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Volumn 125, Issue , 2015, Pages 121-130

Corrigendum to: "Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines" [J Proteomics 125 (2015) 121-130] doi: 10.1016/j.jprot.2015.05.016.;Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines

Author keywords

[No Author keywords available]

Indexed keywords

ATP5B PROTEIN; BETA ACTIN; BETA TUBULIN; CHAPERONIN 60; CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE SUBUNIT IV; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 29; ENO1 PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN BETA 1; HEAT SHOCK TRANSCRIPTION FACTOR 1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HISTONE; PROTEOME; THYMOSTIMULIN; TRIOSEPHOSPHATE ISOMERASE; TRIOSEPHOSPHATE ISOMERASE 1; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 84939417418     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2015.10.012     Document Type: Erratum
Times cited : (11)

References (76)
  • 1
    • 0034458548 scopus 로고    scopus 로고
    • Deaths of children during an outbreak of hand, foot, and mouth disease in Sarawak, Malaysia: clinical and pathological characteristics of the disease. For the Outbreak Study Group
    • Chan L.G., Parashar U.D., Lye M.S., Ong F.G., Zaki S.R., Alexander J.P., et al. Deaths of children during an outbreak of hand, foot, and mouth disease in Sarawak, Malaysia: clinical and pathological characteristics of the disease. For the Outbreak Study Group. Clin. Infect. Dis. 2000, 31:678-683.
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 678-683
    • Chan, L.G.1    Parashar, U.D.2    Lye, M.S.3    Ong, F.G.4    Zaki, S.R.5    Alexander, J.P.6
  • 2
    • 0033714797 scopus 로고    scopus 로고
    • Acute encephalomyelitis during an outbreak of enterovirus type 71 infection in Taiwan: report of an autopsy case with pathologic, immunofluorescence, and molecular studies
    • Hsueh C., Jung S.M., Shih S.R., Kuo T.T., Shieh W.J., Zaki S., et al. Acute encephalomyelitis during an outbreak of enterovirus type 71 infection in Taiwan: report of an autopsy case with pathologic, immunofluorescence, and molecular studies. Mod. Pathol. 2000, 13:1200-1205.
    • (2000) Mod. Pathol. , vol.13 , pp. 1200-1205
    • Hsueh, C.1    Jung, S.M.2    Shih, S.R.3    Kuo, T.T.4    Shieh, W.J.5    Zaki, S.6
  • 3
    • 0034886767 scopus 로고    scopus 로고
    • First fatal case of enterovirus 71 infection in Hong Kong
    • Ng D.K., Law A.K., Cherk S.W., Mak K.L. First fatal case of enterovirus 71 infection in Hong Kong. Hong Kong Med. J. 2001, 7:193-196.
    • (2001) Hong Kong Med. J. , vol.7 , pp. 193-196
    • Ng, D.K.1    Law, A.K.2    Cherk, S.W.3    Mak, K.L.4
  • 4
    • 0033598371 scopus 로고    scopus 로고
    • An epidemic of enterovirus 71 infection in Taiwan. Taiwan Enterovirus Epidemic Working Group
    • Ho M., Chen E.R., Hsu K.H., Twu S.J., Chen K.T., Tsai S.F., et al. An epidemic of enterovirus 71 infection in Taiwan. Taiwan Enterovirus Epidemic Working Group. N. Engl. J. Med. 1999, 341:929-935.
    • (1999) N. Engl. J. Med. , vol.341 , pp. 929-935
    • Ho, M.1    Chen, E.R.2    Hsu, K.H.3    Twu, S.J.4    Chen, K.T.5    Tsai, S.F.6
  • 5
    • 79551604505 scopus 로고    scopus 로고
    • An enterovirus 71 epidemic in Guangdong Province of China, 2008: epidemiological, clinical, and virogenic manifestations
    • Sun L.M., Zheng H.Y., Zheng H.Z., Guo X., He J.F., Guan D.W., et al. An enterovirus 71 epidemic in Guangdong Province of China, 2008: epidemiological, clinical, and virogenic manifestations. Jpn. J. Infect. Dis. 2011, 64:13-18.
    • (2011) Jpn. J. Infect. Dis. , vol.64 , pp. 13-18
    • Sun, L.M.1    Zheng, H.Y.2    Zheng, H.Z.3    Guo, X.4    He, J.F.5    Guan, D.W.6
  • 9
    • 80052286633 scopus 로고    scopus 로고
    • Pathogenesis study of enterovirus 71 infection in rhesus monkeys
    • Zhang Y., Cui W., Liu L., Wang J., Zhao H., Liao Y., et al. Pathogenesis study of enterovirus 71 infection in rhesus monkeys. Lab. Investig. 2011, 91:1337-1350.
    • (2011) Lab. Investig. , vol.91 , pp. 1337-1350
    • Zhang, Y.1    Cui, W.2    Liu, L.3    Wang, J.4    Zhao, H.5    Liao, Y.6
  • 10
    • 33845451948 scopus 로고    scopus 로고
    • Differences in replication capacity between enterovirus 71 isolates obtained from patients with encephalitis and those obtained from patients with herpangina in Taiwan
    • Kung C.M., King C.C., Lee C.N., Huang L.M., Lee P.I., Kao C.L. Differences in replication capacity between enterovirus 71 isolates obtained from patients with encephalitis and those obtained from patients with herpangina in Taiwan. J. Med. Virol. 2007, 79:60-68.
    • (2007) J. Med. Virol. , vol.79 , pp. 60-68
    • Kung, C.M.1    King, C.C.2    Lee, C.N.3    Huang, L.M.4    Lee, P.I.5    Kao, C.L.6
  • 11
    • 1642503750 scopus 로고    scopus 로고
    • A murine oral enterovirus 71 infection model with central nervous system involvement
    • Chen Y.C., Yu C.K., Wang Y.F., Liu C.C., Su I.J., Lei H.Y. A murine oral enterovirus 71 infection model with central nervous system involvement. J. Gen. Virol. 2004, 85:69-77.
    • (2004) J. Gen. Virol. , vol.85 , pp. 69-77
    • Chen, Y.C.1    Yu, C.K.2    Wang, Y.F.3    Liu, C.C.4    Su, I.J.5    Lei, H.Y.6
  • 12
    • 3242704988 scopus 로고    scopus 로고
    • A mouse-adapted enterovirus 71 strain causes neurological disease in mice after oral infection
    • Wang Y.F., Chou C.T., Lei H.Y., Liu C.C., Wang S.M., Yan J.J., et al. A mouse-adapted enterovirus 71 strain causes neurological disease in mice after oral infection. J. Virol. 2004, 78:7916-7924.
    • (2004) J. Virol. , vol.78 , pp. 7916-7924
    • Wang, Y.F.1    Chou, C.T.2    Lei, H.Y.3    Liu, C.C.4    Wang, S.M.5    Yan, J.J.6
  • 13
    • 34548191213 scopus 로고    scopus 로고
    • Retrograde axonal transport: a major transmission route of enterovirus 71 in mice
    • Chen C.S., Yao Y.C., Lin S.C., Lee Y.P., Wang Y.F., Wang J.R., et al. Retrograde axonal transport: a major transmission route of enterovirus 71 in mice. J. Virol. 2007, 81:8996-9003.
    • (2007) J. Virol. , vol.81 , pp. 8996-9003
    • Chen, C.S.1    Yao, Y.C.2    Lin, S.C.3    Lee, Y.P.4    Wang, Y.F.5    Wang, J.R.6
  • 15
    • 7044229558 scopus 로고    scopus 로고
    • Human endothelial cell activation and apoptosis induced by enterovirus 71 infection
    • Liang C.C., Sun M.J., Lei H.Y., Chen S.H., Yu C.K., Liu C.C., et al. Human endothelial cell activation and apoptosis induced by enterovirus 71 infection. J. Med. Virol. 2004, 74:597-603.
    • (2004) J. Med. Virol. , vol.74 , pp. 597-603
    • Liang, C.C.1    Sun, M.J.2    Lei, H.Y.3    Chen, S.H.4    Yu, C.K.5    Liu, C.C.6
  • 16
    • 42949119231 scopus 로고    scopus 로고
    • The distribution of inflammation and virus in human enterovirus 71 encephalomyelitis suggests possible viral spread by neural pathways
    • Wong K.T., Munisamy B., Ong K.C., Kojima H., Noriyo N., Chua K.B., et al. The distribution of inflammation and virus in human enterovirus 71 encephalomyelitis suggests possible viral spread by neural pathways. J. Neuropathol. Exp. Neurol. 2008, 67:162-169.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 162-169
    • Wong, K.T.1    Munisamy, B.2    Ong, K.C.3    Kojima, H.4    Noriyo, N.5    Chua, K.B.6
  • 17
    • 84861303020 scopus 로고    scopus 로고
    • Human SCARB2-dependent infection by coxsackievirus A7, A14, and A16 and enterovirus 71
    • Yamayoshi S., Iizuka S., Yamashita T., Minagawa H., Mizuta K., Okamoto M., et al. Human SCARB2-dependent infection by coxsackievirus A7, A14, and A16 and enterovirus 71. J. Virol. 2012, 86:5686-5696.
    • (2012) J. Virol. , vol.86 , pp. 5686-5696
    • Yamayoshi, S.1    Iizuka, S.2    Yamashita, T.3    Minagawa, H.4    Mizuta, K.5    Okamoto, M.6
  • 18
    • 67650491431 scopus 로고    scopus 로고
    • Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71
    • Nishimura Y., Shimojima M., Tano Y., Miyamura T., Wakita T., Shimizu H. Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71. Nat. Med. 2009, 15:794-797.
    • (2009) Nat. Med. , vol.15 , pp. 794-797
    • Nishimura, Y.1    Shimojima, M.2    Tano, Y.3    Miyamura, T.4    Wakita, T.5    Shimizu, H.6
  • 19
    • 80655125503 scopus 로고    scopus 로고
    • Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity
    • Yang S.L., Chou Y.T., Wu C.N., Ho M.S. Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity. J. Virol. 2011, 85:11809-11820.
    • (2011) J. Virol. , vol.85 , pp. 11809-11820
    • Yang, S.L.1    Chou, Y.T.2    Wu, C.N.3    Ho, M.S.4
  • 20
    • 70349659503 scopus 로고    scopus 로고
    • Sialylated glycans as receptor and inhibitor of enterovirus 71 infection to DLD-1 intestinal cells
    • Yang B., Chuang H., Yang K.D. Sialylated glycans as receptor and inhibitor of enterovirus 71 infection to DLD-1 intestinal cells. Virol. J. 2009, 6:141.
    • (2009) Virol. J. , vol.6 , pp. 141
    • Yang, B.1    Chuang, H.2    Yang, K.D.3
  • 21
    • 84871962446 scopus 로고    scopus 로고
    • Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor
    • Tan C.W., Poh C.L., Sam I.C., Chan Y.F. Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor. J. Virol. 2013, 87:611-620.
    • (2013) J. Virol. , vol.87 , pp. 611-620
    • Tan, C.W.1    Poh, C.L.2    Sam, I.C.3    Chan, Y.F.4
  • 22
    • 84899089054 scopus 로고    scopus 로고
    • Cell surface vimentin is an attachment receptor for enterovirus 71
    • Du N., Cong H., Tian H., Zhang H., Zhang W., Song L., et al. Cell surface vimentin is an attachment receptor for enterovirus 71. J. Virol. 2014, 88:5816-5833.
    • (2014) J. Virol. , vol.88 , pp. 5816-5833
    • Du, N.1    Cong, H.2    Tian, H.3    Zhang, H.4    Zhang, W.5    Song, L.6
  • 23
    • 12144273494 scopus 로고    scopus 로고
    • Diverse apoptotic pathways in enterovirus 71-infected cells
    • Chang S.C., Lin J.Y., Lo L.Y., Li M.L., Shih S.R. Diverse apoptotic pathways in enterovirus 71-infected cells. J. Neurovirol. 2004, 10:338-349.
    • (2004) J. Neurovirol. , vol.10 , pp. 338-349
    • Chang, S.C.1    Lin, J.Y.2    Lo, L.Y.3    Li, M.L.4    Shih, S.R.5
  • 24
    • 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, 293:386-395.
    • (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
  • 25
    • 84881257327 scopus 로고    scopus 로고
    • Characterisation of enterovirus 71 replication kinetics in human colorectal cell line, HT29
    • Lui Y.L., Timms P., Hafner L.M., Tan T.L., Tan K.H., Tan E.L. Characterisation of enterovirus 71 replication kinetics in human colorectal cell line, HT29. Springerplus 2013, 2:267.
    • (2013) Springerplus , vol.2 , pp. 267
    • Lui, Y.L.1    Timms, P.2    Hafner, L.M.3    Tan, T.L.4    Tan, K.H.5    Tan, E.L.6
  • 26
    • 27244455727 scopus 로고    scopus 로고
    • Enterovirus 71 infection induces apoptosis in Vero cells
    • Chan Y.F., Abubakar S. Enterovirus 71 infection induces apoptosis in Vero cells. Malays. J. Pathol. 2003, 25:29-35.
    • (2003) Malays. J. Pathol. , vol.25 , pp. 29-35
    • Chan, Y.F.1    Abubakar, S.2
  • 27
    • 84858974593 scopus 로고    scopus 로고
    • Viral and host factors that contribute to pathogenicity of enterovirus 71
    • Huang H.I., Weng K.F., Shih S.R. Viral and host factors that contribute to pathogenicity of enterovirus 71. Future Microbiol 2012, 7:467-479.
    • (2012) Future Microbiol , vol.7 , pp. 467-479
    • Huang, H.I.1    Weng, K.F.2    Shih, S.R.3
  • 28
    • 84881377501 scopus 로고    scopus 로고
    • Robust antiviral responses to enterovirus 71 infection in human intestinal epithelial cells
    • Chi C., Sun Q., Wang S., Zhang Z., Li X., Cardona C.J., et al. Robust antiviral responses to enterovirus 71 infection in human intestinal epithelial cells. Virus Res. 2013, 176:53-60.
    • (2013) Virus Res. , vol.176 , pp. 53-60
    • Chi, C.1    Sun, Q.2    Wang, S.3    Zhang, Z.4    Li, X.5    Cardona, C.J.6
  • 30
    • 0032854227 scopus 로고    scopus 로고
    • Molecular detection of enteroviruses from an outbreak of hand, foot and mouth disease in Malaysia in 1997
    • Abubakar S., Chee H.Y., Shafee N., Chua K.B., Lam S.K. Molecular detection of enteroviruses from an outbreak of hand, foot and mouth disease in Malaysia in 1997. Scand. J. Infect. Dis. 1999, 31:331-335.
    • (1999) Scand. J. Infect. Dis. , vol.31 , pp. 331-335
    • Abubakar, S.1    Chee, H.Y.2    Shafee, N.3    Chua, K.B.4    Lam, S.K.5
  • 31
    • 77149178707 scopus 로고    scopus 로고
    • CBB staining protocol with higher sensitivity and mass spectrometric compatibility
    • Pink M., Verma N., Rettenmeier A.W., Schmitz-Spanke S. CBB staining protocol with higher sensitivity and mass spectrometric compatibility. Electrophoresis 2010, 31:593-598.
    • (2010) Electrophoresis , vol.31 , pp. 593-598
    • Pink, M.1    Verma, N.2    Rettenmeier, A.W.3    Schmitz-Spanke, S.4
  • 32
    • 78651324347 scopus 로고    scopus 로고
    • The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored
    • Szklarczyk D., Franceschini A., Kuhn M., Simonovic M., Roth A., Minguez P., et al. The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored. Nucleic Acids Res. 2011, 39:D561-D568.
    • (2011) Nucleic Acids Res. , vol.39 , pp. D561-D568
    • Szklarczyk, D.1    Franceschini, A.2    Kuhn, M.3    Simonovic, M.4    Roth, A.5    Minguez, P.6
  • 33
    • 84872564893 scopus 로고    scopus 로고
    • Excretion of enterovirus 71 in persons infected with hand, foot and mouth disease
    • Li J., Lin C., Qu M., Li X., Gao Z., Zhang X., et al. Excretion of enterovirus 71 in persons infected with hand, foot and mouth disease. Virol. J. 2013, 10:31.
    • (2013) Virol. J. , vol.10 , pp. 31
    • Li, J.1    Lin, C.2    Qu, M.3    Li, X.4    Gao, Z.5    Zhang, X.6
  • 34
    • 61649086141 scopus 로고    scopus 로고
    • Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins
    • Finsterbusch T., Steinfeldt T., Doberstein K., Rodner C., Mankertz A. Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins. Virology 2009, 386:122-131.
    • (2009) Virology , vol.386 , pp. 122-131
    • Finsterbusch, T.1    Steinfeldt, T.2    Doberstein, K.3    Rodner, C.4    Mankertz, A.5
  • 35
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3
    • Chandra D., Choy G., Tang D.G. Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J. Biol. Chem. 2007, 282:31289-31301.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 37
    • 77949879489 scopus 로고    scopus 로고
    • ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum
    • Coe H., Jung J., Groenendyk J., Prins D., Michalak M. ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J. Biol. Chem. 2010, 285:6725-6738.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6725-6738
    • Coe, H.1    Jung, J.2    Groenendyk, J.3    Prins, D.4    Michalak, M.5
  • 38
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard K., Szabo E., Michalak M., Opas M. Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int. Rev. Cytol. 2005, 245:91-121.
    • (2005) Int. Rev. Cytol. , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 39
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding
    • Ellgaard L., Frickel E.M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem. Biophys. 2003, 39:223-247.
    • (2003) Cell Biochem. Biophys. , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 40
    • 33749612518 scopus 로고    scopus 로고
    • Assembly of MHC class I molecules within the endoplasmic reticulum
    • Zhang Y., Williams D.B. Assembly of MHC class I molecules within the endoplasmic reticulum. Immunol. Res. 2006, 35:151-162.
    • (2006) Immunol. Res. , vol.35 , pp. 151-162
    • Zhang, Y.1    Williams, D.B.2
  • 41
    • 0034013539 scopus 로고    scopus 로고
    • Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells
    • Miyake H., Hara I., Arakawa S., Kamidono S. Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J. Cell. Biochem. 2000, 77:396-408.
    • (2000) J. Cell. Biochem. , vol.77 , pp. 396-408
    • Miyake, H.1    Hara, I.2    Arakawa, S.3    Kamidono, S.4
  • 42
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation
    • Reddy R.K., Mao C., Baumeister P., Austin R.C., Kaufman R.J., Lee A.S. Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 2003, 278:20915-20924.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 43
    • 0035882167 scopus 로고    scopus 로고
    • Apolipoprotein A-I stimulates the transport of intracellular cholesterol to cell-surface cholesterol-rich domains (caveolae)
    • Sviridov D., Fidge N., Beaumier-Gallon G., Fielding C. Apolipoprotein A-I stimulates the transport of intracellular cholesterol to cell-surface cholesterol-rich domains (caveolae). Biochem. J. 2001, 358:79-86.
    • (2001) Biochem. J. , vol.358 , pp. 79-86
    • Sviridov, D.1    Fidge, N.2    Beaumier-Gallon, G.3    Fielding, C.4
  • 44
    • 0345734205 scopus 로고    scopus 로고
    • Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry
    • Danthi P., Chow M. Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry. J. Virol. 2004, 78:33-41.
    • (2004) J. Virol. , vol.78 , pp. 33-41
    • Danthi, P.1    Chow, M.2
  • 45
    • 33645280052 scopus 로고    scopus 로고
    • Liposome-mediated transient transfection reduces cholesterol-dependent coxsackievirus infectivity
    • Wong J., Zhang J., Gao G., Esfandiarei M., Si X., Wang Y., et al. Liposome-mediated transient transfection reduces cholesterol-dependent coxsackievirus infectivity. J. Virol. Methods 2006, 133:211-218.
    • (2006) J. Virol. Methods , vol.133 , pp. 211-218
    • Wong, J.1    Zhang, J.2    Gao, G.3    Esfandiarei, M.4    Si, X.5    Wang, Y.6
  • 46
    • 80052023116 scopus 로고    scopus 로고
    • Comparative proteome analyses of host protein expression in response to enterovirus 71 and coxsackievirus A16 infections
    • Lee J.J., Seah J.B., Chow V.T., Poh C.L., Tan E.L. Comparative proteome analyses of host protein expression in response to enterovirus 71 and coxsackievirus A16 infections. J. Proteome 2011, 74:2018-2024.
    • (2011) J. Proteome , vol.74 , pp. 2018-2024
    • Lee, J.J.1    Seah, J.B.2    Chow, V.T.3    Poh, C.L.4    Tan, E.L.5
  • 47
    • 33644863314 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
    • Leong W.F., Chow V.T. Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 2006, 8:565-580.
    • (2006) Cell. Microbiol. , vol.8 , pp. 565-580
    • Leong, W.F.1    Chow, V.T.2
  • 48
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: essential regulators of actin dynamics
    • Bamburg J.R. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 1999, 15:185-230.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 50
    • 83655180829 scopus 로고    scopus 로고
    • Increased replication of respiratory syncytial virus in the presence of cytokeratin 8 and 18
    • Shirato K., Ujike M., Kawase M., Matsuyama S. Increased replication of respiratory syncytial virus in the presence of cytokeratin 8 and 18. J. Med. Virol. 2012, 84:365-370.
    • (2012) J. Med. Virol. , vol.84 , pp. 365-370
    • Shirato, K.1    Ujike, M.2    Kawase, M.3    Matsuyama, S.4
  • 51
    • 84888292851 scopus 로고    scopus 로고
    • Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins
    • Liu X., Wang Q., Chen W., Wang C. Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins. Cytokine Growth Factor Rev. 2013, 24:559-570.
    • (2013) Cytokine Growth Factor Rev. , vol.24 , pp. 559-570
    • Liu, X.1    Wang, Q.2    Chen, W.3    Wang, C.4
  • 52
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • Sadler A.J., Williams B.R. Interferon-inducible antiviral effectors. Nat. Rev. Immunol. 2008, 8:559-568.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.2
  • 53
    • 54449095457 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5' untranslated region and participates in virus replication
    • Lin J.Y., Li M.L., Huang P.N., Chien K.Y., Horng J.T., Shih S.R. Heterogeneous nuclear ribonuclear protein K interacts with the enterovirus 71 5' untranslated region and participates in virus replication. J. Gen. Virol. 2008, 89:2540-2549.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2540-2549
    • Lin, J.Y.1    Li, M.L.2    Huang, P.N.3    Chien, K.Y.4    Horng, J.T.5    Shih, S.R.6
  • 54
    • 77949568793 scopus 로고    scopus 로고
    • Delayed kinetics of poliovirus RNA synthesis in a human cell line with reduced levels of hnRNP C proteins
    • Brunner J.E., Ertel K.J., Rozovics J.M., Semler B.L. Delayed kinetics of poliovirus RNA synthesis in a human cell line with reduced levels of hnRNP C proteins. Virology 2010, 400:240-247.
    • (2010) Virology , vol.400 , pp. 240-247
    • Brunner, J.E.1    Ertel, K.J.2    Rozovics, J.M.3    Semler, B.L.4
  • 55
    • 77950851941 scopus 로고    scopus 로고
    • Mechanistic consequences of hnRNP C binding to both RNA termini of poliovirus negative-strand RNA intermediates
    • Ertel K.J., Brunner J.E., Semler B.L. Mechanistic consequences of hnRNP C binding to both RNA termini of poliovirus negative-strand RNA intermediates. J. Virol. 2010, 84:4229-4242.
    • (2010) J. Virol. , vol.84 , pp. 4229-4242
    • Ertel, K.J.1    Brunner, J.E.2    Semler, B.L.3
  • 57
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A., Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003, 40:427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 58
    • 13544269402 scopus 로고    scopus 로고
    • Internalization and trafficking mechanisms of coxsackievirus B3 in HeLa cells
    • Chung S.K., Kim J.Y., Kim I.B., Park S.I., Paek K.H., Nam J.H. Internalization and trafficking mechanisms of coxsackievirus B3 in HeLa cells. Virology 2005, 333:31-40.
    • (2005) Virology , vol.333 , pp. 31-40
    • Chung, S.K.1    Kim, J.Y.2    Kim, I.B.3    Park, S.I.4    Paek, K.H.5    Nam, J.H.6
  • 59
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler R., Zou J., Voellmy R. Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1996, 1:33-39.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 60
    • 78650957391 scopus 로고    scopus 로고
    • The essential role of clathrin-mediated endocytosis in the infectious entry of human enterovirus 71
    • Hussain K.M., Leong K.L., Ng M.M., Chu J.J. The essential role of clathrin-mediated endocytosis in the infectious entry of human enterovirus 71. J. Biol. Chem. 2011, 286:309-321.
    • (2011) J. Biol. Chem. , vol.286 , pp. 309-321
    • Hussain, K.M.1    Leong, K.L.2    Ng, M.M.3    Chu, J.J.4
  • 62
    • 67449097826 scopus 로고    scopus 로고
    • Role of microtubules in extracellular release of poliovirus
    • Taylor M.P., Burgon T.B., Kirkegaard K., Jackson W.T. Role of microtubules in extracellular release of poliovirus. J. Virol. 2009, 83:6599-6609.
    • (2009) J. Virol. , vol.83 , pp. 6599-6609
    • Taylor, M.P.1    Burgon, T.B.2    Kirkegaard, K.3    Jackson, W.T.4
  • 63
    • 84857067656 scopus 로고    scopus 로고
    • Echovirus 11 infection induces dramatic changes in the actin cytoskeleton of polarized Caco-2 cells
    • Sobo K., Stuart A.D., Rubbia-Brandt L., Brown T.D., McKee T.A. Echovirus 11 infection induces dramatic changes in the actin cytoskeleton of polarized Caco-2 cells. J. Gen. Virol. 2012, 93:475-487.
    • (2012) J. Gen. Virol. , vol.93 , pp. 475-487
    • Sobo, K.1    Stuart, A.D.2    Rubbia-Brandt, L.3    Brown, T.D.4    McKee, T.A.5
  • 64
    • 79951550023 scopus 로고    scopus 로고
    • MiR-101 regulates HSV-1 replication by targeting ATP5B
    • Zheng S.Q., Li Y.X., Zhang Y., Li X., Tang H. MiR-101 regulates HSV-1 replication by targeting ATP5B. Antivir. Res. 2011, 89:219-226.
    • (2011) Antivir. Res. , vol.89 , pp. 219-226
    • Zheng, S.Q.1    Li, Y.X.2    Zhang, Y.3    Li, X.4    Tang, H.5
  • 65
    • 84875212441 scopus 로고    scopus 로고
    • ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling
    • Chang Y., Wang S.X., Wang Y.B., Zhou J., Li W.H., Wang N., et al. ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling. FEBS Lett. 2013, 587:607-613.
    • (2013) FEBS Lett. , vol.587 , pp. 607-613
    • Chang, Y.1    Wang, S.X.2    Wang, Y.B.3    Zhou, J.4    Li, W.H.5    Wang, N.6
  • 66
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden M.G., Cantley L.C., Thompson C.B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 2009, 324:1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 67
    • 4444274231 scopus 로고    scopus 로고
    • Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores
    • Belov G.A., Lidsky P.V., Mikitas O.V., Egger D., Lukyanov K.A., Bienz K., et al. Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores. J. Virol. 2004, 78:10166-10177.
    • (2004) J. Virol. , vol.78 , pp. 10166-10177
    • Belov, G.A.1    Lidsky, P.V.2    Mikitas, O.V.3    Egger, D.4    Lukyanov, K.A.5    Bienz, K.6
  • 68
    • 80053992186 scopus 로고    scopus 로고
    • Host factors in enterovirus 71 replication
    • Shih S.R., Stollar V., Li M.L. Host factors in enterovirus 71 replication. J. Virol. 2011, 85:9658-9666.
    • (2011) J. Virol. , vol.85 , pp. 9658-9666
    • Shih, S.R.1    Stollar, V.2    Li, M.L.3
  • 69
    • 84876820281 scopus 로고    scopus 로고
    • HnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly
    • Chiou N.T., Shankarling G., Lynch K.W. hnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly. Mol. Cell 2013, 49:972-982.
    • (2013) Mol. Cell , vol.49 , pp. 972-982
    • Chiou, N.T.1    Shankarling, G.2    Lynch, K.W.3
  • 70
    • 84876318702 scopus 로고    scopus 로고
    • Translational repression and eIF4A2 activity are critical for microRNA-mediated gene regulation
    • Meijer H.A., Kong Y.W., Lu W.T., Wilczynska A., Spriggs R.V., Robinson S.W., et al. Translational repression and eIF4A2 activity are critical for microRNA-mediated gene regulation. Science 2013, 340:82-85.
    • (2013) Science , vol.340 , pp. 82-85
    • Meijer, H.A.1    Kong, Y.W.2    Lu, W.T.3    Wilczynska, A.4    Spriggs, R.V.5    Robinson, S.W.6
  • 72
    • 0037428390 scopus 로고    scopus 로고
    • Determinants for membrane association and permeabilization of the coxsackievirus 2B protein and the identification of the Golgi complex as the target organelle
    • de Jong A.S., Wessels E., Dijkman H.B., Galama J.M., Melchers W.J., Willems P.H., et al. Determinants for membrane association and permeabilization of the coxsackievirus 2B protein and the identification of the Golgi complex as the target organelle. J. Biol. Chem. 2003, 278:1012-1021.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1012-1021
    • de Jong, A.S.1    Wessels, E.2    Dijkman, H.B.3    Galama, J.M.4    Melchers, W.J.5    Willems, P.H.6
  • 73
    • 3843070861 scopus 로고    scopus 로고
    • ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain
    • MacLeod J.C., Sayer R.J., Lucocq J.M., Hubbard M.J. ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain. J. Comp. Neurol. 2004, 477:29-42.
    • (2004) J. Comp. Neurol. , vol.477 , pp. 29-42
    • MacLeod, J.C.1    Sayer, R.J.2    Lucocq, J.M.3    Hubbard, M.J.4
  • 74
    • 0027439695 scopus 로고
    • Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence
    • Ozawa M., Muramatsu T. Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J. Biol. Chem. 1993, 268:699-705.
    • (1993) J. Biol. Chem. , vol.268 , pp. 699-705
    • Ozawa, M.1    Muramatsu, T.2
  • 75
    • 84876936843 scopus 로고    scopus 로고
    • Voltage-dependent anion channels modulate mitochondrial metabolism in cancer cells: regulation by free tubulin and erastin
    • Maldonado E.N., Sheldon K.L., DeHart D.N., Patnaik J., Manevich Y., Townsend D.M., et al. Voltage-dependent anion channels modulate mitochondrial metabolism in cancer cells: regulation by free tubulin and erastin. J. Biol. Chem. 2013, 288:11920-11929.
    • (2013) J. Biol. Chem. , vol.288 , pp. 11920-11929
    • Maldonado, E.N.1    Sheldon, K.L.2    DeHart, D.N.3    Patnaik, J.4    Manevich, Y.5    Townsend, D.M.6
  • 76
    • 78049520062 scopus 로고    scopus 로고
    • Calcium flux between the endoplasmic reticulum and mitochondrion contributes to poliovirus-induced apoptosis
    • Brisac C., Teoule F., Autret A., Pelletier I., Colbere-Garapin F., Brenner C., et al. Calcium flux between the endoplasmic reticulum and mitochondrion contributes to poliovirus-induced apoptosis. J. Virol. 2010, 84:12226-12235.
    • (2010) J. Virol. , vol.84 , pp. 12226-12235
    • Brisac, C.1    Teoule, F.2    Autret, A.3    Pelletier, I.4    Colbere-Garapin, F.5    Brenner, C.6


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