메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; CYCLOHEXIMIDE; DACTINOMYCIN; FAT DROPLET; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVINOLIN; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; VIRUS PROTEIN; X BOX BINDING PROTEIN 1;

EID: 84872749486     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038202     Document Type: Article
Times cited : (59)

References (69)
  • 1
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • In: Knipe DM, Howley PM, editors, 5 ed. Philadelphia, Lippincott, Williams & Wilkins
    • Lindenbach BD, Rice CM, Thiel H-J, (2007) Flaviviridae: The viruses and their replication. In: Knipe DM, Howley PM, editors. Fields Virology 5 ed. Philadelphia Lippincott, Williams & Wilkins pp. 1101-1152.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Rice, C.M.2    Thiel, H.-J.3
  • 2
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J, (2008) Modification of intracellular membrane structures for virus replication. Nat Rev Microbiol 6: 363-374.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 3
    • 77957957039 scopus 로고    scopus 로고
    • Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories
    • den Boon JA, Ahlquist P, (2010) Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories. Annu Rev Microbiol 64: 241-256.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 241-256
    • den Boon, J.A.1    Ahlquist, P.2
  • 5
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch S, Miller S, Romero-Brey I, Merz A, Bleck CK, et al. (2009) Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5: 365-375.
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1    Miller, S.2    Romero-Brey, I.3    Merz, A.4    Bleck, C.K.5
  • 6
    • 77957201605 scopus 로고    scopus 로고
    • The Endoplasmic Reticulum Provides the Membrane Platform for Biogenesis of the Flavivirus Replication Complex
    • Gillespie LK, Hoenen A, Morgan G, Mackenzie JM, (2010) The Endoplasmic Reticulum Provides the Membrane Platform for Biogenesis of the Flavivirus Replication Complex. J Virol 84: 10438-10447.
    • (2010) J Virol , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 7
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P, (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 8
    • 15944408402 scopus 로고    scopus 로고
    • ER stress signaling by regulated proteolysis of ATF6
    • Shen J, Prywes R, (2005) ER stress signaling by regulated proteolysis of ATF6. Methods 35: 382-389.
    • (2005) Methods , vol.35 , pp. 382-389
    • Shen, J.1    Prywes, R.2
  • 9
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M, Kaufman RJ, (2005) ER stress and the unfolded protein response. Mutat Res 569: 29-63.
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 10
    • 34247111608 scopus 로고    scopus 로고
    • eIF2a Phosphorylation in Cellular Response and Disease
    • In: Mathews MB, Sonemberg N, Hershey, J.W.B, editors, Cold Spring Harbor, New York, Cold Spring Harbor Laboratory Press
    • Ron D, Harding HP, (2007) eIF2a Phosphorylation in Cellular Response and Disease. In: Mathews MB, Sonemberg N, Hershey, J.W.B, editors. Translational Control in Biology and Medicine Cold Spring Harbor, New York Cold Spring Harbor Laboratory Press pp. 345-368.
    • (2007) Translational Control in Biology and Medicine , pp. 345-368
    • Ron, D.1    Harding, H.P.2
  • 11
    • 3142658576 scopus 로고    scopus 로고
    • XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation
    • Shaffer AL, Shapiro-Shelef M, Iwakoshi NN, Lee AH, Qian SB, et al. (2004) XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21: 81-93.
    • (2004) Immunity , vol.21 , pp. 81-93
    • Shaffer, A.L.1    Shapiro-Shelef, M.2    Iwakoshi, N.N.3    Lee, A.H.4    Qian, S.B.5
  • 12
    • 67650000500 scopus 로고    scopus 로고
    • ATF6{alpha} induces XBP1-independent expansion of the endoplasmic reticulum
    • Bommiasamy H, Back SH, Fagone P, Lee K, Meshinchi S, et al. (2009) ATF6{alpha} induces XBP1-independent expansion of the endoplasmic reticulum. J Cell Sci 122: 1626-1636.
    • (2009) J Cell Sci , vol.122 , pp. 1626-1636
    • Bommiasamy, H.1    Back, S.H.2    Fagone, P.3    Lee, K.4    Meshinchi, S.5
  • 13
    • 5444222234 scopus 로고    scopus 로고
    • XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum
    • Sriburi R, Jackowski S, Mori K, Brewer JW, (2004) XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J Cell Biol 167: 35-41.
    • (2004) J Cell Biol , vol.167 , pp. 35-41
    • Sriburi, R.1    Jackowski, S.2    Mori, K.3    Brewer, J.W.4
  • 14
    • 34147172715 scopus 로고    scopus 로고
    • Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis
    • Sriburi R, Bommiasamy H, Buldak GL, Robbins GR, Frank M, et al. (2007) Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis. J Biol Chem 282: 7024-7034.
    • (2007) J Biol Chem , vol.282 , pp. 7024-7034
    • Sriburi, R.1    Bommiasamy, H.2    Buldak, G.L.3    Robbins, G.R.4    Frank, M.5
  • 15
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski DT, Arnold SM, Miller CN, Wu J, Li J, et al. (2006) Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol 4: e374.
    • (2006) PLoS Biol , vol.4
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3    Wu, J.4    Li, J.5
  • 17
    • 0028960739 scopus 로고
    • Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13
    • Hua X, Wu J, Goldstein JL, Brown MS, Hobbs HH, (1995) Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13. Genomics 25: 667-673.
    • (1995) Genomics , vol.25 , pp. 667-673
    • Hua, X.1    Wu, J.2    Goldstein, J.L.3    Brown, M.S.4    Hobbs, H.H.5
  • 18
    • 0033618342 scopus 로고    scopus 로고
    • Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
    • Zelenski NG, Rawson RB, Brown MS, Goldstein JL, (1999) Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins. J Biol Chem 274: 21973-21980.
    • (1999) J Biol Chem , vol.274 , pp. 21973-21980
    • Zelenski, N.G.1    Rawson, R.B.2    Brown, M.S.3    Goldstein, J.L.4
  • 19
    • 0033529560 scopus 로고    scopus 로고
    • Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins
    • Espenshade PJ, Cheng D, Goldstein JL, Brown MS, (1999) Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins. J Biol Chem 274: 22795-22804.
    • (1999) J Biol Chem , vol.274 , pp. 22795-22804
    • Espenshade, P.J.1    Cheng, D.2    Goldstein, J.L.3    Brown, M.S.4
  • 20
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J, Rawson RB, Komuro R, Chen X, Dave UP, et al. (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6: 1355-1364.
    • (2000) Mol Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5
  • 21
    • 33847709027 scopus 로고    scopus 로고
    • SREBP in signal transduction: cholesterol metabolism and beyond
    • Bengoechea-Alonso MT, Ericsson J, (2007) SREBP in signal transduction: cholesterol metabolism and beyond. Curr Opin Cell Biol 19: 215-222.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 215-222
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 22
    • 49649102821 scopus 로고    scopus 로고
    • Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis
    • Murray CL, Jones CT, Rice CM, (2008) Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis. Nat Rev Microbiol 6: 699-708.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 699-708
    • Murray, C.L.1    Jones, C.T.2    Rice, C.M.3
  • 23
    • 63449100931 scopus 로고    scopus 로고
    • Chapter 6: cubic membranes the missing dimension of cell membrane organization
    • Almsherqi ZA, Landh T, Kohlwein SD, Deng Y, (2009) Chapter 6: cubic membranes the missing dimension of cell membrane organization. Int Rev Cell Mol Biol 274: 275-342.
    • (2009) Int Rev Cell Mol Biol , vol.274 , pp. 275-342
    • Almsherqi, Z.A.1    Landh, T.2    Kohlwein, S.D.3    Deng, Y.4
  • 24
    • 64649101780 scopus 로고    scopus 로고
    • Pathogenesis of flavivirus infections: using and abusing the host cell
    • Fernandez-Garcia MD, Mazzon M, Jacobs M, Amara A, (2009) Pathogenesis of flavivirus infections: using and abusing the host cell. Cell Host Microbe 5: 318-328.
    • (2009) Cell Host Microbe , vol.5 , pp. 318-328
    • Fernandez-Garcia, M.D.1    Mazzon, M.2    Jacobs, M.3    Amara, A.4
  • 25
    • 77954315602 scopus 로고    scopus 로고
    • Do viruses subvert cholesterol homeostasis to induce host cubic membranes?
    • Deng Y, Almsherqi ZA, Ng MM, Kohlwein SD, (2010) Do viruses subvert cholesterol homeostasis to induce host cubic membranes? Trends Cell Biol 20: 371-379.
    • (2010) Trends Cell Biol , vol.20 , pp. 371-379
    • Deng, Y.1    Almsherqi, Z.A.2    Ng, M.M.3    Kohlwein, S.D.4
  • 26
    • 79954601093 scopus 로고    scopus 로고
    • Dengue Virus Modulates the Unfolded Protein Response in a Time-dependent Manner
    • Pena J, Harris E, (2011) Dengue Virus Modulates the Unfolded Protein Response in a Time-dependent Manner. J Biol Chem 286: 14226-14236.
    • (2011) J Biol Chem , vol.286 , pp. 14226-14236
    • Pena, J.1    Harris, E.2
  • 27
    • 0030809393 scopus 로고    scopus 로고
    • Location of the internal ribosome entry site in the 5′ non-coding region of the immunoglobulin heavy-chain binding protein (BiP) mRNA: evidence for specific RNA-protein interactions
    • Yang Q, Sarnow P, (1997) Location of the internal ribosome entry site in the 5′ non-coding region of the immunoglobulin heavy-chain binding protein (BiP) mRNA: evidence for specific RNA-protein interactions. Nucleic Acids Res 25: 2800-2807.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2800-2807
    • Yang, Q.1    Sarnow, P.2
  • 28
    • 0343088819 scopus 로고
    • Translation of glucose-regulated protein 78/immunoglobulin heavy-chain binding protein mRNA is increased in poliovirus-infected cells at a time when cap-dependent translation of cellular mRNAs is inhibited
    • Sarnow P, (1989) Translation of glucose-regulated protein 78/immunoglobulin heavy-chain binding protein mRNA is increased in poliovirus-infected cells at a time when cap-dependent translation of cellular mRNAs is inhibited. Proc Natl Acad of Sci U S A 86: 5795-5799.
    • (1989) Proc Natl Acad of Sci U S A , vol.86 , pp. 5795-5799
    • Sarnow, P.1
  • 29
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • Lee AH, Scapa EF, Cohen DE, Glimcher LH, (2008) Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 320: 1492-1496.
    • (2008) Science , vol.320 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 30
    • 0027139362 scopus 로고
    • SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element
    • Hua X, Yokoyama C, Wu J, Briggs MR, Brown MS, et al. (1993) SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element. Proc Natl Acad Sci U S A 90: 11603-11607.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11603-11607
    • Hua, X.1    Yokoyama, C.2    Wu, J.3    Briggs, M.R.4    Brown, M.S.5
  • 31
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • Sakai J, Duncan EA, Rawson RB, Hua X, Brown MS, et al. (1996) Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 85: 1037-1046.
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5
  • 32
    • 0032104180 scopus 로고    scopus 로고
    • Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2
    • Horton JD, Shimomura I, Brown MS, Hammer RE, Goldstein JL, et al. (1998) Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2. J Clin Invest 101: 2331-2339.
    • (1998) J Clin Invest , vol.101 , pp. 2331-2339
    • Horton, J.D.1    Shimomura, I.2    Brown, M.S.3    Hammer, R.E.4    Goldstein, J.L.5
  • 33
    • 34548220998 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress causes the activation of sterol regulatory element binding protein-2
    • Colgan SM, Tang D, Werstuck GH, Austin RC, (2007) Endoplasmic reticulum stress causes the activation of sterol regulatory element binding protein-2. Int J Biochem Cell Biol 39: 1843-1851.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1843-1851
    • Colgan, S.M.1    Tang, D.2    Werstuck, G.H.3    Austin, R.C.4
  • 34
    • 0022540905 scopus 로고
    • Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope
    • Pathak RK, Luskey KL, Anderson RG, (1986) Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope. J Cell Biol 102: 2158-2168.
    • (1986) J Cell Biol , vol.102 , pp. 2158-2168
    • Pathak, R.K.1    Luskey, K.L.2    Anderson, R.G.3
  • 35
    • 34848900462 scopus 로고    scopus 로고
    • Cholesterol manipulation by West Nile virus perturbs the cellular immune response
    • Mackenzie JM, Khromykh AA, Parton RG, (2007) Cholesterol manipulation by West Nile virus perturbs the cellular immune response. Cell Host Microbe 2: 229-239.
    • (2007) Cell Host Microbe , vol.2 , pp. 229-239
    • Mackenzie, J.M.1    Khromykh, A.A.2    Parton, R.G.3
  • 36
    • 45749091387 scopus 로고    scopus 로고
    • Cholesterol Effectively Blocks Entry of Flavivirus
    • Lee C-J, Lin H-R, Liao C-L, Lin Y-L, (2008) Cholesterol Effectively Blocks Entry of Flavivirus. J Virol 82: 6470-6480.
    • (2008) J Virol , vol.82 , pp. 6470-6480
    • Lee, C.-J.1    Lin, H.-R.2    Liao, C.-L.3    Lin, Y.-L.4
  • 37
    • 43949122204 scopus 로고    scopus 로고
    • West Nile virus entry requires cholesterol-rich membrane microdomains and is independent of alphavbeta3 integrin
    • Medigeshi GR, Hirsch AJ, Streblow DN, Nikolich-Zugich J, Nelson JA, (2008) West Nile virus entry requires cholesterol-rich membrane microdomains and is independent of alphavbeta3 integrin. J Virol 82: 5212-5219.
    • (2008) J Virol , vol.82 , pp. 5212-5219
    • Medigeshi, G.R.1    Hirsch, A.J.2    Streblow, D.N.3    Nikolich-Zugich, J.4    Nelson, J.A.5
  • 38
    • 67349187399 scopus 로고    scopus 로고
    • Cholesterol biosynthesis modulation regulates dengue viral replication
    • Rothwell C, Lebreton A, Young Ng C, Lim JY, Liu W, et al. (2009) Cholesterol biosynthesis modulation regulates dengue viral replication. Virology 389: 8-19.
    • (2009) Virology , vol.389 , pp. 8-19
    • Rothwell, C.1    Lebreton, A.2    Young Ng, C.3    Lim, J.Y.4    Liu, W.5
  • 40
  • 41
    • 0036321944 scopus 로고    scopus 로고
    • Hijacking the translation apparatus by RNA viruses
    • Bushell M, Sarnow P, (2002) Hijacking the translation apparatus by RNA viruses. J Cell Biol 158: 395-399.
    • (2002) J Cell Biol , vol.158 , pp. 395-399
    • Bushell, M.1    Sarnow, P.2
  • 42
    • 0037333760 scopus 로고    scopus 로고
    • Translation initiation and viral tricks
    • Schneider RJ, Mohr I, (2003) Translation initiation and viral tricks. Trends Biochem Sci 28: 130-136.
    • (2003) Trends Biochem Sci , vol.28 , pp. 130-136
    • Schneider, R.J.1    Mohr, I.2
  • 43
    • 5644258600 scopus 로고    scopus 로고
    • Viral RNA replication in association with cellular membranes
    • Salonen A, Ahola T, Kaariainen L, (2005) Viral RNA replication in association with cellular membranes. Curr Top Microbiol Immunol 285: 139-173.
    • (2005) Curr Top Microbiol Immunol , vol.285 , pp. 139-173
    • Salonen, A.1    Ahola, T.2    Kaariainen, L.3
  • 44
    • 26944495290 scopus 로고    scopus 로고
    • Wrapping things up about virus RNA replication
    • Mackenzie J, (2005) Wrapping things up about virus RNA replication. Traffic 6: 967-977.
    • (2005) Traffic , vol.6 , pp. 967-977
    • Mackenzie, J.1
  • 45
    • 12344251814 scopus 로고    scopus 로고
    • Translational control in virus-infected cells: models for cellular stress responses
    • Clemens MJ, (2005) Translational control in virus-infected cells: models for cellular stress responses. Semin Cell Dev Biol 16: 13-20.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 13-20
    • Clemens, M.J.1
  • 46
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile Virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie JM, (2006) Regulated cleavages at the West Nile Virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80: 4623-4632.
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 47
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Miller S, Kastner S, Krijnse-Locker J, Buhler S, Bartenschlager R, (2007) The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J Biol Chem 282: 8873-8882.
    • (2007) J Biol Chem , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 48
    • 78649398569 scopus 로고    scopus 로고
    • Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B
    • Gouttenoire J, Roingeard P, Penin F, Moradpour D Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4BJVirol84:12529-1, (2537).
    • J Virol , vol.84 , pp. 12529-12531
    • Gouttenoire, J.1    Roingeard, P.2    Penin, F.3    Moradpour, D.4
  • 49
    • 1842850947 scopus 로고    scopus 로고
    • The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure
    • Chua JJE, Ng MML, Chow VTK, (2004) The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure. Virus Research 102: 151-163.
    • (2004) Virus Research , vol.102 , pp. 151-163
    • Chua, J.J.E.1    Ng, M.M.L.2    Chow, V.T.K.3
  • 50
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D, Wolk B, Gosert R, Bianchi L, Blum HE, et al. (2002) Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol 76: 5974-5984.
    • (2002) J Virol , vol.76 , pp. 5974-5984
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5
  • 51
    • 0141646834 scopus 로고
    • Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Chin DJ, Luskey KL, Anderson RG, Faust JR, Goldstein JL, et al. (1982) Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc Natl Acad Sci U S A 79: 1185-1189.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 1185-1189
    • Chin, D.J.1    Luskey, K.L.2    Anderson, R.G.3    Faust, J.R.4    Goldstein, J.L.5
  • 52
    • 0029993184 scopus 로고    scopus 로고
    • Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection
    • Yamamoto A, Masaki R, Tashiro Y, (1996) Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection. J Cell Sci 109 (Pt 7): 1727-1738.
    • (1996) J Cell Sci , vol.109 , Issue.Pt 7 , pp. 1727-1738
    • Yamamoto, A.1    Masaki, R.2    Tashiro, Y.3
  • 53
    • 0242266921 scopus 로고    scopus 로고
    • Formation of stacked ER cisternae by low affinity protein interactions
    • Snapp EL, Hegde RS, Francolini M, Lombardo F, Colombo S, et al. (2003) Formation of stacked ER cisternae by low affinity protein interactions. J Cell Biol 163: 257-269.
    • (2003) J Cell Biol , vol.163 , pp. 257-269
    • Snapp, E.L.1    Hegde, R.S.2    Francolini, M.3    Lombardo, F.4    Colombo, S.5
  • 54
    • 0344416996 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction
    • Sandig G, Kargel E, Menzel R, Vogel F, Zimmer T, et al. (1999) Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction. Drug Metab Rev 31: 393-410.
    • (1999) Drug Metab Rev , vol.31 , pp. 393-410
    • Sandig, G.1    Kargel, E.2    Menzel, R.3    Vogel, F.4    Zimmer, T.5
  • 55
    • 0038498128 scopus 로고    scopus 로고
    • Transmembrane lipid transfer is crucial for providing neutral lipids during very low density lipoprotein assembly in endoplasmic reticulum
    • Higashi Y, Itabe H, Fukase H, Mori M, Fujimoto Y, et al. (2003) Transmembrane lipid transfer is crucial for providing neutral lipids during very low density lipoprotein assembly in endoplasmic reticulum. J Biol Chem 278: 21450-21458.
    • (2003) J Biol Chem , vol.278 , pp. 21450-21458
    • Higashi, Y.1    Itabe, H.2    Fukase, H.3    Mori, M.4    Fujimoto, Y.5
  • 56
    • 0142027805 scopus 로고    scopus 로고
    • Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes
    • Horton JD, Shah NA, Warrington JA, Anderson NN, Park SW, et al. (2003) Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc Natl Acad Sci U S A 100: 12027-12032.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12027-12032
    • Horton, J.D.1    Shah, N.A.2    Warrington, J.A.3    Anderson, N.N.4    Park, S.W.5
  • 57
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton NS, Perera R, Berger KL, Khadka S, Lacount DJ, et al. (2010) Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc Natl Acad Sci U S A 107: 17345-17350.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5
  • 58
    • 79955448291 scopus 로고    scopus 로고
    • The birth and life of lipid droplets: learning from the hepatitis C virus
    • Roingeard P, Depla M, (2011) The birth and life of lipid droplets: learning from the hepatitis C virus. Biol Cell 103: 223-231.
    • (2011) Biol Cell , vol.103 , pp. 223-231
    • Roingeard, P.1    Depla, M.2
  • 59
    • 34548316984 scopus 로고    scopus 로고
    • The lipid droplet is an important organelle for hepatitis C virus production
    • Miyanari Y, Atsuzawa K, Usuda N, Watashi K, Hishiki T, et al. (2007) The lipid droplet is an important organelle for hepatitis C virus production. Nat Cell Biol 9: 1089-1097.
    • (2007) Nat Cell Biol , vol.9 , pp. 1089-1097
    • Miyanari, Y.1    Atsuzawa, K.2    Usuda, N.3    Watashi, K.4    Hishiki, T.5
  • 60
    • 47649114826 scopus 로고    scopus 로고
    • Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule- and dynein-dependent manner
    • Boulant S, Douglas MW, Moody L, Budkowska A, Targett-Adams P, et al. (2008) Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule- and dynein-dependent manner. Traffic 9: 1268-1282.
    • (2008) Traffic , vol.9 , pp. 1268-1282
    • Boulant, S.1    Douglas, M.W.2    Moody, L.3    Budkowska, A.4    Targett-Adams, P.5
  • 61
    • 50249107793 scopus 로고    scopus 로고
    • Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy
    • Roingeard P, Hourioux C, Blanchard E, Prensier G, (2008) Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy. Histochem Cell Biol 130: 561-566.
    • (2008) Histochem Cell Biol , vol.130 , pp. 561-566
    • Roingeard, P.1    Hourioux, C.2    Blanchard, E.3    Prensier, G.4
  • 62
    • 79952407316 scopus 로고    scopus 로고
    • West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion
    • Ambrose RL, Mackenzie JM, (2011) West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion. J Virol 85: 2723-2732.
    • (2011) J Virol , vol.85 , pp. 2723-2732
    • Ambrose, R.L.1    Mackenzie, J.M.2
  • 63
    • 79959370167 scopus 로고    scopus 로고
    • Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation
    • Hapala I, Marza E, Ferreira T, (2011) Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation. Biol Cell 103: 271-285.
    • (2011) Biol Cell , vol.103 , pp. 271-285
    • Hapala, I.1    Marza, E.2    Ferreira, T.3
  • 65
    • 78349237370 scopus 로고    scopus 로고
    • Dengue Virus-Induced Autophagy Regulates Lipid Metabolism
    • Heaton NS, Randall G, (2010) Dengue Virus-Induced Autophagy Regulates Lipid Metabolism. Cell Host Microbe 8: 422-432.
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 66
    • 79958851217 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum neutral lipid hydrolases
    • Quiroga AD, Lehner R, (2011) Role of endoplasmic reticulum neutral lipid hydrolases. Trends Endocrinol Metab 22: 218-225.
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 218-225
    • Quiroga, A.D.1    Lehner, R.2
  • 67
    • 70350400618 scopus 로고    scopus 로고
    • Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct role in the emergence and regression of lipid droplets
    • Zehmer JK, Bartz R, Bisel B, Liu P, Seemann J, et al. (2009) Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct role in the emergence and regression of lipid droplets. J Cell Sci 122: 3694-3702.
    • (2009) J Cell Sci , vol.122 , pp. 3694-3702
    • Zehmer, J.K.1    Bartz, R.2    Bisel, B.3    Liu, P.4    Seemann, J.5
  • 68
    • 0024404483 scopus 로고
    • Use of a selectable marker regulated by alpha interferon to obtain mutations in the signaling pathway
    • Pellegrini S, John J, Shearer M, Kerr IM, Stark GR, (1989) Use of a selectable marker regulated by alpha interferon to obtain mutations in the signaling pathway. Mol Cell Biol 9: 4605-4612.
    • (1989) Mol Cell Biol , vol.9 , pp. 4605-4612
    • Pellegrini, S.1    John, J.2    Shearer, M.3    Kerr, I.M.4    Stark, G.R.5
  • 69
    • 0034101043 scopus 로고    scopus 로고
    • Modulation of Dengue Virus Infection in Human Cells by Alpha, Beta, and Gamma Interferons
    • Diamond MS, Roberts TG, Edgil D, Lu B, Ernst J, et al. (2000) Modulation of Dengue Virus Infection in Human Cells by Alpha, Beta, and Gamma Interferons. J Virol 74: 4957-4966.
    • (2000) J Virol , vol.74 , pp. 4957-4966
    • Diamond, M.S.1    Roberts, T.G.2    Edgil, D.3    Lu, B.4    Ernst, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.