메뉴 건너뛰기




Volumn 89, Issue 17, 2015, Pages 8897-8908

ERdj5 reductase cooperates with protein disulfide isomerase to promote simian virus 40 endoplasmic reticulum membrane translocation

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN BAP31; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERDJ5; UNCLASSIFIED DRUG; CHAPERONE; DISULFIDE; HEAT SHOCK PROTEIN 40; SMALL INTERFERING RNA;

EID: 84938926543     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00941-15     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein micro 1 mediates membrane disruption
    • Chandran K, Farsetta DL, Nibert ML. 2002. Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein micro 1 mediates membrane disruption. J Virol 76:9920-9933. http://dx.doi.org/10.1128/JVI.76.19.9920-9933.2002.
    • (2002) J Virol , vol.76 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 2
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • Ivanovic T, Agosto MA, Zhang L, Chandran K, Harrison SC, Nibert ML. 2008. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles.EMBOJ 27:1289-1298. http://dx.doi.org/10.1038/emboj.2008.60.
    • (2008) EMBOJ , vol.27 , pp. 1289-1298
    • Ivanovic, T.1    Agosto, M.A.2    Zhang, L.3    Chandran, K.4    Harrison, S.C.5    Nibert, M.L.6
  • 3
    • 79952419255 scopus 로고    scopus 로고
    • Functional genetic and biophysical analyses of membrane disruption by human adenovirus
    • Moyer CL, Wiethoff CM, Maier O, Smith JG, Nemerow GR. 2011. Functional genetic and biophysical analyses of membrane disruption by human adenovirus. J Virol 85:2631-2641. http://dx.doi.org/10.1128/JVI.02321-10.
    • (2011) J Virol , vol.85 , pp. 2631-2641
    • Moyer, C.L.1    Wiethoff, C.M.2    Maier, O.3    Smith, J.G.4    Nemerow, G.R.5
  • 4
    • 75449100099 scopus 로고    scopus 로고
    • A rotavirus spike protein conformational intermediate binds lipid bilayers
    • Trask SD, Kim IS, Harrison SC, Dormitzer PR. 2010. A rotavirus spike protein conformational intermediate binds lipid bilayers. J Virol 84:1764-1770. http://dx.doi.org/10.1128/JVI.01682-09.
    • (2010) J Virol , vol.84 , pp. 1764-1770
    • Trask, S.D.1    Kim, I.S.2    Harrison, S.C.3    Dormitzer, P.R.4
  • 5
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • Wiethoff CM, Wodrich H, Gerace L, Nemerow GR. 2005. Adenovirus protein VI mediates membrane disruption following capsid disassembly. J Virol 79:1992-2000. http://dx.doi.org/10.1128/JVI.79.4.1992-2000.2005.
    • (2005) J Virol , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 6
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck D, Filman DJ, Cheng N, Steven AC, Hogle JM, Belnap DM. 2005. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol 79:7745-7755. http://dx.doi.org/10.1128/JVI.79.12.7745-7755.2005.
    • (2005) J Virol , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3    Steven, A.C.4    Hogle, J.M.5    Belnap, D.M.6
  • 7
    • 22144468063 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
    • Bubeck D, Filman DJ, Hogle JM. 2005. Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat Struct Mol Biol 12:615-618. http://dx.doi.org/10.1038/nsmb955.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 615-618
    • Bubeck, D.1    Filman, D.J.2    Hogle, J.M.3
  • 8
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, Tsai B. 2005. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 20:289-300. http://dx.doi.org/10.1016/j.molcel.2005.08.034.
    • (2005) Mol Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 9
    • 36348964305 scopus 로고    scopus 로고
    • A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane
    • Rainey-Barger EK, Magnuson B, Tsai B. 2007. A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J Virol 81:12996-13004. http://dx.doi.org/10.1128/JVI.01037-07.
    • (2007) J Virol , vol.81 , pp. 12996-13004
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3
  • 10
    • 38449106713 scopus 로고    scopus 로고
    • Penetration of nonenveloped viruses into the cytoplasm
    • Tsai B. 2007. Penetration of nonenveloped viruses into the cytoplasm. Annu Rev Cell Dev Biol 23:23-43. http://dx.doi.org/10.1146/annurev.cellbio.23.090506.123454.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 23-43
    • Tsai, B.1
  • 11
    • 79551714334 scopus 로고    scopus 로고
    • A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection
    • Walczak CP, Tsai B. 2011. A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. J Virol 85: 2386-2396. http://dx.doi.org/10.1128/JVI.01855-10.
    • (2011) J Virol , vol.85 , pp. 2386-2396
    • Walczak, C.P.1    Tsai, B.2
  • 12
    • 84897416878 scopus 로고    scopus 로고
    • A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum
    • Walczak CP, Ravindran MS, Inoue T, Tsai B. 2014. A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum. PLoS Pathog 10: e1004007. http://dx.doi.org/10.1371/journal.ppat.1004007.
    • (2014) PLoS Pathog , vol.10
    • Walczak, C.P.1    Ravindran, M.S.2    Inoue, T.3    Tsai, B.4
  • 13
    • 84876416884 scopus 로고    scopus 로고
    • A cornucopia of human polyomaviruses
    • DeCaprio JA, Garcea RL. 2013. A cornucopia of human polyomaviruses. Nat Rev Microbiol 11:264-276. http://dx.doi.org/10.1038/nrmicro2992.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 264-276
    • DeCaprio, J.A.1    Garcea, R.L.2
  • 15
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 A resolution
    • Stehle T, Gamblin SJ, Yan Y, Harrison SC. 1996. The structure of simian virus 40 refined at 3.1 A resolution. Structure 4:165-182. http://dx.doi.org/10.1016/S0969-2126(96)00020-2.
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 16
    • 0032526711 scopus 로고    scopus 로고
    • Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry
    • Chen XS, Stehle T, Harrison SC. 1998. Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry. EMBO J 17:3233-3240. http://dx.doi.org/10.1093/emboj/17.12.3233.
    • (1998) EMBO J , vol.17 , pp. 3233-3240
    • Chen, X.S.1    Stehle, T.2    Harrison, S.C.3
  • 17
    • 0042691217 scopus 로고    scopus 로고
    • Gangliosides are receptors for murine polyoma virus and SV40
    • Tsai B, Gilbert JM, Stehle T, Lencer W, Benjamin TL, Rapoport TA. 2003. Gangliosides are receptors for murine polyoma virus and SV40. EMBO J 22:4346-4355. http://dx.doi.org/10.1093/emboj/cdg439.
    • (2003) EMBO J , vol.22 , pp. 4346-4355
    • Tsai, B.1    Gilbert, J.M.2    Stehle, T.3    Lencer, W.4    Benjamin, T.L.5    Rapoport, T.A.6
  • 19
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson HA, Chen Y, Norkin LC. 1996. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol Biol Cell 7:1825-1834. http://dx.doi.org/10.1091/mbc.7.11.1825.
    • (1996) Mol Biol Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 20
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin-and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae
    • Damm EM, Pelkmans L, Kartenbeck J, Mezzacasa A, Kurzchalia T, Helenius A. 2005. Clathrin-and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J Cell Biol 168:477-488. http://dx.doi.org/10.1083/jcb.200407113.
    • (2005) J Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 22
    • 0024844490 scopus 로고
    • Endocytosis of simian virus 40 into the endoplasmic reticulum
    • Kartenbeck J, Stukenbrok H, Helenius A. 1989. Endocytosis of simian virus 40 into the endoplasmic reticulum. J Cell Biol 109:2721-2729. http://dx.doi.org/10.1083/jcb.109.6.2721.
    • (1989) J Cell Biol , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 23
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L, Kartenbeck J, Helenius A. 2001. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 3:473-483. http://dx.doi.org/10.1038/35074539.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 24
    • 79958051219 scopus 로고    scopus 로고
    • A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol
    • Inoue T, Tsai B. 2011. A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol. PLoS Pathog 7:e1002037. http://dx.doi.org/10.1371/journal.ppat.1002037.
    • (2011) PLoS Pathog , vol.7
    • Inoue, T.1    Tsai, B.2
  • 25
    • 80455143829 scopus 로고    scopus 로고
    • BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
    • Geiger R, Andritschke D, Friebe S, Herzog F, Luisoni S, Heger T, Helenius A. 2011. BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. Nat Cell Biol 13:1305-1314. http://dx.doi.org/10.1038/ncb2339.
    • (2011) Nat Cell Biol , vol.13 , pp. 1305-1314
    • Geiger, R.1    Andritschke, D.2    Friebe, S.3    Herzog, F.4    Luisoni, S.5    Heger, T.6    Helenius, A.7
  • 26
    • 84857067637 scopus 로고    scopus 로고
    • Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm
    • Kuksin D, Norkin LC. 2012. Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm. J Virol 86:1555-1562. http://dx.doi.org/10.1128/JVI.05753-11.
    • (2012) J Virol , vol.86 , pp. 1555-1562
    • Kuksin, D.1    Norkin, L.C.2
  • 27
    • 84864820752 scopus 로고    scopus 로고
    • Disassociation of the SV40 genome from capsid proteins prior to nuclear entry
    • Kuksin D, Norkin LC. 2012. Disassociation of the SV40 genome from capsid proteins prior to nuclear entry. Virol J 9:158. http://dx.doi.org/10.1186/1743-422X-9-158.
    • (2012) Virol J , vol.9 , pp. 158
    • Kuksin, D.1    Norkin, L.C.2
  • 28
    • 0036720837 scopus 로고    scopus 로고
    • Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40
    • Nakanishi A, Shum D, Morioka H, Otsuka E, Kasamatsu H. 2002. Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40. J Virol 76: 9368-9377. http://dx.doi.org/10.1128/JVI.76.18.9368-9377.2002.
    • (2002) J Virol , vol.76 , pp. 9368-9377
    • Nakanishi, A.1    Shum, D.2    Morioka, H.3    Otsuka, E.4    Kasamatsu, H.5
  • 29
    • 84872020422 scopus 로고    scopus 로고
    • How viruses use the endoplasmic reticulum for entry, replication, and assembly
    • Inoue T, Tsai B. 2013. How viruses use the endoplasmic reticulum for entry, replication, and assembly. Cold Spring Harb Perspect Biol 5:a013250. http://dx.doi.org/10.1101/cshperspect.a013250.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Inoue, T.1    Tsai, B.2
  • 30
    • 35548992416 scopus 로고    scopus 로고
    • Simian virus 40 depends on ER protein folding and quality control factors for entry into host cells
    • Schelhaas M, Malmstrom J, Pelkmans L, Haugstetter J, Ellgaard L, Grunewald K, Helenius A. 2007. Simian virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 131:516-529. http://dx.doi.org/10.1016/j.cell.2007.09.038.
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3    Haugstetter, J.4    Ellgaard, L.5    Grunewald, K.6    Helenius, A.7
  • 31
    • 84925402717 scopus 로고    scopus 로고
    • A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40
    • Inoue T, Tsai B. 2015. A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40. J Virol 89:4069-4079. http://dx.doi.org/10.1128/JVI.03552-14.
    • (2015) J Virol , vol.89 , pp. 4069-4079
    • Inoue, T.1    Tsai, B.2
  • 32
    • 84875204546 scopus 로고    scopus 로고
    • The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation
    • Williams JM, Inoue T, Banks L, Tsai B. 2013. The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation. Mol Biol Cell 24:785-795. http://dx.doi.org/10.1091/mbc.E12-07-0522.
    • (2013) Mol Biol Cell , vol.24 , pp. 785-795
    • Williams, J.M.1    Inoue, T.2    Banks, L.3    Tsai, B.4
  • 34
    • 70350005336 scopus 로고    scopus 로고
    • Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response
    • Uemura A, Oku M, Mori K, Yoshida H. 2009. Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response. J Cell Sci 122:2877-2886. http://dx.doi.org/10.1242/jcs.040584.
    • (2009) J Cell Sci , vol.122 , pp. 2877-2886
    • Uemura, A.1    Oku, M.2    Mori, K.3    Yoshida, H.4
  • 35
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 isrequiredasadisulfidereductase fordegradationofmisfoldedproteins in theER
    • Ushioda R, Hoseki J, Araki K, Jansen G, Thomas DY, Nagata K. 2008. ERdj5 isrequiredasadisulfidereductase fordegradationofmisfoldedproteins in theER. Science 321:569-572. http://dx.doi.org/10.1126/science.1159293.
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 36
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky JL, Werner ED, Dubas ME, Goeckeler JL, Kruse KB, Mc-Cracken AA. 1999. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J Biol Chem 274: 3453-3460. http://dx.doi.org/10.1074/jbc.274.6.3453.
    • (1999) J Biol Chem , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    Mc-Cracken, A.A.6
  • 37
    • 0042970598 scopus 로고    scopus 로고
    • Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP
    • Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. 2003. Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell 14:3437-3448. http://dx.doi.org/10.1091/mbc.E02-12-0847.
    • (2003) Mol Biol Cell , vol.14 , pp. 3437-3448
    • Kabani, M.1    Kelley, S.S.2    Morrow, M.W.3    Montgomery, D.L.4    Sivendran, R.5    Rose, M.D.6    Gierasch, L.M.7    Brodsky, J.L.8
  • 38
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa SI, Fewell SW, Kato Y, Brodsky JL, Endo T. 2001. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153:1061-1070. http://dx.doi.org/10.1083/jcb.153.5.1061.
    • (2001) J Cell Biol , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 39
    • 79951491416 scopus 로고    scopus 로고
    • Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5
    • Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K. 2011. Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. Mol Cell 41:432-444. http://dx.doi.org/10.1016/j.molcel.2011.01.021.
    • (2011) Mol Cell , vol.41 , pp. 432-444
    • Hagiwara, M.1    Maegawa, K.2    Suzuki, M.3    Ushioda, R.4    Araki, K.5    Matsumoto, Y.6    Hoseki, J.7    Nagata, K.8    Inaba, K.9
  • 41
    • 0038805611 scopus 로고    scopus 로고
    • Importance of Vp1 calciumbinding residues in assembly, cell entry, and nuclear entry of simian virus 40
    • Li PP, Naknanishi A, Tran MA, Ishizu K, Kawano M, Phillips M, Handa H, Liddington RC, Kasamatsu H. 2003. Importance of Vp1 calciumbinding residues in assembly, cell entry, and nuclear entry of simian virus 40. J Virol 77:7527-7538. http://dx.doi.org/10.1128/JVI.77.13.7527-7538.2003.
    • (2003) J Virol , vol.77 , pp. 7527-7538
    • Li, P.P.1    Naknanishi, A.2    Tran, M.A.3    Ishizu, K.4    Kawano, M.5    Phillips, M.6    Handa, H.7    Liddington, R.C.8    Kasamatsu, H.9
  • 42
    • 0017726207 scopus 로고
    • Uncoating and gene expression of simian virus 40 in CV-1 cell nuclei inoculated by microinjection
    • Diacumakos EG, Gershey EL. 1977. Uncoating and gene expression of simian virus 40 in CV-1 cell nuclei inoculated by microinjection. J Virol 24:903-906.
    • (1977) J Virol , vol.24 , pp. 903-906
    • Diacumakos, E.G.1    Gershey, E.L.2
  • 43
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky JL. 2012. Cleaning up: ER-associated degradation to the rescue. Cell 151:1163-1167. http://dx.doi.org/10.1016/j.cell.2012.11.012.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 44
    • 84870763849 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum-associated degradation system
    • Olzmann JA, Kopito RR, Christianson JC. 2013. The mammalian endoplasmic reticulum-associated degradation system. Cold Spring Harb Perspect Biol 5:a013185. http://dx.doi.org/10.1101/cshperspect.a013185.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Olzmann, J.A.1    Kopito, R.R.2    Christianson, J.C.3
  • 45
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: targeting proteins for degradation in the endoplasmic reticulum
    • Smith MH, Ploegh HL, Weissman JS. 2011. Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334:1086-1090. http://dx.doi.org/10.1126/science.1209235.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 46
    • 14744277407 scopus 로고    scopus 로고
    • Pairs of Vp1 cysteine residues essential for simian virus 40 infection
    • Li PP, Nakanishi A, Fontanes V, Kasamatsu H. 2005. Pairs of Vp1 cysteine residues essential for simian virus 40 infection. J Virol 79:3859-3864. http://dx.doi.org/10.1128/JVI.79.6.3859-3864.2005.
    • (2005) J Virol , vol.79 , pp. 3859-3864
    • Li, P.P.1    Nakanishi, A.2    Fontanes, V.3    Kasamatsu, H.4
  • 47
    • 84857218845 scopus 로고    scopus 로고
    • Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates
    • Grubb S, Guo L, Fisher EA, Brodsky JL. 2012. Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Mol Biol Cell 23: 520-532. http://dx.doi.org/10.1091/mbc.E11-08-0704.
    • (2012) Mol Biol Cell , vol.23 , pp. 520-532
    • Grubb, S.1    Guo, L.2    Fisher, E.A.3    Brodsky, J.L.4
  • 48
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari M, Galli C, Piccaluga V, Pieren M, Paganetti P. 2002. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J Cell Biol 158: 247-257. http://dx.doi.org/10.1083/jcb.200204122.
    • (2002) J Cell Biol , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 49
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B, Rodighiero C, Lencer WI, Rapoport TA. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104:937-948. http://dx.doi.org/10.1016/S0092-8674(01)00289-6.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 50
    • 34249069585 scopus 로고    scopus 로고
    • Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system
    • Wahlman J, DeMartino GN, Skach WR, Bulleid NJ, Brodsky JL, Johnson AE. 2007. Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system. Cell 129:943-955. http://dx.doi.org/10.1016/j.cell.2007.03.046.
    • (2007) Cell , vol.129 , pp. 943-955
    • Wahlman, J.1    DeMartino, G.N.2    Skach, W.R.3    Bulleid, N.J.4    Brodsky, J.L.5    Johnson, A.E.6
  • 51
    • 84924787742 scopus 로고    scopus 로고
    • Modulation of a pore in the capsid of JC polyomavirus reduces infectivity and prevents exposure of the minor capsid proteins
    • Nelson CD, Stroh LJ, Gee GV, O'Hara BA, Stehle T, Atwood WJ. 2015. Modulation of a pore in the capsid of JC polyomavirus reduces infectivity and prevents exposure of the minor capsid proteins. J Virol 89:3910-3921. http://dx.doi.org/10.1128/JVI.00089-15.
    • (2015) J Virol , vol.89 , pp. 3910-3921
    • Nelson, C.D.1    Stroh, L.J.2    Gee, G.V.3    O'Hara, B.A.4    Stehle, T.5    Atwood, W.J.6
  • 52
    • 84925436575 scopus 로고    scopus 로고
    • The endoplasmic reticulum membrane J protein C18 executes a distinct role in promoting simian virus 40 membrane penetration
    • Bagchi P, Walczak CP, Tsai B. 2015. The endoplasmic reticulum membrane J protein C18 executes a distinct role in promoting simian virus 40 membrane penetration. J Virol 89:4058-4068. http://dx.doi.org/10.1128/JVI.03574-14.
    • (2015) J Virol , vol.89 , pp. 4058-4068
    • Bagchi, P.1    Walczak, C.P.2    Tsai, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.