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Volumn 84, Issue 13, 2010, Pages 6782-6798

Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication

Author keywords

[No Author keywords available]

Indexed keywords

CELL EXTRACT; DOUBLE STRANDED RNA; FAT DROPLET; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; ISOBUTYLMETHYLXANTHINE; ISOPRENALINE; NONSTRUCTURAL PROTEIN 5; PERILIPIN; PERILIPIN A; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 77953300336     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01757-09     Document Type: Article
Times cited : (161)

References (60)
  • 1
    • 0029793171 scopus 로고    scopus 로고
    • Phosphorylation generates different forms of rotavirus NSP5
    • Afrikanova, I., M. C. Miozzo, S. Giambiagi, and O. Burrone. 1996. Phosphorylation generates different forms of rotavirus NSP5. J. Gen. Virol. 77: 2059-2065.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2059-2065
    • Afrikanova, I.1    Miozzo, M.C.2    Giambiagi, S.3    Burrone, O.4
  • 2
    • 33847232565 scopus 로고    scopus 로고
    • Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2
    • Arnoldi, F., M. Campagna, C. Eichwald, U. Desselberger, and O. R. Burrone. 2007. Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2. J. Virol. 81:2128-2137.
    • (2007) J. Virol. , vol.81 , pp. 2128-2137
    • Arnoldi, F.1    Campagna, M.2    Eichwald, C.3    Desselberger, U.4    Burrone, O.R.5
  • 3
    • 1542268895 scopus 로고    scopus 로고
    • Viral molecular machines: Replication systems within the inner cores of dsRNA viruses
    • Bamford, D. H., and L. Mindich. 2004. Viral molecular machines: replication systems within the inner cores of dsRNA viruses. Virus Res. 101:1.
    • (2004) Virus Res. , vol.101 , pp. 1
    • Bamford, D.H.1    Mindich, L.2
  • 4
    • 34548150017 scopus 로고    scopus 로고
    • Dynamic activity of lipid droplets: Protein phosphorylation and GTP-mediated protein translocation
    • Bartz, R., J. K. Zehmer, M. Zhu, Y. Chen, G. Serrero, Y. Zhao, and P. Liu. 2007. Dynamic activity of lipid droplets: protein phosphorylation and GTP-mediated protein translocation. J. Proteome Res. 6:3256-3265.
    • (2007) J. Proteome Res. , vol.6 , pp. 3256-3265
    • Bartz, R.1    Zehmer, J.K.2    Zhu, M.3    Chen, Y.4    Serrero, G.5    Zhao, Y.6    Liu, P.7
  • 6
    • 33744935521 scopus 로고    scopus 로고
    • Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms
    • Berkova, Z., S. E. Crawford, G. Trugnan, T. Yoshimori, A. P. Morris, and M. K. Estes. 2006. Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms. J. Virol. 80:6061-6071.
    • (2006) J. Virol. , vol.80 , pp. 6061-6071
    • Berkova, Z.1    Crawford, S.E.2    Trugnan, G.3    Yoshimori, T.4    Morris, A.P.5    Estes, M.K.6
  • 7
    • 0023146961 scopus 로고
    • Application of nile blue and nile red, two fluorescent probes, for detection of lipid droplets in human skeletal muscle
    • Bonilla, E., and A. Prelle. 1987. Application of nile blue and nile red, two fluorescent probes, for detection of lipid droplets in human skeletal muscle. J. Histochem. Cytochem. 35:619-621.
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 619-621
    • Bonilla, E.1    Prelle, A.2
  • 8
    • 34547592075 scopus 로고    scopus 로고
    • Disrupting the association of hepatitis C virus core protein with lipid droplets correlates with a loss in production of infectious virus
    • Boulant, S., P. Targett-Adams, and J. McLauchlan. 2007. Disrupting the association of hepatitis C virus core protein with lipid droplets correlates with a loss in production of infectious virus. J. Gen. Virol. 88:2204-2213.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2204-2213
    • Boulant, S.1    Targett-Adams, P.2    McLauchlan, J.3
  • 9
    • 0030724392 scopus 로고    scopus 로고
    • Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein
    • Brasaemle, D. L., T. Barber, N. E. Wolins, G. Serrero, E. J. Blanchette- Mackie, and C. Londos. 1997. Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein. J. Lipid Res. 38:2249-2263.
    • (1997) J. Lipid Res. , vol.38 , pp. 2249-2263
    • Brasaemle, D.L.1    Barber, T.2    Wolins, N.E.3    Serrero, G.4    Blanchette- Mackie, E.J.5    Londos, C.6
  • 10
    • 0034623950 scopus 로고    scopus 로고
    • Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis
    • Brasaemle, D. L., B. Rubin, I. A. Harten, J. Gruia-Gray, A. R. Kimmel, and C. Londos. 2000. Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis. J. Biol. Chem. 275:38486-38493.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38486-38493
    • Brasaemle, D.L.1    Rubin, B.2    Harten, I.A.3    Gruia-Gray, J.4    Kimmel, A.R.5    Londos, C.6
  • 11
    • 18144388985 scopus 로고    scopus 로고
    • RNA interference of rotavirus segment 11 mRNA reveals the essential role of NSP5 in the virus replicative cycle
    • Campagna, M., C. Eichwald, F. Vascotto, and O. R. Burrone. 2005. RNA interference of rotavirus segment 11 mRNA reveals the essential role of NSP5 in the virus replicative cycle. J. Gen. Virol. 86:1481-1487.
    • (2005) J. Gen. Virol. , vol.86 , pp. 1481-1487
    • Campagna, M.1    Eichwald, C.2    Vascotto, F.3    Burrone, O.R.4
  • 12
    • 33748641937 scopus 로고    scopus 로고
    • Reovirus outer capsid protein micro1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria
    • Coffey, C. M., A. Sheh, I. S. Kim, K. Chandran, M. L. Nibert, and J. S. Parker. 2006. Reovirus outer capsid protein micro1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J. Virol. 80:8422-8438.
    • (2006) J. Virol. , vol.80 , pp. 8422-8438
    • Coffey, C.M.1    Sheh, A.2    Kim, I.S.3    Chandran, K.4    Nibert, M.L.5    Parker, J.S.6
  • 14
    • 33645755879 scopus 로고    scopus 로고
    • Dissecting rotavirus particle-raft interaction with small interfering RNAs: Insights into rotavirus transit through the secretory pathway
    • Cuadras, M. A., B. B. Bordier, J. L. Zambrano, J. E. Ludert, and H. B. Greenberg. 2006. Dissecting rotavirus particle-raft interaction with small interfering RNAs: insights into rotavirus transit through the secretory pathway. J. Virol. 80:3935-3946.
    • (2006) J. Virol. , vol.80 , pp. 3935-3946
    • Cuadras, M.A.1    Bordier, B.B.2    Zambrano, J.L.3    Ludert, J.E.4    Greenberg, H.B.5
  • 15
    • 0036223703 scopus 로고    scopus 로고
    • Gene expression pattern in Caco-2 cells following rotavirus infection
    • Cuadras, M. A., D. A. Feigelstock, S. An, and H. B. Greenberg. 2002. Gene expression pattern in Caco-2 cells following rotavirus infection. J. Virol. 76:4467-4482.
    • (2002) J. Virol. , vol.76 , pp. 4467-4482
    • Cuadras, M.A.1    Feigelstock, D.A.2    An, S.3    Greenberg, H.B.4
  • 16
    • 1642308801 scopus 로고    scopus 로고
    • Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation
    • Eichwald, C., J. F. Rodriguez, and O. R. Burrone. 2004. Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation. J. Gen. Virol. 85:625-634.
    • (2004) J. Gen. Virol. , vol.85 , pp. 625-634
    • Eichwald, C.1    Rodriguez, J.F.2    Burrone, O.R.3
  • 17
    • 34248595601 scopus 로고    scopus 로고
    • Alpha-synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
    • Esposito, A., C. P. Dohm, P. Kermer, M. Bähr, and F. S. Wouters. 2007. Alpha-synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton. Neurobiol. Dis. 26:521-531.
    • (2007) Neurobiol. Dis. , vol.26 , pp. 521-531
    • Esposito, A.1    Dohm, C.P.2    Kermer, P.3    Bähr, M.4    Wouters, F.S.5
  • 18
    • 28444451587 scopus 로고    scopus 로고
    • Fluorescence lifetime heterogeneity resolution in the frequency domain by lifetime moments analysis
    • Esposito, A., H. C. Gerritsen, and F. S. Wouters. 2005. Fluorescence lifetime heterogeneity resolution in the frequency domain by lifetime moments analysis. Biophys. J. 89:4286-4299.
    • (2005) Biophys. J. , vol.89 , pp. 4286-4299
    • Esposito, A.1    Gerritsen, H.C.2    Wouters, F.S.3
  • 20
    • 34548407520 scopus 로고    scopus 로고
    • Rotaviruses
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), 5th ed. Lippincott Williams & Wilkins Publishers, Philadelphia, PA
    • Estes, M. K., and A. Z. Kapikian. 2007. Rotaviruses, p. 1917-1974. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins Publishers, Philadelphia, PA.
    • (2007) Fields Virology , pp. 1917-1974
    • Estes, M.K.1    Kapikian, A.Z.2
  • 21
    • 0032970118 scopus 로고    scopus 로고
    • Two nonstructural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo
    • Fabbretti, E., I. Afrikanova, F. Vascotto, and O. R. Burrone. 1999. Two nonstructural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo. J. Gen. Virol. 80:333-339.
    • (1999) J. Gen. Virol. , vol.80 , pp. 333-339
    • Fabbretti, E.1    Afrikanova, I.2    Vascotto, F.3    Burrone, O.R.4
  • 22
    • 0020658577 scopus 로고
    • Cocirculation of different rotavirus strains in a local outbreak of infantile gastroenteritis: Monitoring by rapid and sensitive nucleic acid analysis
    • Follett, E. A., and U. Desselberger. 1983. Cocirculation of different rotavirus strains in a local outbreak of infantile gastroenteritis: monitoring by rapid and sensitive nucleic acid analysis. J. Med. Virol. 11:39-52.
    • (1983) J. Med. Virol. , vol.11 , pp. 39-52
    • Follett, E.A.1    Desselberger, U.2
  • 24
    • 0024522801 scopus 로고
    • Structure and stability of mRNA synthesized by vaccinia virus-encoded bacteriophage T7 RNA polymerase in mammalian cells. Importance of the 5′ untranslated leader
    • Fuerst, T. R., and B. Moss. 1989. Structure and stability of mRNA synthesized by vaccinia virus-encoded bacteriophage T7 RNA polymerase in mammalian cells. Importance of the 5′ untranslated leader. J. Mol. Biol. 206:333-348.
    • (1989) J. Mol. Biol. , vol.206 , pp. 333-348
    • Fuerst, T.R.1    Moss, B.2
  • 25
    • 0024317561 scopus 로고
    • Characterization of rotavirus replication intermediates: A model for the assembly of single-shelled particles
    • Gallegos, C. O., and J. T. Patton. 1989. Characterization of rotavirus replication intermediates: a model for the assembly of single-shelled particles. Virology 172:616-627.
    • (1989) Virology , vol.172 , pp. 616-627
    • Gallegos, C.O.1    Patton, J.T.2
  • 26
    • 13544265408 scopus 로고    scopus 로고
    • The use of a fluorescent dye, Nile red, to evaluate the lipid content of single mammalian oocytes
    • Genicot, G., J. L. Leroy, A. V. Soom, and I. Donnay. 2005. The use of a fluorescent dye, Nile red, to evaluate the lipid content of single mammalian oocytes. Theriogenology 63:1181-1194.
    • (2005) Theriogenology , vol.63 , pp. 1181-1194
    • Genicot, G.1    Leroy, J.L.2    Soom, A.V.3    Donnay, I.4
  • 27
    • 31444438260 scopus 로고    scopus 로고
    • Dynamics of lipid dropletassociated proteins during hormonally stimulated lipolysis in engineered adipocytes: Stabilization and lipid droplet binding of adipocyte differentiation- Related protein/adipophilin
    • Gross, D. N., H. Miyoshi, T. Hosaka, H. H. Zhang, E. C. Pino, S. Souza, M. Obin, A. S. Greenberg, and P. F. Pilch. 2006. Dynamics of lipid dropletassociated proteins during hormonally stimulated lipolysis in engineered adipocytes: stabilization and lipid droplet binding of adipocyte differentiation- related protein/adipophilin. Mol. Endocrinol. 20:459-466.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 459-466
    • Gross, D.N.1    Miyoshi, H.2    Hosaka, T.3    Zhang, H.H.4    Pino, E.C.5    Souza, S.6    Obin, M.7    Greenberg, A.S.8    Pilch, P.F.9
  • 29
    • 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
  • 30
    • 0030972879 scopus 로고    scopus 로고
    • Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: Evidence for functionally separate pools of acyl-CoA
    • Igal, R. A., P. Wang, and R. A. Coleman. 1997. Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: evidence for functionally separate pools of acyl-CoA. Biochem. J. 324:529-534.
    • (1997) Biochem. J. , vol.324 , pp. 529-534
    • Igal, R.A.1    Wang, P.2    Coleman, R.A.3
  • 31
    • 33847652985 scopus 로고    scopus 로고
    • Intracellular localization and effects of individually expressed human parechovirus 1 non-structural proteins
    • Krogerus, C., O. Samuilova, T. Poeyry, E. Jokitalo, and T. Hyypiae. 2007. Intracellular localization and effects of individually expressed human parechovirus 1 non-structural proteins. J. Gen. Virol. 88:831-841.
    • (2007) J. Gen. Virol. , vol.88 , pp. 831-841
    • Krogerus, C.1    Samuilova, O.2    Poeyry, T.3    Jokitalo, E.4    Hyypiae, T.5
  • 32
    • 33747171783 scopus 로고    scopus 로고
    • The obligate intracellular pathogen Chlamydia trachomatis targets host lipid droplets
    • Kumar, Y., J. Cocchiaro, and R. H. Valdivia. 2006. The obligate intracellular pathogen Chlamydia trachomatis targets host lipid droplets. Curr. Biol. 16: 1646-1651.
    • (2006) Curr. Biol. , vol.16 , pp. 1646-1651
    • Kumar, Y.1    Cocchiaro, J.2    Valdivia, R.H.3
  • 34
    • 33744904687 scopus 로고    scopus 로고
    • The phosphorylation of serine 492 of perilipin a directs lipid droplet fragmentation and dispersion
    • Marcinkiewicz, A., D. Gauthier, A. Garcia, and D. L. Brasaemle. 2006. The phosphorylation of serine 492 of perilipin a directs lipid droplet fragmentation and dispersion. J. Biol. Chem. 281:11901-11909.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11901-11909
    • Marcinkiewicz, A.1    Gauthier, D.2    Garcia, A.3    Brasaemle, D.L.4
  • 35
    • 29644442801 scopus 로고    scopus 로고
    • Regulated localization of Rab18 to lipid droplets: Effects of lipolytic stimulation and inhibition of lipid droplet catabolism
    • Martin, S., K. Driessen, S. J. Nixon, M. Zerial, and R. G. Parton. 2005. Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism. J. Biol. Chem. 280:42325-42335.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42325-42335
    • Martin, S.1    Driessen, K.2    Nixon, S.J.3    Zerial, M.4    Parton, R.G.5
  • 36
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin, S., and R. G. Parton. 2006. Lipid droplets: a unified view of a dynamic organelle. Nat. Rev. Mol. Cell. Biol. 7:373-378.
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 37
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium
    • Miura, S., J. W. Gan, J. Brzostowski, M. J. Parisi, C. J. Schultz, C. Londos, B. Oliver, and A. R. Kimmel. 2002. Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium. J. Biol. Chem. 277:32253-32257.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32253-32257
    • Miura, S.1    Gan, J.W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5    Londos, C.6    Oliver, B.7    Kimmel, A.R.8
  • 39
    • 0033060605 scopus 로고    scopus 로고
    • Complete inhibition of mouse macrophage-derived foam cell formation by Triacsin C
    • Namatame, I., H. Tomoda, H. Arai, K. Inoue, and S. Omura. 1999. Complete inhibition of mouse macrophage-derived foam cell formation by triacsin C. J. Biochem. 125:319-327. (Pubitemid 29112297)
    • (1999) Journal of Biochemistry , vol.125 , Issue.2 , pp. 319-327
    • Namatame, I.1    Tomoda, H.2    Arai, H.3    Inoue, K.4    Omura, S.5
  • 40
    • 0034054287 scopus 로고    scopus 로고
    • Rotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells
    • Nejmeddine, M., G. Trugnan, C. Sapin, E. Kohli, L. Svensson, S. Lopez, and J. Cohen. 2000. Rotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells. J. Virol. 74:3313-3320.
    • (2000) J. Virol. , vol.74 , pp. 3313-3320
    • Nejmeddine, M.1    Trugnan, G.2    Sapin, C.3    Kohli, E.4    Svensson, L.5    Lopez, S.6    Cohen, J.7
  • 41
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), 4th ed. Lippincott-Raven Publishers, Philadelphia, PA
    • Nibert, M. L., and L. A. Schiff. 2001. Reoviruses and their replication, p. 1679-1728. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 4th ed. Lippincott-Raven Publishers, Philadelphia, PA.
    • (2001) Fields Virology , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 42
    • 33144465371 scopus 로고    scopus 로고
    • Association between hepatitis C virus and very-low-density lipoprotein (VLDL)/LDL analyzed in iodixanol density gradients
    • Nielsen, S. U., M. F. Bassendine, A. D. Burt, C. Martin, W. Pumeechockchai, and G. L. Toms. 2006. Association between hepatitis C virus and very-low-density lipoprotein (VLDL)/LDL analyzed in iodixanol density gradients. J. Virol. 80:2418-2428.
    • (2006) J. Virol. , vol.80 , pp. 2418-2428
    • Nielsen, S.U.1    Bassendine, M.F.2    Burt, A.D.3    Martin, C.4    Pumeechockchai, W.5    Toms, G.L.6
  • 44
    • 33644755614 scopus 로고    scopus 로고
    • The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1
    • Parr, R. D., S. M. Storey, D. M. Mitchell, A. L. McIntosh, M. Zhou, K. D. Mir, and J. M. Ball. 2006. The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1. J. Virol. 80:2842-2854.
    • (2006) J. Virol. , vol.80 , pp. 2842-2854
    • Parr, R.D.1    Storey, S.M.2    Mitchell, D.M.3    McIntosh, A.L.4    Zhou, M.5    Mir, K.D.6    Ball, J.M.7
  • 46
    • 0020445167 scopus 로고
    • Localization of rotavirus antigens in infected cells by ultrastructural immunocytochemistry
    • Petrie, B. L., D. Y. Graham, H. Hanssen, and M. K. Estes. 1982. Localization of rotavirus antigens in infected cells by ultrastructural immunocytochemistry. J. Gen. Virol. 63:457-467.
    • (1982) J. Gen. Virol. , vol.63 , pp. 457-467
    • Petrie, B.L.1    Graham, D.Y.2    Hanssen, H.3    Estes, M.K.4
  • 47
    • 0021238996 scopus 로고
    • Ultrastructural localization of rotavirus antigens using colloidal gold
    • Petrie, B. L., H. B. Greenberg, D. Y. Graham, and M. K. Estes. 1984. Ultrastructural localization of rotavirus antigens using colloidal gold. Virus Res. 1:133-152.
    • (1984) Virus Res. , vol.1 , pp. 133-152
    • Petrie, B.L.1    Greenberg, H.B.2    Graham, D.Y.3    Estes, M.K.4
  • 51
    • 35448999759 scopus 로고    scopus 로고
    • The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domain
    • Sen, A., N. Sen, and E. R. Mackow. 2007. The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domain. J. Virol. 81:11758-11767.
    • (2007) J. Virol. , vol.81 , pp. 11758-11767
    • Sen, A.1    Sen, N.2    Mackow, E.R.3
  • 53
    • 0037424252 scopus 로고    scopus 로고
    • Functional studies on native and mutated forms of perilipins: A role in protein kinase a-mediated lipolysis of triacylglycerols
    • Tansey, J. T., A. M. Huml, R. Vogt, K. E. Davis, J. M. Jones, K. A. Fraser, D. L. Brasaemle, A. R. Kimmel, and C. Londos. 2003. Functional studies on native and mutated forms of perilipins: a role in protein kinase A-mediated lipolysis of triacylglycerols. J. Biol. Chem. 278:8401-8406.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8401-8406
    • Tansey, J.T.1    Huml, A.M.2    Vogt, R.3    Davis, K.E.4    Jones, J.M.5    Fraser, K.A.6    Brasaemle, D.L.7    Kimmel, A.R.8    Londos, C.9
  • 54
    • 0036634873 scopus 로고    scopus 로고
    • Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein
    • Taraporewala, Z. F., P. Schuck, R. F. Ramig, L. Silvestri, and J. T. Patton. 2002. Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein. J. Virol. 76:7082-7093.
    • (2002) J. Virol. , vol.76 , pp. 7082-7093
    • Taraporewala, Z.F.1    Schuck, P.2    Ramig, R.F.3    Silvestri, L.4    Patton, J.T.5
  • 55
    • 67749133561 scopus 로고    scopus 로고
    • Decline and change in seasonality of US rotavirus activity after the introduction of rotavirus vaccine
    • Tate, J. E., C. A. Panozzo, D. C. Payne, M. M. Patel, M. M. Cortese, A. L. Fowlkes, and U. D. Parashar. 2009. Decline and change in seasonality of US rotavirus activity after the introduction of rotavirus vaccine. Pediatrics 124: 465-471.
    • (2009) Pediatrics , vol.124 , pp. 465-471
    • Tate, J.E.1    Panozzo, C.A.2    Payne, D.C.3    Patel, M.M.4    Cortese, M.M.5    Fowlkes, A.L.6    Parashar, U.D.7
  • 56
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • Tauchi-Sato, K., S. Ozeki, T. Houjou, R. Taguchi, and T. Fujimoto. 2002. The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J. Biol. Chem. 277:44507-44512.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 57
    • 7444221874 scopus 로고    scopus 로고
    • Effects of intrabodies specific for rotavirus NSP5 during the virus replicative cycle
    • Vascotto, F., M. Campagna, M. Visintin, A. Cattaneo, and O. R. Burrone. 2004. Effects of intrabodies specific for rotavirus NSP5 during the virus replicative cycle. J. Gen. Virol. 85:3285-3290.
    • (2004) J. Gen. Virol. , vol.85 , pp. 3285-3290
    • Vascotto, F.1    Campagna, M.2    Visintin, M.3    Cattaneo, A.4    Burrone, O.R.5


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