    Kim, K.S.7    Lee, J.8    Jung, J.H.9    Ha, K.T.10
  • 147
    • 69349094578 scopus 로고    scopus 로고
    • Role and regulation of autophagy in cancer
    • [CrossRef] [PubMed]
    • Chen, N.; Karantza-Wadsworth, V. Role and regulation of autophagy in cancer. Biochim. Biophys. Acta Mol. Cell Res. 2009, 1793, 1516–1523. [CrossRef] [PubMed]
    • (2009) Biochim. Biophys. Acta Mol. Cell Res , vol.1793 , pp. 1516-1523
    • Chen, N.1    Karantza-Wadsworth, V.2
  • 148
    • 84988905857 scopus 로고    scopus 로고
    • Recent insights into the function of autophagy in cancer
    • [CrossRef] [PubMed]
    • Amaravadi, R.; Kimmelman, A.C.; White, E. Recent insights into the function of autophagy in cancer. Genes Dev. 2016, 30, 1913–1930. [CrossRef] [PubMed]
    • (2016) Genes Dev , vol.30 , pp. 1913-1930
    • Amaravadi, R.1    Kimmelman, A.C.2    White, E.3
  • 149
    • 77951232212 scopus 로고    scopus 로고
    • Cytoprotective roles for autophagy
    • [CrossRef] [PubMed]
    • Moreau, K.; Luo, S.; Rubinsztein, D.C. Cytoprotective roles for autophagy. Curr. Opin. Cell Biol. 2010, 22, 206–211. [CrossRef] [PubMed]
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 206-211
    • Moreau, K.1    Luo, S.2    Rubinsztein, D.C.3
  • 151
    • 84920415711 scopus 로고    scopus 로고
    • The role for autophagy in cancer
    • [CrossRef] [PubMed]
    • White, E. The role for autophagy in cancer. J. Clin. Investig. 2015, 125, 42–46. [CrossRef] [PubMed]
    • (2015) J. Clin. Investig , vol.125 , pp. 42-46
    • White, E.1
  • 153
    • 85019709546 scopus 로고    scopus 로고
    • Pharmacological modulation of autophagy: Therapeutic potential and persisting obstacles
    • [CrossRef] [PubMed]
    • Galluzzi, L.; Bravo-San Pedro, J.M.; Levine, B.; Green, D.R.; Kroemer, G. Pharmacological modulation of autophagy: Therapeutic potential and persisting obstacles. Nat. Rev. Drug Discov. 2017, 16, 487–511. [CrossRef] [PubMed]
    • (2017) Nat. Rev. Drug Discov , vol.16 , pp. 487-511
    • Galluzzi, L.1    Bravo-San Pedro, J.M.2    Levine, B.3    Green, D.R.4    Kroemer, G.5


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