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Volumn 16, Issue 1, 2015, Pages

Protease 3C of hepatitis A virus induces vacuolization of lysosomal/endosomal organelles and caspase-independent cell death

Author keywords

3C protease; Caspase independent cell death; Cytoplasmic vacuolization; Hepatitis A virus

Indexed keywords

3C PROTEASE; BAFILOMYCIN A1; CASPASE; CASPASE INHIBITOR; CYSTEINE PROTEINASE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; PHOSPHATIDYLSERINE; PROTEIN RAB5; PROTEIN RAB9; PROTEIN RIP1 KINASE; PROTEINASE; RAB PROTEIN; RAB11 PROTEIN; RAB7 PROTEIN; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS PROTEIN; 3C PROTEASES; AGFG1 PROTEIN, HUMAN; BENZYLOXYCARBONYLVALYL-ALANYL-ASPARTYL FLUOROMETHYL KETONE; GUANOSINE TRIPHOSPHATASE; IMIDAZOLE DERIVATIVE; INDOLE DERIVATIVE; MACROLIDE; NECROSTATIN-1; NUCLEOPORIN; PEPTIDE CHLOROMETHYL KETONE; RNA BINDING PROTEIN;

EID: 84924910470     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/s12860-015-0050-z     Document Type: Article
Times cited : (32)

References (92)
  • 2
    • 0025885346 scopus 로고
    • Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus
    • Clark ME, Hämmerle T, Wimmer E, Dasgupta A. Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J. 1991;10:2941-7.
    • (1991) EMBO J , vol.10 , pp. 2941-2947
    • Clark, M.E.1    Hämmerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 3
    • 0027535652 scopus 로고
    • Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
    • Clark ME, Lieberman PM, Berk AJ, Dasgupta A. Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro. Mol Cell Biol. 1993;13:1232-7.
    • (1993) Mol Cell Biol , vol.13 , pp. 1232-1237
    • Clark, M.E.1    Lieberman, P.M.2    Berk, A.J.3    Dasgupta, A.4
  • 4
    • 0031016644 scopus 로고    scopus 로고
    • Inhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro
    • Yalamanchili P, Datta U, Dasgupta A. Inhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro. J Virol. 1997;71:1220-6.
    • (1997) J Virol , vol.71 , pp. 1220-1226
    • Yalamanchili, P.1    Datta, U.2    Dasgupta, A.3
  • 5
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham GJ, McInerney GM, Ross-Smith N. Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J Virol. 2000;74:272-80.
    • (2000) J Virol , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 6
    • 0035695178 scopus 로고    scopus 로고
    • Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity
    • Weidman MK, Yalamanchili P, Ng B, Tsai W, Dasgupta A. Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity. Virology. 2001;291:260-71.
    • (2001) Virology , vol.291 , pp. 260-271
    • Weidman, M.K.1    Yalamanchili, P.2    Ng, B.3    Tsai, W.4    Dasgupta, A.5
  • 7
    • 0036171240 scopus 로고    scopus 로고
    • Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease
    • Kuyumcu-Martinez NM, Joachims M, Lloyd RE. Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J Virol. 2002;76:2062-74.
    • (2002) J Virol , vol.76 , pp. 2062-2074
    • Kuyumcu-Martinez, N.M.1    Joachims, M.2    Lloyd, R.E.3
  • 8
    • 5444250376 scopus 로고    scopus 로고
    • Rhinovirus 3C protease precursors 3CD and 3CD' localize to the nuclei of infected cells
    • Amineva SP, Aminev AG, Palmenberg AC, Gern JE. Rhinovirus 3C protease precursors 3CD and 3CD' localize to the nuclei of infected cells. J Gen Virol. 2004;85:2969-79.
    • (2004) J Gen Virol , vol.85 , pp. 2969-2979
    • Amineva, S.P.1    Aminev, A.G.2    Palmenberg, A.C.3    Gern, J.E.4
  • 9
    • 0842347402 scopus 로고    scopus 로고
    • Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Protease Inhibits Host Cell Translation: a Novel Mechanism for Host Translation Shutoff
    • Kuyumcu-Martinez NM, Eden MEV, Younan P, Lloyd RE. Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Protease Inhibits Host Cell Translation: a Novel Mechanism for Host Translation Shutoff. Mol Cell Biol. 2004;24:1779-90.
    • (2004) Mol Cell Biol , vol.24 , pp. 1779-1790
    • Kuyumcu-Martinez, N.M.1    Eden, M.E.V.2    Younan, P.3    Lloyd, R.E.4
  • 10
    • 70349659010 scopus 로고    scopus 로고
    • Enterovirus 71 3C protease cleaves a novel target CstF-64 and inhibits cellular polyadenylation
    • Weng K-F, Li M-L, Hung C-T, Shih S-R. Enterovirus 71 3C protease cleaves a novel target CstF-64 and inhibits cellular polyadenylation. PLoS Pathog. 2009;5:e1000593.
    • (2009) PLoS Pathog , vol.5 , pp. e1000593
    • Weng, K.-F.1    Li, M.-L.2    Hung, C.-T.3    Shih, S.-R.4
  • 11
    • 84869067803 scopus 로고    scopus 로고
    • Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication
    • Kobayashi M, Arias C, GaRabedian A, Palmenberg AC, Mohr I. Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication. J Virol. 2012;86:10686-94.
    • (2012) J Virol , vol.86 , pp. 10686-10694
    • Kobayashi, M.1    Arias, C.2    GaRabedian, A.3    Palmenberg, A.C.4    Mohr, I.5
  • 12
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk MM, Grigera PR, Bergmann IE, Zibert A, Multhaup G, Beck E. Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. J Virol. 1990;64:748-56.
    • (1990) J Virol , vol.64 , pp. 748-756
    • Falk, M.M.1    Grigera, P.R.2    Bergmann, I.E.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 13
    • 0029126160 scopus 로고
    • Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4
    • Joachims M, Harris KS, Etchison D. Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4. Virology. 1995;211:451-61.
    • (1995) Virology , vol.211 , pp. 451-461
    • Joachims, M.1    Harris, K.S.2    Etchison, D.3
  • 14
    • 55249116074 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus, but not bovine enterovirus, targets the host cell cytoskeleton via the nonstructural protein 3Cpro
    • Armer H, Moffat K, Wileman T, Belsham GJ, Jackson T, Duprex WP, et al. Foot-and-mouth disease virus, but not bovine enterovirus, targets the host cell cytoskeleton via the nonstructural protein 3Cpro. J Virol. 2008;82:10556-66.
    • (2008) J Virol , vol.82 , pp. 10556-10566
    • Armer, H.1    Moffat, K.2    Wileman, T.3    Belsham, G.J.4    Jackson, T.5    Duprex, W.P.6
  • 16
    • 79953279338 scopus 로고    scopus 로고
    • The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling
    • Mukherjee A, Morosky SA, Delorme-Axford E, Dybdahl-Sissoko N, Oberste MS, Wang T, et al. The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling. PLoS Pathog. 2011;7:e1001311.
    • (2011) PLoS Pathog , vol.7 , pp. e1001311
    • Mukherjee, A.1    Morosky, S.A.2    Delorme-Axford, E.3    Dybdahl-Sissoko, N.4    Oberste, M.S.5    Wang, T.6
  • 17
    • 84873053639 scopus 로고    scopus 로고
    • Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses cellular responses
    • Lei X, Xiao X, Xue Q, Jin Q, He B, Wang J. Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses cellular responses. J Virol. 2013;87:1690-8.
    • (2013) J Virol , vol.87 , pp. 1690-1698
    • Lei, X.1    Xiao, X.2    Xue, Q.3    Jin, Q.4    He, B.5    Wang, J.6
  • 18
    • 0036057766 scopus 로고    scopus 로고
    • The 3C protease activity of enterovirus 71 induces human neural cell apoptosis
    • Li M-L, Hsu T-A, Chen T-C, Chang S-C, Lee J-C, Chen C-C, et al. The 3C protease activity of enterovirus 71 induces human neural cell apoptosis. Virology. 2002;293:386-95.
    • (2002) Virology , vol.293 , pp. 386-395
    • Li, M.-L.1    Hsu, T.-A.2    Chen, T.-C.3    Chang, S.-C.4    Lee, J.-C.5    Chen, C.-C.6
  • 19
    • 2642511414 scopus 로고    scopus 로고
    • Individual expression of poliovirus 2Apro and 3Cpro induces activation of caspase-3 and PARP cleavage in HeLa cells
    • Calandria C, Irurzun A, Barco A, Carrasco L. Individual expression of poliovirus 2Apro and 3Cpro induces activation of caspase-3 and PARP cleavage in HeLa cells. Virus Res. 2004;104:39-49.
    • (2004) Virus Res , vol.104 , pp. 39-49
    • Calandria, C.1    Irurzun, A.2    Barco, A.3    Carrasco, L.4
  • 20
    • 33847266242 scopus 로고    scopus 로고
    • Coxsackievirus B3 proteases 2A and 3C induce apoptotic cell death through mitochondrial injury and cleavage of eIF4GI but not DAP5/p97/NAT1
    • Chau DHW, Yuan J, Zhang H, Cheung P, Lim T, Liu Z, et al. Coxsackievirus B3 proteases 2A and 3C induce apoptotic cell death through mitochondrial injury and cleavage of eIF4GI but not DAP5/p97/NAT1. Apoptosis. 2006;12:513-24.
    • (2006) Apoptosis , vol.12 , pp. 513-524
    • Chau, D.H.W.1    Yuan, J.2    Zhang, H.3    Cheung, P.4    Lim, T.5    Liu, Z.6
  • 21
    • 34848898241 scopus 로고    scopus 로고
    • Poly(A) binding protein, C-terminally truncated by the hepatitis A virus proteinase 3C, inhibits viral translation
    • Zhang B, Morace G, Gauss-Müller V, Kusov Y. Poly(A) binding protein, C-terminally truncated by the hepatitis A virus proteinase 3C, inhibits viral translation. Nucleic Acids Res. 2007;35:5975-84.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5975-5984
    • Zhang, B.1    Morace, G.2    Gauss-Müller, V.3    Kusov, Y.4
  • 22
    • 36048978253 scopus 로고    scopus 로고
    • RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease
    • Zhang B, Seitz S, Kusov Y, Zell R, Gauss-Müller V. RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease. Biochem Biophys Res Commun. 2007;364:725-30.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 725-730
    • Zhang, B.1    Seitz, S.2    Kusov, Y.3    Zell, R.4    Gauss-Müller, V.5
  • 23
    • 34249855382 scopus 로고    scopus 로고
    • Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor
    • Yang Y, Liang Y, Qu L, Chen Z, Yi M, Li K, et al. Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc Natl Acad Sci USA. 2007;104:7253-8.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7253-7258
    • Yang, Y.1    Liang, Y.2    Qu, L.3    Chen, Z.4    Yi, M.5    Li, K.6
  • 24
    • 79960598740 scopus 로고    scopus 로고
    • Disruption of TLR3 Signaling Due to Cleavage of TRIF by the Hepatitis A Virus Protease-Polymerase Processing Intermediate, 3CD
    • Qu L, Feng Z, Yamane D, Liang Y, Lanford RE, Li K, et al. Disruption of TLR3 Signaling Due to Cleavage of TRIF by the Hepatitis A Virus Protease-Polymerase Processing Intermediate, 3CD. PLoS Pathog. 2011;7:e1002169.
    • (2011) PLoS Pathog , vol.7 , pp. e1002169
    • Qu, L.1    Feng, Z.2    Yamane, D.3    Liang, Y.4    Lanford, R.E.5    Li, K.6
  • 25
    • 12844264099 scopus 로고    scopus 로고
    • Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization
    • Peters H, Kusov YY, Meyer S, Benie AJ, Bäuml E, Wolff M, et al. Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization. Biochem J. 2005;385:363-70.
    • (2005) Biochem J , vol.385 , pp. 363-370
    • Peters, H.1    Kusov, Y.Y.2    Meyer, S.3    Benie, A.J.4    Bäuml, E.5    Wolff, M.6
  • 26
    • 0007574262 scopus 로고
    • Localization of mitochondria in living cells with rhodamine 123
    • Johnson LV, Walsh ML, Chen LB. Localization of mitochondria in living cells with rhodamine 123. Proc Natl Acad Sci USA. 1980;77:990-4.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 990-994
    • Johnson, L.V.1    Walsh, M.L.2    Chen, L.B.3
  • 29
    • 33747600931 scopus 로고    scopus 로고
    • Do lysosomes induce cell death?
    • Stoka V, Turk V, Turk B. Do lysosomes induce cell death? IUBMB Life. 2006;58:493-4.
    • (2006) IUBMB Life , vol.58 , pp. 493-494
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 30
    • 67349269527 scopus 로고    scopus 로고
    • Necrostatin-1 reverts shikonin-induced necroptosis to apoptosis
    • Han W, Xie J, Li L, Liu Z, Hu X. Necrostatin-1 reverts shikonin-induced necroptosis to apoptosis. Apoptosis. 2009;14:674-86.
    • (2009) Apoptosis , vol.14 , pp. 674-686
    • Han, W.1    Xie, J.2    Li, L.3    Liu, Z.4    Hu, X.5
  • 31
    • 79959251425 scopus 로고    scopus 로고
    • Reactive oxygen species-dependent necroptosis in Jurkat T cells induced by pathogenic free-living Naegleria fowleri
    • Song J, Jang HJ, Lee YA, Kim KA, Lee SK, Shin MH. Reactive oxygen species-dependent necroptosis in Jurkat T cells induced by pathogenic free-living Naegleria fowleri. Parasite Immunology. 2011;33:390-400.
    • (2011) Parasite Immunology , vol.33 , pp. 390-400
    • Song, J.1    Jang, H.J.2    Lee, Y.A.3    Kim, K.A.4    Lee, S.K.5    Shin, M.H.6
  • 32
    • 1542285418 scopus 로고    scopus 로고
    • Simultaneous human papilloma virus type 16 E7 and cdk inhibitor p21 expression induces apoptosis and cathepsin B activation
    • Kaznelson DW, Bruun S, Monrad A, Gjerløv S, Birk J, Röpke C, et al. Simultaneous human papilloma virus type 16 E7 and cdk inhibitor p21 expression induces apoptosis and cathepsin B activation. Virology. 2004;320:301-12.
    • (2004) Virology , vol.320 , pp. 301-312
    • Kaznelson, D.W.1    Bruun, S.2    Monrad, A.3    Gjerløv, S.4    Birk, J.5    Röpke, C.6
  • 33
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death
    • 2+-dependent proteases in ischemic neuronal death. Cell Calcium. 2004;36:285-93.
    • (2004) Cell Calcium , vol.36 , pp. 285-293
    • Yamashima, T.1
  • 34
    • 27844595293 scopus 로고    scopus 로고
    • Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis
    • Harwood SM, Yaqoob MM, Allen DA. Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis. Ann Clin Biochem. 2005;42:415-31.
    • (2005) Ann Clin Biochem , vol.42 , pp. 415-431
    • Harwood, S.M.1    Yaqoob, M.M.2    Allen, D.A.3
  • 35
    • 78649634982 scopus 로고    scopus 로고
    • Genetic control of necrosis - another type of programmed cell death
    • McCall K. Genetic control of necrosis - another type of programmed cell death. Curr Opin Cell Biol. 2010;22:882-8.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 882-888
    • McCall, K.1
  • 38
    • 0033199115 scopus 로고    scopus 로고
    • Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
    • Wolf BB, Goldstein JC, Stennicke HR, Beere H, Amarante-Mendes GP, Salvesen GS, et al. Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation. Blood. 1999;94:1683-92.
    • (1999) Blood , vol.94 , pp. 1683-1692
    • Wolf, B.B.1    Goldstein, J.C.2    Stennicke, H.R.3    Beere, H.4    Amarante-Mendes, G.P.5    Salvesen, G.S.6
  • 39
    • 0032898735 scopus 로고    scopus 로고
    • Non-specific effects of methyl ketone peptide inhibitors of caspases
    • Schotte P, Declercq W, Van Huffel S, Vandenabeele P, Beyaert R. Non-specific effects of methyl ketone peptide inhibitors of caspases. FEBS Lett. 1999;442:117-21.
    • (1999) FEBS Lett , vol.442 , pp. 117-121
    • Schotte, P.1    Declercq, W.2    Huffel, S.3    Vandenabeele, P.4    Beyaert, R.5
  • 40
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N, Zaru R, Micheau O, Thome M, Attinger A, Valitutti S, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol. 2000;1:489-95.
    • (2000) Nat Immunol , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 42
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • Rizzuto R, Brini M, Pizzo P, Murgia M, Pozzan T. Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr Biol. 1995;5:635-42.
    • (1995) Curr Biol , vol.5 , pp. 635-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 43
    • 14744281338 scopus 로고    scopus 로고
    • Bcl-X(L) specifically activates Bak to induce swelling and restructuring of the endoplasmic reticulum
    • Klee M, Pimentel-Muiños FX. Bcl-X(L) specifically activates Bak to induce swelling and restructuring of the endoplasmic reticulum. J Cell Biol. 2005;168:723-34.
    • (2005) J Cell Biol , vol.168 , pp. 723-734
    • Klee, M.1    Pimentel-Muiños, F.X.2
  • 44
    • 4444227321 scopus 로고    scopus 로고
    • Lysosome associated membrane protein 1 (Lamp1) traffics directly from the TGN to early endosomes
    • Cook NR, Row PE, Davidson HW. Lysosome associated membrane protein 1 (Lamp1) traffics directly from the TGN to early endosomes. Traffic. 2004;5:685-99.
    • (2004) Traffic , vol.5 , pp. 685-699
    • Cook, N.R.1    Row, P.E.2    Davidson, H.W.3
  • 45
  • 47
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol. 2009;10:513-25.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 48
    • 0026744303 scopus 로고
    • The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci C, Parton RG, Mather IH, Stunnenberg H, Simons K, Hoflack B, et al. The small GTPase Rab5 functions as a regulatory factor in the early endocytic pathway. Cell. 1992;70:715-28.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6
  • 49
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease
    • Spinosa MR, Progida C, De Luca A, Colucci AMR, Alifano P, Bucci C. Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J Neurosci. 2008;28:1640-8.
    • (2008) J Neurosci , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    Luca, A.3    Colucci, A.M.R.4    Alifano, P.5    Bucci, C.6
  • 50
    • 0031032509 scopus 로고    scopus 로고
    • The small GTP binding protein Rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin
    • Papini E, Satin B, Bucci C, de Bernard M, Telford JL, Manetti R, et al. The small GTP binding protein Rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin. EMBO J. 1997;16:15-24.
    • (1997) EMBO J , vol.16 , pp. 15-24
    • Papini, E.1    Satin, B.2    Bucci, C.3    Bernard, M.4    Telford, J.L.5    Manetti, R.6
  • 51
    • 84879800679 scopus 로고    scopus 로고
    • Zhou X-p: Promotion of autophagy at the maturation step by IL-6 is associated with the sustained mitogen-activated protein kinase/extracellular signal-regulated kinase activity
    • Li X-Z, Sui C-Y, Chen Q, Chen X-P, Zhang H. Zhou X-p: Promotion of autophagy at the maturation step by IL-6 is associated with the sustained mitogen-activated protein kinase/extracellular signal-regulated kinase activity. Mol Cell Biochem. 2013;380:219-27.
    • (2013) Mol Cell Biochem , vol.380 , pp. 219-227
    • Li, X.-Z.1    Sui, C.-Y.2    Chen, Q.3    Chen, X.-P.4    Zhang, H.5
  • 52
    • 73649089980 scopus 로고    scopus 로고
    • ERK and cell death: Mechanisms of ERK-induced cell death - apoptosis, autophagy and senescence
    • Cagnol S, Chambard J-C. ERK and cell death: Mechanisms of ERK-induced cell death - apoptosis, autophagy and senescence. FEBS J. 2010;277:2-21.
    • (2010) FEBS J , vol.277 , pp. 2-21
    • Cagnol, S.1    Chambard, J.-C.2
  • 53
    • 8044257699 scopus 로고    scopus 로고
    • The Phosphatidylinositol 3-Kinase Inhibitors Wortmannin and LY294002 Inhibit Autophagy in Isolated Rat Hepatocytes
    • Blommaart EF, Krause U, Schellens JP, Vreeling-Sindelárová H, Meijer AJ. The Phosphatidylinositol 3-Kinase Inhibitors Wortmannin and LY294002 Inhibit Autophagy in Isolated Rat Hepatocytes. Eur J Biochem. 1997;243:240-6.
    • (1997) Eur J Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelárová, H.4    Meijer, A.J.5
  • 54
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem. 2000;275:992-8.
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 55
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes
    • Jahreiss L, Menzies FM, Rubinsztein DC. The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Traffic. 2008;9:574-87.
    • (2008) Traffic , vol.9 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 57
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague MJ, Urbé S, Aniento F, Gruenberg J. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J Biol Chem. 1994;269:21-4.
    • (1994) J Biol Chem , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbé, S.2    Aniento, F.3    Gruenberg, J.4
  • 59
    • 50349092363 scopus 로고    scopus 로고
    • Active ras triggers death in glioblastoma cells through hyperstimulation of macropinocytosis
    • Overmeyer JH, Kaul A, Johnson EE, Maltese WA. Active ras triggers death in glioblastoma cells through hyperstimulation of macropinocytosis. Mol Cancer Res. 2008;6:965-77.
    • (2008) Mol Cancer Res , vol.6 , pp. 965-977
    • Overmeyer, J.H.1    Kaul, A.2    Johnson, E.E.3    Maltese, W.A.4
  • 60
    • 78649670089 scopus 로고    scopus 로고
    • Induction of nonapoptotic cell death by activated Ras requires inverse regulation of Rac1 and Arf6
    • Bhanot H, Young AM, Overmeyer JH, Maltese WA. Induction of nonapoptotic cell death by activated Ras requires inverse regulation of Rac1 and Arf6. Mol Cancer Res. 2010;8:1358-74.
    • (2010) Mol Cancer Res , vol.8 , pp. 1358-1374
    • Bhanot, H.1    Young, A.M.2    Overmeyer, J.H.3    Maltese, W.A.4
  • 61
    • 0037099047 scopus 로고    scopus 로고
    • Membrane ruffling and macropinocytosis in A431 cells require cholesterol
    • Grimmer S, van Deurs B, Sandvig K. Membrane ruffling and macropinocytosis in A431 cells require cholesterol. J Cell Sci. 2002;115:2953-62.
    • (2002) J Cell Sci , vol.115 , pp. 2953-2962
    • Grimmer, S.1    Deurs, B.2    Sandvig, K.3
  • 62
    • 30344461890 scopus 로고    scopus 로고
    • Picornaviruses and cell death
    • Buenz EJ, Howe CL. Picornaviruses and cell death. Trends Microbiol. 2006;14:28-36.
    • (2006) Trends Microbiol , vol.14 , pp. 28-36
    • Buenz, E.J.1    Howe, C.L.2
  • 64
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • Maeno E, Ishizaki Y, Kanaseki T, Hazama A, Okada Y. Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis. Proc Natl Acad Sci USA. 2000;97:9487-92.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 65
    • 77951923949 scopus 로고    scopus 로고
    • Mitochondrial control of caspase-dependent and -independent cell death
    • Pradelli LA, Bénéteau M, Ricci J-E. Mitochondrial control of caspase-dependent and -independent cell death. Cell Mol Life Sci. 2010;67:1589-97.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1589-1597
    • Pradelli, L.A.1    Bénéteau, M.2    Ricci, J.-E.3
  • 66
    • 0033828987 scopus 로고    scopus 로고
    • Effector caspases are dispensable for the early nuclear morphological changes during chemical-induced apoptosis
    • Johnson VL, Ko SC, Holmstrom TH, Eriksson JE, Chow SC. Effector caspases are dispensable for the early nuclear morphological changes during chemical-induced apoptosis. J Cell Sci. 2000;113:2941-53.
    • (2000) J Cell Sci , vol.113 , pp. 2941-2953
    • Johnson, V.L.1    Ko, S.C.2    Holmstrom, T.H.3    Eriksson, J.E.4    Chow, S.C.5
  • 67
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death
    • Kroemer G, Martin SJ. Caspase-independent cell death. Nat Med. 2005;11:725-30.
    • (2005) Nat Med , vol.11 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 68
    • 70349145859 scopus 로고    scopus 로고
    • Caspase-independent pathways of programmed cell death: the unraveling of new targets of cancer therapy?
    • Constantinou C, Papas KA, Constantinou AI. Caspase-independent pathways of programmed cell death: the unraveling of new targets of cancer therapy? Curr Cancer Drug Targets. 2009;9:717-28.
    • (2009) Curr Cancer Drug Targets , vol.9 , pp. 717-728
    • Constantinou, C.1    Papas, K.A.2    Constantinou, A.I.3
  • 69
    • 0034772572 scopus 로고    scopus 로고
    • VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration
    • Hirabayashi M, Inoue K, Tanaka K, Nakadate K, Ohsawa Y, Kamei Y, et al. VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration. Cell Death Differ. 2001;8:977-84.
    • (2001) Cell Death Differ , vol.8 , pp. 977-984
    • Hirabayashi, M.1    Inoue, K.2    Tanaka, K.3    Nakadate, K.4    Ohsawa, Y.5    Kamei, Y.6
  • 70
    • 0036735015 scopus 로고    scopus 로고
    • Prion channel proteins and their role in vacuolation and neurodegenerative diseases
    • Kourie JI. Prion channel proteins and their role in vacuolation and neurodegenerative diseases. Eur Biophys J. 2002;31:409-16.
    • (2002) Eur Biophys J , vol.31 , pp. 409-416
    • Kourie, J.I.1
  • 71
    • 16844366080 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and its role in motor neuron degeneration in ALS
    • Manfredi G, Xu Z. Mitochondrial dysfunction and its role in motor neuron degeneration in ALS. Mitochondrion. 2005;5:77-87.
    • (2005) Mitochondrion , vol.5 , pp. 77-87
    • Manfredi, G.1    Xu, Z.2
  • 72
    • 79953186102 scopus 로고    scopus 로고
    • Cardiomyocyte hypertrophy, oncosis, and autophagic vacuolization predict mortality in idiopathic dilated cardiomyopathy with advanced heart failure
    • Vigliano CA, Meckert PMC, Diez M, Favaloro LE, Cortés C, Fazzi L, et al. Cardiomyocyte hypertrophy, oncosis, and autophagic vacuolization predict mortality in idiopathic dilated cardiomyopathy with advanced heart failure. J Am Coll Cardiol. 2011;57:1523-31.
    • (2011) J Am Coll Cardiol , vol.57 , pp. 1523-1531
    • Vigliano, C.A.1    Meckert, P.M.C.2    Diez, M.3    Favaloro, L.E.4    Cortés, C.5    Fazzi, L.6
  • 73
    • 67651100666 scopus 로고    scopus 로고
    • A novel role for MAP1 LC3 in nonautophagic cytoplasmic vacuolation death of cancer cells
    • Kar R, Singha PK, Venkatachalam MA, Saikumar P. A novel role for MAP1 LC3 in nonautophagic cytoplasmic vacuolation death of cancer cells. Oncogene. 2009;28:2556-68.
    • (2009) Oncogene , vol.28 , pp. 2556-2568
    • Kar, R.1    Singha, P.K.2    Venkatachalam, M.A.3    Saikumar, P.4
  • 74
    • 70350046244 scopus 로고    scopus 로고
    • Valosin containing protein associated inclusion body myopathy: abnormal vacuolization, autophagy and cell fusion in myoblasts
    • Vesa J, Su H, Watts GD, Krause S, Walter MC, Martin B, et al. Valosin containing protein associated inclusion body myopathy: abnormal vacuolization, autophagy and cell fusion in myoblasts. Neuromuscul Disord. 2009;19:766-72.
    • (2009) Neuromuscul Disord , vol.19 , pp. 766-772
    • Vesa, J.1    Su, H.2    Watts, G.D.3    Krause, S.4    Walter, M.C.5    Martin, B.6
  • 75
    • 65649151403 scopus 로고    scopus 로고
    • Sepsis induces extensive autophagic vacuolization in hepatocytes: a clinical and laboratory-based study
    • Watanabe E, Muenzer JT, Hawkins WG, Davis CG, Dixon DJ, McDunn JE, et al. Sepsis induces extensive autophagic vacuolization in hepatocytes: a clinical and laboratory-based study. Lab Invest. 2009;89:549-61.
    • (2009) Lab Invest , vol.89 , pp. 549-561
    • Watanabe, E.1    Muenzer, J.T.2    Hawkins, W.G.3    Davis, C.G.4    Dixon, D.J.5    McDunn, J.E.6
  • 76
    • 37849006735 scopus 로고    scopus 로고
    • A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release
    • Alcalá S, Klee M, Fernández J, Fleischer A, Pimentel-Muiños FX. A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release. Oncogene. 2008;27:44-54.
    • (2008) Oncogene , vol.27 , pp. 44-54
    • Alcalá, S.1    Klee, M.2    Fernández, J.3    Fleischer, A.4    Pimentel-Muiños, F.X.5
  • 77
    • 78649901091 scopus 로고    scopus 로고
    • Alternative cell death mechanisms in development and beyond
    • Yuan J, Kroemer G. Alternative cell death mechanisms in development and beyond. Genes Dev. 2010;24:2592-602.
    • (2010) Genes Dev , vol.24 , pp. 2592-2602
    • Yuan, J.1    Kroemer, G.2
  • 78
    • 84872188814 scopus 로고    scopus 로고
    • Manumycin A inhibits triple-negative breast cancer growth through LC3-mediated cytoplasmic vacuolation death
    • Singha PK, Pandeswara S, Venkatachalam MA, Saikumar P. Manumycin A inhibits triple-negative breast cancer growth through LC3-mediated cytoplasmic vacuolation death. Cell Death Dis. 2013;4:e457.
    • (2013) Cell Death Dis , vol.4 , pp. e457
    • Singha, P.K.1    Pandeswara, S.2    Venkatachalam, M.A.3    Saikumar, P.4
  • 79
    • 0034687754 scopus 로고    scopus 로고
    • An alternative, nonapoptotic form of programmed cell death
    • Sperandio S, de Belle I, Bredesen DE. An alternative, nonapoptotic form of programmed cell death. Proc Natl Acad Sci USA. 2000;97:14376-81.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14376-14381
    • Sperandio, S.1    Belle, I.2    Bredesen, D.E.3
  • 81
    • 27144503701 scopus 로고    scopus 로고
    • Vitamin D analog EB1089 triggers dramatic lysosomal changes and Beclin 1-mediated autophagic cell death
    • Høyer-Hansen M, Bastholm L, Mathiasen IS, Elling F, Jäättelä M. Vitamin D analog EB1089 triggers dramatic lysosomal changes and Beclin 1-mediated autophagic cell death. Cell Death Differ. 2005;12:1297-309.
    • (2005) Cell Death Differ , vol.12 , pp. 1297-1309
    • Høyer-Hansen, M.1    Bastholm, L.2    Mathiasen, I.S.3    Elling, F.4    Jäättelä, M.5
  • 82
    • 34548601919 scopus 로고    scopus 로고
    • Autophagic cell death induced by TrkA receptor activation in human glioblastoma cells
    • Hansen K, Wagner B, Hamel W, Schweizer M, Haag F, Westphal M, et al. Autophagic cell death induced by TrkA receptor activation in human glioblastoma cells. J Neurochem. 2007;103:259-75.
    • (2007) J Neurochem , vol.103 , pp. 259-275
    • Hansen, K.1    Wagner, B.2    Hamel, W.3    Schweizer, M.4    Haag, F.5    Westphal, M.6
  • 83
    • 84871329234 scopus 로고    scopus 로고
    • Lysosome vacuolation disrupts the completion of autophagy during norephedrine exposure in SH-SY5Y human neuroblastoma cells
    • Funakoshi T, Aki T, Unuma K, Uemura K. Lysosome vacuolation disrupts the completion of autophagy during norephedrine exposure in SH-SY5Y human neuroblastoma cells. Brain Res. 2013;1490:9-22.
    • (2013) Brain Res , vol.1490 , pp. 9-22
    • Funakoshi, T.1    Aki, T.2    Unuma, K.3    Uemura, K.4
  • 84
    • 33746166864 scopus 로고    scopus 로고
    • Disruption of autophagy at the maturation step by the carcinogen lindane is associated with the sustained mitogen-activated protein kinase/extracellular signal-regulated kinase activity
    • Corcelle E, Nebout M, Bekri S, Gauthier N, Hofman P, Poujeol P, et al. Disruption of autophagy at the maturation step by the carcinogen lindane is associated with the sustained mitogen-activated protein kinase/extracellular signal-regulated kinase activity. Cancer Res. 2006;66:6861-70.
    • (2006) Cancer Res , vol.66 , pp. 6861-6870
    • Corcelle, E.1    Nebout, M.2    Bekri, S.3    Gauthier, N.4    Hofman, P.5    Poujeol, P.6
  • 85
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • Klionsky DJ, Elazar Z, Seglen PO, Rubinsztein DC. Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy. 2008;4:849-950.
    • (2008) Autophagy , vol.4 , pp. 849-950
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 86
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero P, Bittova L, Pfeffer SR. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol. 2002;156:511-8.
    • (2002) J Cell Biol , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 87
    • 80055060433 scopus 로고    scopus 로고
    • Endo-lysosomal vesicles positive for Rab7 and Lamp1 are terminal vesicles for the transport of dextran
    • Humphries WH, Szymanski CJ, Payne CK. Endo-lysosomal vesicles positive for Rab7 and Lamp1 are terminal vesicles for the transport of dextran. PLoS ONE. 2011;6:e26626.
    • (2011) PLoS ONE , vol.6 , pp. e26626
    • Humphries, W.H.1    Szymanski, C.J.2    Payne, C.K.3
  • 88
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes
    • Vonderheit A, Helenius A. Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol. 2005;3:e233.
    • (2005) PLoS Biol , vol.3 , pp. e233
    • Vonderheit, A.1    Helenius, A.2
  • 89
    • 0033379104 scopus 로고    scopus 로고
    • Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway
    • Trischler M, Stoorvogel W, Ullrich O. Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway. J Cell Sci. 1999;112:4773-83.
    • (1999) J Cell Sci , vol.112 , pp. 4773-4783
    • Trischler, M.1    Stoorvogel, W.2    Ullrich, O.3
  • 90
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sönnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol. 2000;149:901-14.
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sönnichsen, B.1    Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 91
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • Hutagalung AH, Novick PJ. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev. 2011;91:119-49.
    • (2011) Physiol Rev , vol.91 , pp. 119-149
    • Hutagalung, A.H.1    Novick, P.J.2
  • 92
    • 33646789810 scopus 로고    scopus 로고
    • Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes
    • Johnson EE, Overmeyer JH, Gunning WT, Maltese WA. Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes. J Cell Sci. 2006;119:1219-32.
    • (2006) J Cell Sci , vol.119 , pp. 1219-1232
    • Johnson, E.E.1    Overmeyer, J.H.2    Gunning, W.T.3    Maltese, W.A.4


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