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Volumn 83, Issue 19, 2009, Pages 9923-9939

Characterization of hepatitis C virus core protein multimerization and membrane envelopment: Revelation of a cascade of core-membrane interactions

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; GENOMIC DNA; PROTEINASE K;

EID: 70349284497     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00066-09     Document Type: Article
Times cited : (25)

References (78)
  • 1
    • 0036301679 scopus 로고    scopus 로고
    • Processing of the Hepatitis C virus precursor protein expressed in the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/S0006-291X(02)00635-6, PII S0006291X02006356
    • Acosta-Rivero, N., A. Musacchio, L. Lorenzo, C. Alvarez, and J. Morales. 2002. Processing of the hepatitis C virus precursor protein expressed in the methylotrophic yeast Pichia pastoris. Biochem. Biophys. Res. Commun. 295:81-84. (Pubitemid 34743778)
    • (2002) Biochemical and Biophysical Research Communications , vol.295 , Issue.1 , pp. 81-84
    • Acosta-Rivero, N.1    Musacchio, A.2    Lorenzo, L.3    Alvarez, C.4    Morales, J.5
  • 4
    • 11144246127 scopus 로고    scopus 로고
    • Novel insights into hepatitis C virus replication and persistence
    • Bartenschlager, R., M. Frese, and T. Pietschmann. 2004. Novel insights into hepatitis C virus replication and persistence. Adv. Virus Res. 63:71-180.
    • (2004) Adv. Virus Res. , vol.63 , pp. 71-180
    • Bartenschlager, R.1    Frese, M.2    Pietschmann, T.3
  • 5
    • 0033920795 scopus 로고    scopus 로고
    • Replication of hepatitis C virus
    • Bartenschlager, R., and V. Lohmann. 2000. Replication of hepatitis C virus. J. Gen. Virol. 81:1631-1648.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1631-1648
    • Bartenschlager, R.1    Lohmann, V.2
  • 6
    • 0031977996 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins assemble into viruslike particles in insect cells
    • Baumert, T. F., S. Ito, D. T. Wong, and T. J. Liang. 1998. Hepatitis C virus structural proteins assemble into viruslike particles in insect cells. J. Virol. 72:3827-3836. (Pubitemid 28188682)
    • (1998) Journal of Virology , vol.72 , Issue.5 , pp. 3827-3836
    • Baumert, T.F.1    Ito, S.2    Wong, D.T.3    Liang, T.J.4
  • 9
    • 0034623816 scopus 로고    scopus 로고
    • Efficient initiation of HCV RNA replication in cell culture
    • Blight, K. J., A. A. Kolykhalov, and C. M. Rice. 2000. Efficient initiation of HCV RNA replication in cell culture. Science 290:1972-1974.
    • (2000) Science , vol.290 , pp. 1972-1974
    • Blight, K.J.1    Kolykhalov, A.A.2    Rice, C.M.3
  • 10
    • 0036893332 scopus 로고    scopus 로고
    • Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication
    • Blight, K. J., J. A. McKeating, and C. M. Rice. 2002. Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J. Virol. 76:13001-13014.
    • (2002) J. Virol. , vol.76 , pp. 13001-13014
    • Blight, K.J.1    McKeating, J.A.2    Rice, C.M.3
  • 12
    • 23844530172 scopus 로고    scopus 로고
    • Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features
    • DOI 10.1128/JVI.79.17.11353-11365.2005
    • Boulant, S., C. Vanbelle, C. Ebel, F. Penin, and J. P. Lavergne. 2005. Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features. J. Virol. 79:11353-11365. (Pubitemid 41170677)
    • (2005) Journal of Virology , vol.79 , Issue.17 , pp. 11353-11365
    • Boulant, S.1    Vanbelle, C.2    Ebel, C.3    Penin, F.4    Lavergne, J.-P.5
  • 13
    • 33645219694 scopus 로고    scopus 로고
    • Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of the severe acute respiratory syndrome coronavirus
    • Chan, W. E., C. K. Chuang, S. H. Yeh, M. S. Chang, and S. S. Chen. 2006. Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of the severe acute respiratory syndrome coronavirus. J. Virol. 80:3225-3237.
    • (2006) J. Virol. , vol.80 , pp. 3225-3237
    • Chan, W.E.1    Chuang, C.K.2    Yeh, S.H.3    Chang, M.S.4    Chen, S.S.5
  • 15
    • 0034812854 scopus 로고    scopus 로고
    • Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41
    • Chen, S. S., S. F. Lee, and C. T. Wang. 2001. Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41. J. Virol. 75:9925-9938.
    • (2001) J. Virol. , vol.75 , pp. 9925-9938
    • Chen, S.S.1    Lee, S.F.2    Wang, C.T.3
  • 16
    • 0027500162 scopus 로고
    • Membrane association of functional vesicular stomatitis virus matrix protein in vivo
    • Chong, L. D., and J. K. Rose. 1993. Membrane association of functional vesicular stomatitis virus matrix protein in vivo. J. Virol. 67:407-414.
    • (1993) J. Virol. , vol.67 , pp. 407-414
    • Chong, L.D.1    Rose, J.K.2
  • 17
    • 0029819555 scopus 로고    scopus 로고
    • Rab4 and cellubrevin define different early endosome populations on the pathway of transferrin receptor recycling
    • Daro, E., P. van der Sluijs, T. Galli, and I. Mellman. 1996. Rab4 and cellubrevin define different early endosome populations on the pathway of transferrin receptor recycling. Proc. Natl. Acad. Sci. USA 93:9559-9564.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9559-9564
    • Daro, E.1    Van Der Sluijs, P.2    Galli, T.3    Mellman, I.4
  • 18
    • 0036889344 scopus 로고    scopus 로고
    • Generation of hepatitis C virus-like particles by use of a recombinant vesicular stomatitis virus vector
    • Ezelle, H. J., D. Markovic, and G. N. Barber. 2002. Generation of hepatitis C virus-like particles by use of a recombinant vesicular stomatitis virus vector. J. Virol. 76:12325-12334.
    • (2002) J. Virol. , vol.76 , pp. 12325-12334
    • Ezelle, H.J.1    Markovic, D.2    Barber, G.N.3
  • 20
    • 33750698300 scopus 로고    scopus 로고
    • Differential biophysical properties of infectious intracellular and secreted hepatitis C virus particles
    • DOI 10.1128/JVI.01150-06
    • Gastaminza, P., S. B. Kapadia, and F. V. Chisari. 2006. Differential biophysical properties of infectious intracellular and secreted hepatitis C virus particles. J. Virol. 80:11074-11081. (Pubitemid 44706548)
    • (2006) Journal of Virology , vol.80 , Issue.22 , pp. 11074-11081
    • Gastaminza, P.1    Kapadia, S.B.2    Chisari, F.V.3
  • 21
    • 17344381535 scopus 로고    scopus 로고
    • Hepatitis C virus biology
    • Giannini, C., and C. Bréchot. 2003. Hepatitis C virus biology. Cell Death Differ. 10(Suppl. 1):S27-S38.
    • (2003) Cell Death Differ. , vol.10 , Issue.SUPPL. 1
    • Giannini, C.1    Bréchot, C.2
  • 22
    • 33744938142 scopus 로고    scopus 로고
    • Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines
    • Grigorov, B., F. Arcanger, P. Roingeard, J. L. Darlix, and D. Muriaux. 2006. Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J. Mol. Biol. 359:848-862.
    • (2006) J. Mol. Biol. , vol.359 , pp. 848-862
    • Grigorov, B.1    Arcanger, F.2    Roingeard, P.3    Darlix, J.L.4    Muriaux, D.5
  • 23
    • 0037040227 scopus 로고    scopus 로고
    • The domains required to direct core proteins of hepatitis C virus and GB virus-B to lipid droplets share common features with plant oleosin proteins
    • Hope, R. G., D. J. Murphy, and J. McLauchlan. 2002. The domains required to direct core proteins of hepatitis C virus and GB virus-B to lipid droplets share common features with plant oleosin proteins. J. Biol. Chem. 277:4261-4270.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4261-4270
    • Hope, R.G.1    Murphy, D.J.2    McLauchlan, J.3
  • 24
    • 0036190918 scopus 로고    scopus 로고
    • Selectable subgenomic and genome-length dicistronic RNAs derived from an infectious molecular clone of the HCV-N strain of hepatitis C virus replicate efficiently in cultured Huh7 cells
    • DOI 10.1128/JVI.76.6.2997-3006.2002
    • Ikeda, M., M. Yi, K. Li, and S. M. Lemon. 2002. Selectable subgenomic and genome-length dicistronic RNAs derived from an infectious molecular clone of the HCV-N strain of hepatitis C virus replicate efficiently in cultured Huh7 cells. J. Virol. 76:2997-3006. (Pubitemid 34184884)
    • (2002) Journal of Virology , vol.76 , Issue.6 , pp. 2997-3006
    • Ikeda, M.1    Yi, M.2    Li, K.3    Lemon, S.M.4
  • 25
    • 4143071422 scopus 로고    scopus 로고
    • Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly
    • Klein, K. C., S. J. Polyak, and J. R. Lingappa. 2004. Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly. J. Virol. 78:9257-9269.
    • (2004) J. Virol. , vol.78 , pp. 9257-9269
    • Klein, K.C.1    Polyak, S.J.2    Lingappa, J.R.3
  • 26
    • 1242342119 scopus 로고    scopus 로고
    • The Matrix Protein of Marburg Virus Is Transported to the Plasma Membrane along Cellular Membranes: Exploiting the Retrograde Late Endosomal Pathway
    • DOI 10.1128/JVI.78.5.2382-2393.2004
    • Kolesnikova, L., S. Bamberg, B. Berghofer, and S. Becker. 2004. The matrix protein of Marburg virus is transported to the plasma membrane along cellular membranes: exploiting the retrograde late endosomal pathway. J. Virol. 78:2382-2393. (Pubitemid 38228931)
    • (2004) Journal of Virology , vol.78 , Issue.5 , pp. 2382-2393
    • Kolesnikova, L.1    Bamberg, S.2    Berghofer, B.3    Becker, S.4
  • 27
    • 0032863144 scopus 로고    scopus 로고
    • Association of Nef with the human immunodeficiency virus type 1 core
    • Kotov, A., J. Zhou, P. Flicker, and C. Aiken. 1999. Association of Nef with the human immunodeficiency virus type 1 core. J. Virol. 73:8824-8830. (Pubitemid 29441749)
    • (1999) Journal of Virology , vol.73 , Issue.10 , pp. 8824-8830
    • Kotov, A.1    Zhou, J.2    Flicker, P.3    Aiken, C.4
  • 28
    • 0035130118 scopus 로고    scopus 로고
    • Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein
    • DOI 10.1128/JVI.75.5.2119-2129.2001
    • Kunkel, M., M. Lorinczi, R. Rijnbrand, S. M. Lemon, and S. J. Watowich. 2001. Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein. J. Virol. 75:2119-2129. (Pubitemid 32147551)
    • (2001) Journal of Virology , vol.75 , Issue.5 , pp. 2119-2129
    • Kunkel, M.1    Lorinczi, M.2    Rijnbrand, R.3    Lemon, S.M.4    Watowich, S.J.5
  • 29
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • Lemberg, M. K., and B. Martoglio. 2002. Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol. Cell 10:735-744.
    • (2002) Mol. Cell , vol.10 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 30
    • 33745527481 scopus 로고    scopus 로고
    • Viral hepatitis and liver cancer: The case of hepatitis C
    • DOI 10.1038/sj.onc.1209562, PII 1209562
    • Levrero, M. 2006. Viral hepatitis and liver cancer: the case of hepatitis C. Oncogene 25:3834-3847. (Pubitemid 43980479)
    • (2006) Oncogene , vol.25 , Issue.27 , pp. 3834-3847
    • Levrero, M.1
  • 32
    • 0031060106 scopus 로고    scopus 로고
    • Regulated processing of hepatitis C virus core protein is linked to subcellular localization
    • Liu, Q., C. Tackney, R. A. Bhat, A. M. Prince, and P. Zhang. 1997. Regulated processing of hepatitis C virus core protein is linked to subcellular localization. J. Virol. 71:657-662. (Pubitemid 26412339)
    • (1997) Journal of Virology , vol.71 , Issue.1 , pp. 657-662
    • Liu, Q.1    Tackney, C.2    Bhat, R.A.3    Prince, A.M.4    Zhang, P.5
  • 33
    • 0029897323 scopus 로고    scopus 로고
    • Interaction between hepatitis C virus core protein and E1 envelope protein
    • Lo, S., M. Selby, and J. Ou. 1996. Interaction between hepatitis C virus core protein and E1 envelope protein. J. Virol. 70:5177-5182.
    • (1996) J. Virol. , vol.70 , pp. 5177-5182
    • Lo, S.1    Selby, M.2    Ou, J.3
  • 34
    • 0028840840 scopus 로고
    • Differential subcellular localization of hepatitis C virus core gene products
    • Lo, S. Y., F. Masiarz, S. B. Hwang, M. M. Lai, and J. H. Ou. 1995. Differential subcellular localization of hepatitis C virus core gene products. Virology 213:455-461.
    • (1995) Virology , vol.213 , pp. 455-461
    • Lo, S.Y.1    Masiarz, F.2    Hwang, S.B.3    Lai, M.M.4    Ou, J.H.5
  • 35
    • 0345188811 scopus 로고    scopus 로고
    • Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line
    • DOI 10.1126/science.285.5424.110
    • Lohmann, V., F. Korner, J. Koch, U. Herian, L. Theilmann, and R. Bartenschlager. 1999. Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 285:110-113. (Pubitemid 29307577)
    • (1999) Science , vol.285 , Issue.5424 , pp. 110-113
    • Lohmann, V.1    Korner, F.2    Koch, J.-O.3    Herian, U.4    Theilmann, L.5    Bartenschlager, R.6
  • 36
    • 0036933011 scopus 로고    scopus 로고
    • The first hydrophobic domain of the hepatitis C virus E1 protein is important for interaction with the capsid protein
    • Ma, H. C., C. H. Ke, T. Y. Hsieh, and S. Y. Lo. 2002. The first hydrophobic domain of the hepatitis C virus E1 protein is important for interaction with the capsid protein. J. Gen. Virol. 83:3085-3092.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3085-3092
    • Ma, H.C.1    Ke, C.H.2    Hsieh, T.Y.3    Lo, S.Y.4
  • 38
    • 0035866317 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins reside in the endoplasmic reticulum as well as in the intermediate compartment/cis-Golgi complex region of stably transfected cells
    • Martire, G., A. Viola, L. Iodice, L. V. Lotti, R. Gradini, and S. Bonatti. 2001. Hepatitis C virus structural proteins reside in the endoplasmic reticulum as well as in the intermediate compartment/cis-Golgi complex region of stably transfected cells. Virology 280:176-182.
    • (2001) Virology , vol.280 , pp. 176-182
    • Martire, G.1    Viola, A.2    Iodice, L.3    Lotti, L.V.4    Gradini, R.5    Bonatti, S.6
  • 39
    • 0029930196 scopus 로고    scopus 로고
    • Homotypic interaction and multimerization of hepatitis C virus core protein
    • DOI 10.1006/viro.1996.0164
    • Matsumoto, M., S. B. Hwang, K. S. Jeng, N. Zhu, and M. M. Lai. 1996. Homotypic interaction and multimerization of hepatitis C virus core protein. Virology 218:43-51. (Pubitemid 26133085)
    • (1996) Virology , vol.218 , Issue.1 , pp. 43-51
    • Matsumoto, M.1    Hwang, S.B.2    Jeng, K.-S.3    Zhu, N.4    Lai, M.M.C.5
  • 40
    • 0034053296 scopus 로고    scopus 로고
    • Properties of the hepatitis C virus core protein: A structural protein that modulates cellular processes
    • McLauchlan, J. 2000. Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes. J. Viral. Hepat. 7:2-14.
    • (2000) J. Viral. Hepat. , vol.7 , pp. 2-14
    • McLauchlan, J.1
  • 41
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • DOI 10.1093/emboj/cdf414
    • McLauchlan, J., M. K. Lemberg, G. Hope, and B. Martoglio. 2002. Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J. 21:3980-3988. (Pubitemid 34857431)
    • (2002) EMBO Journal , vol.21 , Issue.15 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 42
    • 0025249362 scopus 로고
    • Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups
    • Miller, R. H., and R. H. Purcell. 1990. Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups. Proc. Natl. Acad. Sci. USA 87:2057-2061.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2057-2061
    • Miller, R.H.1    Purcell, R.H.2
  • 44
    • 0030218609 scopus 로고    scopus 로고
    • Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein
    • DOI 10.1006/viro.1996.0397
    • Moradpour, D., C. Englert, T. Wakita, and J. R. Wands. 1996. Characterization of cell lines allowing tightly regulated expression of hepatitis C virus core protein. Virology 222:51-63. (Pubitemid 26281358)
    • (1996) Virology , vol.222 , Issue.1 , pp. 51-63
    • Moradpour, D.1    Englert, C.2    Wakita, T.3    Wands, J.R.4
  • 47
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy, D. J. 2001. The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40:325-438.
    • (2001) Prog. Lipid Res. , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 49
    • 50149086906 scopus 로고    scopus 로고
    • Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation
    • Okamoto, K., Y. Mori, Y. Komoda, T. Okamoto, M. Okochi, M. Takeda, T. Suzuki, K. Moriishi, and Y. Matsuura. 2008. Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation. J. Virol. 82:8349-8361.
    • (2008) J. Virol. , vol.82 , pp. 8349-8361
    • Okamoto, K.1    Mori, Y.2    Komoda, Y.3    Okamoto, T.4    Okochi, M.5    Takeda, M.6    Suzuki, T.7    Moriishi, K.8    Matsuura, Y.9
  • 50
    • 2642539953 scopus 로고    scopus 로고
    • Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein
    • DOI 10.1128/JVI.78.12.6370-6380.2004
    • Okamoto, K., K. Moriishi, T. Miyamura, and Y. Matsuura. 2004. Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein. J. Virol. 78:6370-6380. (Pubitemid 38715935)
    • (2004) Journal of Virology , vol.78 , Issue.12 , pp. 6370-6380
    • Okamoto, K.1    Moriishi, K.2    Miyamura, T.3    Matsuura, Y.4
  • 51
    • 0034731432 scopus 로고    scopus 로고
    • A loss of function mutant of the presenilin homologue SEL-12 undergoes aberrant endoproteolysis in Caenorhabditis elegans and increases Aβ42 generation in human cells
    • Okochi, M., S. Eimer, A. Bottcher, R. Baumeister, H. Romig, J. Walter, A. Capell, H. Steiner, and C. Haass. 2000. A loss of function mutant of the presenilin homologue SEL-12 undergoes aberrant endoproteolysis in Caenorhabditis elegans and increases Aβ42 generation in human cells. J. Biol. Chem. 275:40925-40932.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40925-40932
    • Okochi, M.1    Eimer, S.2    Bottcher, A.3    Baumeister, R.4    Romig, H.5    Walter, J.6    Capell, A.7    Steiner, H.8    Haass, C.9
  • 52
    • 0029618182 scopus 로고
    • Ultrastructural studies of neutral lipid localization in Streptomyces
    • Packter, N. M., and E. R. Olukoshi. 1995. Ultrastructural studies of neutral lipid localization in Streptomyces. Arch. Microbiol. 164:420-427.
    • (1995) Arch. Microbiol. , vol.164 , pp. 420-427
    • Packter, N.M.1    Olukoshi, E.R.2
  • 53
    • 0842303291 scopus 로고    scopus 로고
    • Pathophysiology of hepatitis C virus infection and related liver disease
    • DOI 10.1016/j.tim.2003.12.005
    • Pawlotsky, J. M. 2004. Pathophysiology of hepatitis C virus infection and related liver disease. Trends Microbiol. 12:96-102. (Pubitemid 38167344)
    • (2004) Trends in Microbiology , vol.12 , Issue.2 , pp. 96-102
    • Pawlotsky, J.-M.1
  • 54
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear, W. S., G. P. Nolan, M. L. Scott, and D. Baltimore. 1993. Production of high-titer helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. USA 90:8392-8396.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 55
  • 57
    • 0028233530 scopus 로고
    • Biosynthesis and biochemical properties of the hepatitis C virus core protein
    • Santolini, E., G. Migliaccio, and N. La Monica. 1994. Biosynthesis and biochemical properties of the hepatitis C virus core protein. J. Virol. 68:3631-3641. (Pubitemid 24177387)
    • (1994) Journal of Virology , vol.68 , Issue.6 , pp. 3631-3641
    • Santolini, E.1    Migliaccio, G.2    La Monica, N.3
  • 58
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • DOI 10.1093/embo-reports/kve180
    • Sastre, M., H. Steiner, K. Fuchs, A. Capell, G. Multhaup, M. M. Condron, D. B. Teplow, and C. Haass. 2001. Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. 2:835-841. (Pubitemid 32982753)
    • (2001) EMBO Reports , vol.2 , Issue.9 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 59
    • 37549005607 scopus 로고    scopus 로고
    • The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly
    • Shavinskaya, A., S. Boulant, F. Penin, J. McLauchlan, and R. Bartenschlager. 2007. The lipid droplet binding domain of hepatitis C virus core protein is a major determinant for efficient virus assembly. J. Biol. Chem. 282:37158-37169.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37158-37169
    • Shavinskaya, A.1    Boulant, S.2    Penin, F.3    McLauchlan, J.4    Bartenschlager, R.5
  • 61
    • 0028355603 scopus 로고
    • Identification of human immunodeficiency virus type 1 gag protein domains essential to membrane binding and particle assembly
    • Spearman, P., J.-J. Wang, N. Y. Heyden, and L. Ratner. 1994. Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly. J. Virol. 68:3232-3242. (Pubitemid 24129773)
    • (1994) Journal of Virology , vol.68 , Issue.5 , pp. 3232-3242
    • Spearman, P.1    Wang, J.-J.2    Vander Heyden, N.3    Ratner, L.4
  • 62
    • 0028854268 scopus 로고
    • Nuclear localization of the truncated hepatitis C virus core protein with its hydrophobic C terminus deleted
    • Suzuki, R., Y. Matsuura, T. Suzuki, A. Ando, J. Chiba, S. Harada, I. Saito, and T. Miyamura. 1995. Nuclear localization of the truncated hepatitis C virus core protein with its hydrophobic C terminus deleted. J. Gen. Virol. 76:53-61.
    • (1995) J. Gen. Virol. , vol.76 , pp. 53-61
    • Suzuki, R.1    Matsuura, Y.2    Suzuki, T.3    Ando, A.4    Chiba, J.5    Harada, S.6    Saito, I.7    Miyamura, T.8
  • 64
    • 0035866327 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of hepatitis C virus core protein is regulated by processing at its carboxyl terminus
    • DOI 10.1006/viro.2000.0785
    • Suzuki, R., K. Tamura, J. Li, K. Ishii, Y. Matsuura, T. Miyamura, and T. Suzuki. 2001. Ubiquitin-mediated degradation of hepatitis C virus core protein is regulated by processing at its carboxyl terminus. Virology 280:301-309. (Pubitemid 34165360)
    • (2001) Virology , vol.280 , Issue.2 , pp. 301-309
    • Suzuki, R.1    Tamura, K.2    Li, J.3    Ishii, K.4    Matsuura, Y.5    Miyamura, T.6    Suzuki, T.7
  • 67
    • 47749084704 scopus 로고    scopus 로고
    • Maturation of hepatitis C virus core protein by signal peptide peptidase is required for virus production
    • Targett-Adams, P., G. Hope, S. Boulant, and J. McLauchlan. 2008. Maturation of hepatitis C virus core protein by signal peptide peptidase is required for virus production. J. Biol. Chem. 283:16850-16859.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16850-16859
    • Targett-Adams, P.1    Hope, G.2    Boulant, S.3    McLauchlan, J.4
  • 68
    • 0036345943 scopus 로고    scopus 로고
    • Interaction between hepatitis C virus proteins and host cell factors
    • Tellinghuisen, T. L., and C. M. Rice. 2002. Interaction between hepatitis C virus proteins and host cell factors. Curr. Opin. Microbiol. 5:419-427.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 419-427
    • Tellinghuisen, T.L.1    Rice, C.M.2
  • 71
    • 0345099452 scopus 로고    scopus 로고
    • The roles of hepatitis C virus proteins in modulation of cellular functions: A novel action mechanism of the HCV core protein on gene regulation by nuclear hormone receptors
    • DOI 10.1111/j.1349-7006.2003.tb01381.x
    • Watashi, K., and K. Shimotohno. 2003. The roles of hepatitis C virus proteins in modulation of cellular functions: a novel action mechanism of the HCV core protein on gene regulation by nuclear hormone receptors. Cancer Sci. 94:937-943. (Pubitemid 37508974)
    • (2003) Cancer Science , vol.94 , Issue.11 , pp. 937-943
    • Watashi, K.1    Shimotohno, K.2
  • 72
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • DOI 10.1126/science.1070925
    • Weihofen, A., K. Binns, M. K. Lemberg, K. Ashman, and B. Martoglio. 2002. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296:2215-2218. (Pubitemid 34680305)
    • (2002) Science , vol.296 , Issue.5576 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 73
    • 0034613193 scopus 로고    scopus 로고
    • Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor
    • Weihofen, A., M. K. Lemberg, H. L. Ploegh, M. Bogyo, and B. Martoglio. 2000. Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor. J. Biol. Chem. 275:30951-30956.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30951-30956
    • Weihofen, A.1    Lemberg, M.K.2    Ploegh, H.L.3    Bogyo, M.4    Martoglio, B.5
  • 74
    • 33749058310 scopus 로고    scopus 로고
    • A proposed model of fat packaging by exchangeable lipid droplet proteins
    • Wolins, N. E., D. L. Brasaemle, and P. E. Bickel. 2006. A proposed model of fat packaging by exchangeable lipid droplet proteins. FEBS Lett. 580:5484-5491.
    • (2006) FEBS Lett. , vol.580 , pp. 5484-5491
    • Wolins, N.E.1    Brasaemle, D.L.2    Bickel, P.E.3
  • 75
    • 0033809342 scopus 로고    scopus 로고
    • Gag in immature human immunodeficiency virus type 1 particles
    • Gag in immature human immunodeficiency virus type 1 particles. J. Virol. 74:9381-9387.
    • (2000) J. Virol. , vol.74 , pp. 9381-9387
    • Wyma, D.J.1    Kotov, A.2    Aiken, C.3
  • 76
    • 0042671326 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilin and presenilin-like proteases
    • DOI 10.1242/jcs.00651
    • Xia, W., and M. S. Wolfe. 2003. Intramembrane proteolysis by presenilin and presenilin-like proteases. J. Cell Sci. 116:2839-2844. (Pubitemid 36926973)
    • (2003) Journal of Cell Science , vol.116 , Issue.14 , pp. 2839-2844
    • Xia, W.1    Wolfe, M.S.2


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