메뉴 건너뛰기




Volumn 414, Issue 2, 2011, Pages 277-281

Cell death pathology: Cross-talk with autophagy and its clinical implications

Author keywords

Apoptosis; Autophagy; Cancer; P53; Programmed cell death

Indexed keywords

BECLIN 1; CASPASE; CASPASE 3; CASPASE 7; CASPASE 8; CYTOCHROME C; DEATH RECEPTOR; OBATOCLAX; PEMETREXED; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BCL 2; PROTEIN BCL XL; SORAFENIB; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; VINCRISTINE;

EID: 80054839348     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.09.080     Document Type: Short Survey
Times cited : (72)

References (81)
  • 1
    • 57649149333 scopus 로고    scopus 로고
    • Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009
    • Kroemer G., Galluzzi L., Vandenabeele P., et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ. 2009, 16:3-11.
    • (2009) Cell Death Differ. , vol.16 , pp. 3-11
    • Kroemer, G.1    Galluzzi, L.2    Vandenabeele, P.3
  • 2
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S., Tassa A., Qu X., et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005, 122:922-939.
    • (2005) Cell , vol.122 , pp. 922-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3
  • 4
    • 78349308821 scopus 로고    scopus 로고
    • Negative regulation of autophagy
    • Liang C. Negative regulation of autophagy. Cell Death Differ. 2010, 17:1807-1815.
    • (2010) Cell Death Differ. , vol.17 , pp. 1807-1815
    • Liang, C.1
  • 5
    • 67549139899 scopus 로고    scopus 로고
    • Toll-like receptors in control of immunological autophagy
    • Delgado M.A., Deretic V. Toll-like receptors in control of immunological autophagy. Cell Death Differ. 2009, 16:976-983.
    • (2009) Cell Death Differ. , vol.16 , pp. 976-983
    • Delgado, M.A.1    Deretic, V.2
  • 6
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: how does the end begin?
    • Noda T., Fujita N., Yoshimori T. The late stages of autophagy: how does the end begin?. Cell Death Differ. 2009, 16:984-990.
    • (2009) Cell Death Differ. , vol.16 , pp. 984-990
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 7
    • 67549139908 scopus 로고    scopus 로고
    • Vesicular trafficking and autophagosome formation
    • Longatti A., Tooze S.A. Vesicular trafficking and autophagosome formation. Cell Death Differ. 2009, 16:956-965.
    • (2009) Cell Death Differ. , vol.16 , pp. 956-965
    • Longatti, A.1    Tooze, S.A.2
  • 8
    • 67549142261 scopus 로고    scopus 로고
    • Life and death partners: apoptosis, autophagy and the cross-talk between them
    • Eisenberg-Lerner A., Bialik S., Simon H.U. Life and death partners: apoptosis, autophagy and the cross-talk between them. Cell Death Differ. 2009, 16:966-975.
    • (2009) Cell Death Differ. , vol.16 , pp. 966-975
    • Eisenberg-Lerner, A.1    Bialik, S.2    Simon, H.U.3
  • 9
    • 57649234905 scopus 로고    scopus 로고
    • Autophagy genes and ageing
    • Vellai T. Autophagy genes and ageing. Cell Death Differ. 2009, 16:94-102.
    • (2009) Cell Death Differ. , vol.16 , pp. 94-102
    • Vellai, T.1
  • 10
    • 57649228468 scopus 로고    scopus 로고
    • Autophagy and cell death in model organisms
    • Kourtis N., Tavernarakis N. Autophagy and cell death in model organisms. Cell Death Differ. 2009, 16:21-30.
    • (2009) Cell Death Differ. , vol.16 , pp. 21-30
    • Kourtis, N.1    Tavernarakis, N.2
  • 11
    • 57649184088 scopus 로고    scopus 로고
    • Control of autophagy by oncogenes and tumor suppressor genes
    • Maiuri M.C., Tasdemir E., Criollo A., et al. Control of autophagy by oncogenes and tumor suppressor genes. Cell Death Differ. 2009, 16:87-93.
    • (2009) Cell Death Differ. , vol.16 , pp. 87-93
    • Maiuri, M.C.1    Tasdemir, E.2    Criollo, A.3
  • 12
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang X.H., Jackson S., Seaman M., et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 1999, 402:672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3
  • 13
    • 67549096696 scopus 로고    scopus 로고
    • Bif-1/endophilin B1: a candidate for crescent driving force in autophagy
    • Takahashi Y., Meyerkord C.L., Wang H.G. Bif-1/endophilin B1: a candidate for crescent driving force in autophagy. Cell Death Differ. 2009, 16:947-955.
    • (2009) Cell Death Differ. , vol.16 , pp. 947-955
    • Takahashi, Y.1    Meyerkord, C.L.2    Wang, H.G.3
  • 14
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
    • Zhang J., Ney P.A. Role of BNIP3 and NIX in cell death, autophagy, and mitophagy. Cell Death Differ. 2009, 16:939-946.
    • (2009) Cell Death Differ. , vol.16 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 15
    • 62849105988 scopus 로고    scopus 로고
    • The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death
    • Burton T.R., Gibson S.B. The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death. Cell Death Differ. 2009, 16:515-523.
    • (2009) Cell Death Differ. , vol.16 , pp. 515-523
    • Burton, T.R.1    Gibson, S.B.2
  • 16
    • 34248998801 scopus 로고    scopus 로고
    • Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1
    • Maiuri M.C., Le Toumelin G., Criollo A., et al. Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1. EMBO J. 2007, 26:2527-2539.
    • (2007) EMBO J. , vol.26 , pp. 2527-2539
    • Maiuri, M.C.1    Le Toumelin, G.2    Criollo, A.3
  • 17
    • 79958155708 scopus 로고    scopus 로고
    • Characterization of a caspase-3-substrate kinome using an N- and C-terminally tagged protein kinase library produced by a cell-free system
    • Tadokoro D., Takahama S., Shimizu K., et al. Characterization of a caspase-3-substrate kinome using an N- and C-terminally tagged protein kinase library produced by a cell-free system. Cell Death Dis. 2010, 1:e89.
    • (2010) Cell Death Dis. , vol.1
    • Tadokoro, D.1    Takahama, S.2    Shimizu, K.3
  • 18
    • 79958701128 scopus 로고    scopus 로고
    • Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis
    • Cheng J.P., Betin V.M., Weir H., et al. Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis. Cell Death Dis. 2010, 1:e82.
    • (2010) Cell Death Dis. , vol.1
    • Cheng, J.P.1    Betin, V.M.2    Weir, H.3
  • 19
    • 78649636176 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria
    • Wirawan E., VandeWalle L., Kersse K., et al. Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria. Cell Death Dis. 2010, 1:e18.
    • (2010) Cell Death Dis. , vol.1
    • Wirawan, E.1    VandeWalle, L.2    Kersse, K.3
  • 20
    • 70449529788 scopus 로고    scopus 로고
    • FLIP-mediated autophagy regulation in cell death control
    • Lee J.S., Li Q., Lee J.Y., et al. FLIP-mediated autophagy regulation in cell death control. Nat. Cell Biol. 2009, 11:1355-1362.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1355-1362
    • Lee, J.S.1    Li, Q.2    Lee, J.Y.3
  • 21
    • 0036160679 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR): pro- and anti-apoptotic
    • Castedo M., Ferri K.F., Kroemer G. Mammalian target of rapamycin (mTOR): pro- and anti-apoptotic. Cell Death Differ. 2002, 9:99-100.
    • (2002) Cell Death Differ. , vol.9 , pp. 99-100
    • Castedo, M.1    Ferri, K.F.2    Kroemer, G.3
  • 22
    • 77950501014 scopus 로고    scopus 로고
    • MTOR regulation of autophagy
    • Jung C.H., Ro S.H., Cao J., et al. mTOR regulation of autophagy. FEBS Lett. 2010, 7:1287-1295.
    • (2010) FEBS Lett. , vol.7 , pp. 1287-1295
    • Jung, C.H.1    Ro, S.H.2    Cao, J.3
  • 23
    • 78149475031 scopus 로고    scopus 로고
    • Activation of mTOR coincides with autophagy during ligation-induced atrophy in the rat submandibular gland
    • Silver N., Proctor G.B., Arno M., et al. Activation of mTOR coincides with autophagy during ligation-induced atrophy in the rat submandibular gland. Cell Death Dis. 2010, 1:e14.
    • (2010) Cell Death Dis. , vol.1
    • Silver, N.1    Proctor, G.B.2    Arno, M.3
  • 24
    • 77949542302 scopus 로고    scopus 로고
    • The receptor for advanced glycation end products (RAGE) sustains autophagy and limits apoptosis, promoting pancreatic tumor cell survival
    • Kang R., Tang D., Schapiro N.E., et al. The receptor for advanced glycation end products (RAGE) sustains autophagy and limits apoptosis, promoting pancreatic tumor cell survival. Cell Death Differ. 2010, 4:666-676.
    • (2010) Cell Death Differ. , vol.4 , pp. 666-676
    • Kang, R.1    Tang, D.2    Schapiro, N.E.3
  • 26
    • 67949101910 scopus 로고    scopus 로고
    • Active transcription of the human FAS/CD95/TNFRSF6 gene involves the p53 family
    • Schilling T., Schleithoff E.S., Kairat A., et al. Active transcription of the human FAS/CD95/TNFRSF6 gene involves the p53 family. Biochem. Biophys. Res. Commun. 2009, 387:399-404.
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 399-404
    • Schilling, T.1    Schleithoff, E.S.2    Kairat, A.3
  • 28
    • 0033600234 scopus 로고    scopus 로고
    • Regulation of the p53 homolog p73 by c-Abl tyrosine kinase in cell death response to cisplatin
    • Gong J.G., Costanzo A., Yang H.Q., et al. Regulation of the p53 homolog p73 by c-Abl tyrosine kinase in cell death response to cisplatin. Nature 1999, 399:806-809.
    • (1999) Nature , vol.399 , pp. 806-809
    • Gong, J.G.1    Costanzo, A.2    Yang, H.Q.3
  • 29
    • 1542379662 scopus 로고    scopus 로고
    • P73 induces apoptosis via PUMA transactivation and Bax mitochondrial translocation
    • Melino G., Bernassola F., Ranalli M., et al. p73 induces apoptosis via PUMA transactivation and Bax mitochondrial translocation. J. Biol. Chem. 2004, 279:8076-8083.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8076-8083
    • Melino, G.1    Bernassola, F.2    Ranalli, M.3
  • 31
    • 79952129478 scopus 로고    scopus 로고
    • Differential regulation of the p73 cistrome by mammalian target of rapamycin reveals transcriptional programs of mesenchymal differentiation and tumorigenesis
    • Rosenbluth J.M., Mays D.J., Jiang A., et al. Differential regulation of the p73 cistrome by mammalian target of rapamycin reveals transcriptional programs of mesenchymal differentiation and tumorigenesis. Proc. Natl. Acad. Sci. USA 2011, 108:2076-2081.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2076-2081
    • Rosenbluth, J.M.1    Mays, D.J.2    Jiang, A.3
  • 32
    • 79952083494 scopus 로고    scopus 로고
    • Resistance to caspase-8 and -9 fragments in a malignant pleural mesothelioma cell line with acquired cisplatin-resistance
    • Janson V., Johansson A., Grankvist K. Resistance to caspase-8 and -9 fragments in a malignant pleural mesothelioma cell line with acquired cisplatin-resistance. Cell Death Dis. 2010, 1:e78.
    • (2010) Cell Death Dis. , vol.1
    • Janson, V.1    Johansson, A.2    Grankvist, K.3
  • 33
    • 79551675278 scopus 로고    scopus 로고
    • XIAP impairs Smac release from the mitochondria during apoptosis
    • Flanagan L., Sebastià J., Tuffy L.P., et al. XIAP impairs Smac release from the mitochondria during apoptosis. Cell Death Dis. 2010, 1:e49.
    • (2010) Cell Death Dis. , vol.1
    • Flanagan, L.1    Sebastià, J.2    Tuffy, L.P.3
  • 34
    • 78650414544 scopus 로고    scopus 로고
    • Extraribosomal functions associated with the C terminus of the 37/67 kDalaminin receptor are required for maintaining cell viability
    • Scheiman J., Jamieson K.V., Ziello J., et al. Extraribosomal functions associated with the C terminus of the 37/67 kDalaminin receptor are required for maintaining cell viability. Cell Death Dis. 2010, 1:e42.
    • (2010) Cell Death Dis. , vol.1
    • Scheiman, J.1    Jamieson, K.V.2    Ziello, J.3
  • 35
    • 57049155399 scopus 로고    scopus 로고
    • Directing cancer cells to self-destruct with pro-apoptotic receptor agonists
    • Ashkenazi A. Directing cancer cells to self-destruct with pro-apoptotic receptor agonists. Nat. Rev. Drug Discov. 2008, 12:1001-1012.
    • (2008) Nat. Rev. Drug Discov. , vol.12 , pp. 1001-1012
    • Ashkenazi, A.1
  • 36
    • 79958698544 scopus 로고    scopus 로고
    • Synergistic induction of cell death in liver tumor cells by TRAIL and chemotherapeutic drugs via the BH3-only proteins Bim and Bid
    • Schneider-Jakob S., Corazza N., Badmann A., et al. Synergistic induction of cell death in liver tumor cells by TRAIL and chemotherapeutic drugs via the BH3-only proteins Bim and Bid. Cell Death Dis. 2010, 1:e86.
    • (2010) Cell Death Dis. , vol.1
    • Schneider-Jakob, S.1    Corazza, N.2    Badmann, A.3
  • 37
    • 79958750290 scopus 로고    scopus 로고
    • Rapid and efficient cancer cell killing mediated by high-affinity death receptor homotrimerizing TRAIL variants
    • Reis C.R., van der Sloot A.M., Natoni A., et al. Rapid and efficient cancer cell killing mediated by high-affinity death receptor homotrimerizing TRAIL variants. Cell Death Dis. 2010, 1:e83.
    • (2010) Cell Death Dis. , vol.1
    • Reis, C.R.1    van der Sloot, A.M.2    Natoni, A.3
  • 38
    • 77957361864 scopus 로고    scopus 로고
    • Targeting microRNAs in cancer: rationale, strategies and challenges
    • Garzon R., Marcucci G., Croce C.M. Targeting microRNAs in cancer: rationale, strategies and challenges. Nat. Rev. Drug Discov. 2010, 10:775-789.
    • (2010) Nat. Rev. Drug Discov. , vol.10 , pp. 775-789
    • Garzon, R.1    Marcucci, G.2    Croce, C.M.3
  • 39
    • 84856533765 scopus 로고    scopus 로고
    • MiR-130a targets MET and induces TRAIL-sensitivity in NSCLC by downregulating miR-221 and 222
    • (doi:10.1038/onc.2011.260)
    • Acunzo M., Visone R., Romano G., et al. miR-130a targets MET and induces TRAIL-sensitivity in NSCLC by downregulating miR-221 and 222. Oncogene 2011, (doi:10.1038/onc.2011.260).
    • (2011) Oncogene
    • Acunzo, M.1    Visone, R.2    Romano, G.3
  • 40
    • 79959811503 scopus 로고    scopus 로고
    • Downregulation of miR-205 and miR-31 confers resistance to chemotherapy-induced apoptosis in prostate cancer cells
    • Bhatnagar N., Li X., Padi S.K., et al. Downregulation of miR-205 and miR-31 confers resistance to chemotherapy-induced apoptosis in prostate cancer cells. Cell Death Dis. 2010, 1:e105.
    • (2010) Cell Death Dis. , vol.1
    • Bhatnagar, N.1    Li, X.2    Padi, S.K.3
  • 41
    • 79957552560 scopus 로고    scopus 로고
    • Enhancer of Zeste homolog 2 (EZH2) is overexpressed in recurrent nasopharyngeal carcinoma and is regulated by miR-26a, miR-101, and miR-98
    • Alajez N.M., Shi W., Hui A.B., et al. Enhancer of Zeste homolog 2 (EZH2) is overexpressed in recurrent nasopharyngeal carcinoma and is regulated by miR-26a, miR-101, and miR-98. Cell Death Dis. 2010, 1:e85.
    • (2010) Cell Death Dis. , vol.1
    • Alajez, N.M.1    Shi, W.2    Hui, A.B.3
  • 42
    • 74249102653 scopus 로고    scopus 로고
    • Elevated expression of the tyrosine phosphatase SHP-1 defines a subset of high-grade breast tumors
    • Insabato L., Amelio I., Quarto M., et al. Elevated expression of the tyrosine phosphatase SHP-1 defines a subset of high-grade breast tumors. Oncology 2009, 6:378-384.
    • (2009) Oncology , vol.6 , pp. 378-384
    • Insabato, L.1    Amelio, I.2    Quarto, M.3
  • 43
    • 79959985637 scopus 로고    scopus 로고
    • Differential effects of the phosphatidylinositol 4-kinases, PI4KIIα and PI4KIIIβ, on Akt activation and apoptosis
    • Chu K.M., Minogue S., Hsuan J.J., et al. Differential effects of the phosphatidylinositol 4-kinases, PI4KIIα and PI4KIIIβ, on Akt activation and apoptosis. Cell Death Dis. 2010, 1:e106.
    • (2010) Cell Death Dis. , vol.1
    • Chu, K.M.1    Minogue, S.2    Hsuan, J.J.3
  • 44
    • 79958742235 scopus 로고    scopus 로고
    • Palmitoylation of human FasL modulates its cell death-inducing function
    • Guardiola-Serrano F., Rossin A., Cahuzac N., et al. Palmitoylation of human FasL modulates its cell death-inducing function. Cell Death Dis. 2010, 1:e88.
    • (2010) Cell Death Dis. , vol.1
    • Guardiola-Serrano, F.1    Rossin, A.2    Cahuzac, N.3
  • 45
    • 79951818357 scopus 로고    scopus 로고
    • Apoptosis of human melanoma cells induced by inhibition of B-RAFV600E involves preferential splicing of bimS
    • Jiang C.C., Lai F., Tay K.H., et al. Apoptosis of human melanoma cells induced by inhibition of B-RAFV600E involves preferential splicing of bimS. Cell Death Dis. 2010, 1:e69.
    • (2010) Cell Death Dis. , vol.1
    • Jiang, C.C.1    Lai, F.2    Tay, K.H.3
  • 46
    • 79958260693 scopus 로고    scopus 로고
    • Expression of coxsackie and adenovirus receptor distinguishes transitional cancer states in therapy-induced cellular senescence
    • Wu P.C., Wang Q., Dong Z.M., et al. Expression of coxsackie and adenovirus receptor distinguishes transitional cancer states in therapy-induced cellular senescence. Cell Death Dis. 2010, 1:e70.
    • (2010) Cell Death Dis. , vol.1
    • Wu, P.C.1    Wang, Q.2    Dong, Z.M.3
  • 47
    • 79956265753 scopus 로고    scopus 로고
    • Negative regulation of UCP2 by TGFβ signaling characterizes low and intermediate-grade primary breast cancer
    • Sayeed A., Meng Z., Luciani G., et al. Negative regulation of UCP2 by TGFβ signaling characterizes low and intermediate-grade primary breast cancer. Cell Death Dis. 2010, 1:e53.
    • (2010) Cell Death Dis. , vol.1
    • Sayeed, A.1    Meng, Z.2    Luciani, G.3
  • 48
    • 79953067256 scopus 로고    scopus 로고
    • Impact of the DNA methyltransferases expression on the methylation status of apoptosis-associated genes in glioblastomamultiforme
    • Hervouet E., Vallette F.M., Cartron P.F. Impact of the DNA methyltransferases expression on the methylation status of apoptosis-associated genes in glioblastomamultiforme. Cell Death Dis. 2010, 1:e8.
    • (2010) Cell Death Dis. , vol.1
    • Hervouet, E.1    Vallette, F.M.2    Cartron, P.F.3
  • 49
    • 77951220669 scopus 로고    scopus 로고
    • Role of autophagy in suppression of inflammation and cancer
    • White E., Karp C., Strohecker A.M., et al. Role of autophagy in suppression of inflammation and cancer. Curr. Opin. Cell Biol. 2010, 22:212-217.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 212-217
    • White, E.1    Karp, C.2    Strohecker, A.M.3
  • 50
    • 79952228407 scopus 로고    scopus 로고
    • Activated Ras requires autophagy to maintain oxidative metabolism and tumorigenesis
    • Guo J.Y., Chen H.Y., Mathew R., et al. Activated Ras requires autophagy to maintain oxidative metabolism and tumorigenesis. Genes Dev. 2011, 25:460-470.
    • (2011) Genes Dev. , vol.25 , pp. 460-470
    • Guo, J.Y.1    Chen, H.Y.2    Mathew, R.3
  • 51
    • 70350365288 scopus 로고    scopus 로고
    • Desmethylclomipramine induces the accumulation of autophagy markers by blocking autophagic flux
    • Rossi M., Munarriz E.R., Bartesaghi S., et al. Desmethylclomipramine induces the accumulation of autophagy markers by blocking autophagic flux. J. Cell Sci. 2009, 122:3330-3339.
    • (2009) J. Cell Sci. , vol.122 , pp. 3330-3339
    • Rossi, M.1    Munarriz, E.R.2    Bartesaghi, S.3
  • 52
    • 33846794896 scopus 로고    scopus 로고
    • Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma
    • Amaravadi R.K., Yu D., Lum J.J., et al. Autophagy inhibition enhances therapy-induced apoptosis in a Myc-induced model of lymphoma. J. Clin. Invest. 2007, 117:326-336.
    • (2007) J. Clin. Invest. , vol.117 , pp. 326-336
    • Amaravadi, R.K.1    Yu, D.2    Lum, J.J.3
  • 53
    • 50349098812 scopus 로고    scopus 로고
    • Involvement of protective autophagy in TRAIL resistance of apoptosis-defective tumor cells
    • Han J., Hou W., Goldstein L.A., et al. Involvement of protective autophagy in TRAIL resistance of apoptosis-defective tumor cells. J. Biol. Chem. 2008, 283:19665-19677.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19665-19677
    • Han, J.1    Hou, W.2    Goldstein, L.A.3
  • 54
    • 79953038110 scopus 로고    scopus 로고
    • Cytotoxicity of apigenin on leukemia cell lines: implications for prevention and therapy
    • Ruela-de-Sousa R.R., Fuhler G.M., Blom N., et al. Cytotoxicity of apigenin on leukemia cell lines: implications for prevention and therapy. Cell Death Dis. 2010, 1:e19.
    • (2010) Cell Death Dis. , vol.1
    • Ruela-de-Sousa, R.R.1    Fuhler, G.M.2    Blom, N.3
  • 55
    • 79958759965 scopus 로고    scopus 로고
    • Proton pump inhibition induces autophagy as a survival mechanism following oxidative stress in human melanoma cells
    • Marino M.L., Fais S., Djavaheri-Mergny M., et al. Proton pump inhibition induces autophagy as a survival mechanism following oxidative stress in human melanoma cells. Cell Death Dis. 2010, 1:e87.
    • (2010) Cell Death Dis. , vol.1
    • Marino, M.L.1    Fais, S.2    Djavaheri-Mergny, M.3
  • 56
    • 34249279169 scopus 로고    scopus 로고
    • GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspaseactivation
    • Colell A., Ricci J.E., Tait S., et al. GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspaseactivation. Cell 2007, 129:983-997.
    • (2007) Cell , vol.129 , pp. 983-997
    • Colell, A.1    Ricci, J.E.2    Tait, S.3
  • 57
    • 33645115547 scopus 로고    scopus 로고
    • Adding chloroquine to conventional treatment for glioblastomamultiforme: a randomized, double- blind, placebo-controlled trial
    • Sotelo J., Briceno E., Lopez-Gonzalez M.A. Adding chloroquine to conventional treatment for glioblastomamultiforme: a randomized, double- blind, placebo-controlled trial. Ann. Intern. Med. 2006, 144:337-343.
    • (2006) Ann. Intern. Med. , vol.144 , pp. 337-343
    • Sotelo, J.1    Briceno, E.2    Lopez-Gonzalez, M.A.3
  • 58
    • 79960410571 scopus 로고    scopus 로고
    • Sorafenib enhances pemetrexed cytotoxicity through an autophagy-dependent mechanism in cancer cells
    • Bareford M.D., Park M.A., Yacoub A., et al. Sorafenib enhances pemetrexed cytotoxicity through an autophagy-dependent mechanism in cancer cells. Cancer Res. 2011, 71:4955-4956.
    • (2011) Cancer Res. , vol.71 , pp. 4955-4956
    • Bareford, M.D.1    Park, M.A.2    Yacoub, A.3
  • 59
    • 79959774131 scopus 로고    scopus 로고
    • Obatoclax induces Atg7-dependent autophagy independent of beclin-1 and BAX/BAK
    • McCoy F., Hurwitz J., McTavish N., et al. Obatoclax induces Atg7-dependent autophagy independent of beclin-1 and BAX/BAK. Cell Death Dis. 2010, 1:e108.
    • (2010) Cell Death Dis. , vol.1
    • McCoy, F.1    Hurwitz, J.2    McTavish, N.3
  • 60
    • 79958276489 scopus 로고    scopus 로고
    • GX15-070 (obatoclax) overcomes glucocorticoid resistance in acute lymphoblastic leukemia through induction of apoptosis and autophagy
    • Heidari N., Hicks M.A., Harada H. GX15-070 (obatoclax) overcomes glucocorticoid resistance in acute lymphoblastic leukemia through induction of apoptosis and autophagy. Cell Death Dis. 2010, 1:e76.
    • (2010) Cell Death Dis. , vol.1
    • Heidari, N.1    Hicks, M.A.2    Harada, H.3
  • 61
    • 79958266013 scopus 로고    scopus 로고
    • Androgens modulate autophagy and cell death via regulation of the endoplasmic reticulum chaperone glucose-regulated protein 78/BiP in prostate cancer cells
    • Bennett H.L., Fleming J.T., O'Prey J., et al. Androgens modulate autophagy and cell death via regulation of the endoplasmic reticulum chaperone glucose-regulated protein 78/BiP in prostate cancer cells. Cell Death Dis. 2010, 1:e72.
    • (2010) Cell Death Dis. , vol.1
    • Bennett, H.L.1    Fleming, J.T.2    O'Prey, J.3
  • 62
    • 79959968916 scopus 로고    scopus 로고
    • The novel estrogen-induced gene EIG121 regulates autophagy and promotes cell survival under stress
    • Deng L., Feng J., Broaddus R.R. The novel estrogen-induced gene EIG121 regulates autophagy and promotes cell survival under stress. Cell Death Dis. 2010, 1:e32.
    • (2010) Cell Death Dis. , vol.1
    • Deng, L.1    Feng, J.2    Broaddus, R.R.3
  • 63
    • 79958855476 scopus 로고    scopus 로고
    • Familial amyloidprecursor protein mutants cause caspase-6-dependent but amyloid β-peptide-independent neuronal degeneration in primary human neuron cultures
    • Sivananthan S.N., Lee A.W., Goodyer C.G., et al. Familial amyloidprecursor protein mutants cause caspase-6-dependent but amyloid β-peptide-independent neuronal degeneration in primary human neuron cultures. Cell Death Dis. 2010, 1:e100.
    • (2010) Cell Death Dis. , vol.1
    • Sivananthan, S.N.1    Lee, A.W.2    Goodyer, C.G.3
  • 64
    • 77956369812 scopus 로고    scopus 로고
    • Imaging multiple phases of neurodegeneration: a novel approach to assessing cell death in vivo
    • Cordeiro M.F., Guo L., Coxon K.M., et al. Imaging multiple phases of neurodegeneration: a novel approach to assessing cell death in vivo. Cell Death Dis. 2010, 1:e3.
    • (2010) Cell Death Dis. , vol.1
    • Cordeiro, M.F.1    Guo, L.2    Coxon, K.M.3
  • 65
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
    • Sarkar S., Ravikumar B., Floto R.A., et al. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ. 2009, 16:46-56.
    • (2009) Cell Death Differ. , vol.16 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3
  • 66
    • 26444441008 scopus 로고    scopus 로고
    • CAG repeat implicates a dominant property of Huntingtin in mitochondrial energy metabolism
    • Seong I.S., Ivanova E., Lee J.M., et al. CAG repeat implicates a dominant property of Huntingtin in mitochondrial energy metabolism. Hum. Mol. Genet. 2005, 14:2871-2880.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2871-2880
    • Seong, I.S.1    Ivanova, E.2    Lee, J.M.3
  • 67
    • 22844440902 scopus 로고    scopus 로고
    • Mitochondrial impairment in patients and asymptomatic mutation carriers of Huntington's disease
    • Saft C., Zange J., Andrich J., et al. Mitochondrial impairment in patients and asymptomatic mutation carriers of Huntington's disease. Mov. Disord. 2005, 20:674-679.
    • (2005) Mov. Disord. , vol.20 , pp. 674-679
    • Saft, C.1    Zange, J.2    Andrich, J.3
  • 68
    • 79951482092 scopus 로고    scopus 로고
    • Mutant Huntingtin induces activation of the Bcl-2/adenovirus E1B 19-kDa interacting protein (BNip3)
    • Sassone J., Colciago C., Marchi P., et al. Mutant Huntingtin induces activation of the Bcl-2/adenovirus E1B 19-kDa interacting protein (BNip3). Cell Death Dis. 2010, 1:e7.
    • (2010) Cell Death Dis. , vol.1
    • Sassone, J.1    Colciago, C.2    Marchi, P.3
  • 69
    • 77952216305 scopus 로고    scopus 로고
    • Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease
    • Yacoubian T.A., Slone S.R., Harrington A.J., et al. Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease. Cell Death Dis. 2010, 1:e2.
    • (2010) Cell Death Dis. , vol.1
    • Yacoubian, T.A.1    Slone, S.R.2    Harrington, A.J.3
  • 70
    • 79958719815 scopus 로고    scopus 로고
    • The acetylation of RelA in Lys310 dictates the NF-κB-dependent response in post-ischemic injury
    • Lanzillotta A., Sarnico I., Ingrassia R., et al. The acetylation of RelA in Lys310 dictates the NF-κB-dependent response in post-ischemic injury. Cell Death Dis. 2010, 1:e96.
    • (2010) Cell Death Dis. , vol.1
    • Lanzillotta, A.1    Sarnico, I.2    Ingrassia, R.3
  • 71
    • 79958278799 scopus 로고    scopus 로고
    • MicroRNA-21 dysregulates the expression of MEF2C in neurons in monkey and human SIV/HIV neurological disease
    • Yelamanchili S.V., Chaudhuri A.D., Chen L.N., et al. MicroRNA-21 dysregulates the expression of MEF2C in neurons in monkey and human SIV/HIV neurological disease. Cell Death Dis. 2010, 1:e77.
    • (2010) Cell Death Dis. , vol.1
    • Yelamanchili, S.V.1    Chaudhuri, A.D.2    Chen, L.N.3
  • 72
    • 79958266014 scopus 로고    scopus 로고
    • Autism spectrum disorder is related to endoplasmic reticulum stress induced by mutations in the synaptic cell adhesion molecule, CADM1
    • Fujita E., Dai H., Tanabe Y., et al. Autism spectrum disorder is related to endoplasmic reticulum stress induced by mutations in the synaptic cell adhesion molecule, CADM1. Cell Death Dis. 2010, 1:e47.
    • (2010) Cell Death Dis. , vol.1
    • Fujita, E.1    Dai, H.2    Tanabe, Y.3
  • 73
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., et al. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3
  • 74
    • 56449083411 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration and development
    • Winslow A.R., Rubinsztein D.C. Autophagy in neurodegeneration and development. Biochim. Biophys. Acta 2008, 1782:723-729.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 723-729
    • Winslow, A.R.1    Rubinsztein, D.C.2
  • 75
    • 24944482408 scopus 로고    scopus 로고
    • Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
    • Iwata A., Christianson J.C., Bucci M., et al. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc. Natl. Acad. Sci. USA 2005, 102:13135-13140.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13135-13140
    • Iwata, A.1    Christianson, J.C.2    Bucci, M.3
  • 76
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B., Vacher C., Berger Z., et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet. 2004, 36:585-595.
    • (2004) Nat. Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 77
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: a question of balance
    • Cherra S.J., Chu C.T. Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol. 2008, 3:309-323.
    • (2008) Future Neurol. , vol.3 , pp. 309-323
    • Cherra, S.J.1    Chu, C.T.2
  • 78
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia
    • Lee J.A., Gao F.B. Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J. Neurosci. 2009, 29:8506-8511.
    • (2009) J. Neurosci. , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 79
    • 79958730602 scopus 로고    scopus 로고
    • Lithium reduces apoptosis and autophagy after neonatal hypoxia-ischemia
    • Li Q., Li H., Roughton K., et al. Lithium reduces apoptosis and autophagy after neonatal hypoxia-ischemia. Cell Death Dis. 2010, 1:e56.
    • (2010) Cell Death Dis. , vol.1
    • Li, Q.1    Li, H.2    Roughton, K.3
  • 80
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine B., Klionsky D.J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 2004, 6:463-477.
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 81
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: unanswered questions
    • Klionsky D.J. The molecular machinery of autophagy: unanswered questions. J. Cell Sci. 2005, 1:7-18.
    • (2005) J. Cell Sci. , vol.1 , pp. 7-18
    • Klionsky, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.