메뉴 건너뛰기




Volumn 88, Issue 5, 2014, Pages 3016-3026

The tobacco mosaic virus movement protein associates with but does not integrate into biological membranes

Author keywords

[No Author keywords available]

Indexed keywords

PLANT VIRUS MOVEMENT PROTEIN; TOBACCO MOSAIC VIRUS MOVEMENT PROTEIN; UNCLASSIFIED DRUG;

EID: 84896737759     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03648-13     Document Type: Article
Times cited : (61)

References (58)
  • 1
    • 81755174264 scopus 로고    scopus 로고
    • Wrapping membranes around plant virus infection
    • Verchot J. 2011. Wrapping membranes around plant virus infection. Curr. Opin. Virol. 1:388-395. http://dx.doi.org/10.1016/j.coviro.2011.09 .009.
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 388-395
    • Verchot, J.1
  • 2
    • 0026842469 scopus 로고
    • Visualization and characterization of tobacco mosaic virus movement protein binding to single-stranded nucleic acids
    • Citovsky V, Wong ML, Shaw AL, Prasad BV, Zambryski P. 1992. Visualization and characterization of tobacco mosaic virus movement protein binding to single-stranded nucleic acids. Plant Cell 4:397-411. http://dx.doi.org/10.1105/tpc.4.4.397.
    • (1992) Plant Cell , vol.4 , pp. 397-411
    • Citovsky, V.1    Wong, M.L.2    Shaw, A.L.3    Prasad, B.V.4    Zambryski, P.5
  • 3
    • 0026541815 scopus 로고
    • In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product
    • Akiyama Y, Kamitani S, Kusukawa N, Ito K. 1992. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J. Biol. Chem. 267:22440-22445.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22440-22445
    • Akiyama, Y.1    Kamitani, S.2    Kusukawa, N.3    Ito, K.4
  • 4
    • 0035036236 scopus 로고    scopus 로고
    • Non-targeted and targeted protein movement through plasmodesmata in leaves in different developmental and physiological states
    • Crawford KM, Zambryski PC. 2001. Non-targeted and targeted protein movement through plasmodesmata in leaves in different developmental and physiological states. Plant Physiol. 125:1802-1812. http://dx.doi.org /10.1104/pp.125.4.1802.
    • (2001) Plant Physiol. , vol.125 , pp. 1802-1812
    • Crawford, K.M.1    Zambryski, P.C.2
  • 5
    • 0027983027 scopus 로고
    • Direct functional assay for tobacco mosaic virus cell-to-cell movement protein and identification of a domain involved in increasing plasmodesmal permeability
    • Waigmann E, Lucas WJ, Citovsky V, Zambryski P. 1994. Direct functional assay for tobacco mosaic virus cell-to-cell movement protein and identification of a domain involved in increasing plasmodesmal permeability. Proc. Natl. Acad. Sci. U. S. A. 91:1433-1437. http://dx.doi.org/10 .1073/pnas.91.4.1433.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1433-1437
    • Waigmann, E.1    Lucas, W.J.2    Citovsky, V.3    Zambryski, P.4
  • 6
    • 33645069960 scopus 로고
    • Movement protein of tobacco mosaic virus modifies plasmodesmatal size exclusion limit
    • Wolf S, Deom CM, Beachy RN, Lucas WJ. 1989. Movement protein of tobacco mosaic virus modifies plasmodesmatal size exclusion limit. Science 246:377-379. http://dx.doi.org/10.1126/science.246.4928.377.
    • (1989) Science , vol.246 , pp. 377-379
    • Wolf, S.1    Deom, C.M.2    Beachy, R.N.3    Lucas, W.J.4
  • 7
    • 0031259853 scopus 로고    scopus 로고
    • Gating of epidermal plasmodesmata is restricted to the leading edge of expanding infection sites of tobacco mosaic virus (TMV)
    • Oparka KJ, Prior DA, Santa Cruz S, Padgett HS, Beachy RN. 1997. Gating of epidermal plasmodesmata is restricted to the leading edge of expanding infection sites of tobacco mosaic virus (TMV). Plant J. 12:781-789. http://dx.doi.org/10.1046/j.1365-313X.1997.12040781.x.
    • (1997) Plant J. , vol.12 , pp. 781-789
    • Oparka, K.J.1    Prior, D.A.2    Santa Cruz, S.3    Padgett, H.S.4    Beachy, R.N.5
  • 8
    • 84879992326 scopus 로고    scopus 로고
    • Microtubules in viral replication and transport
    • Niehl A, Pena EJ, Amari K, Heinlein M. 2013. Microtubules in viral replication and transport. Plant J. 75:290-308. http://dx.doi.org/10.1111 /tpj.12134.
    • (2013) Plant J. , vol.75 , pp. 290-308
    • Niehl, A.1    Pena, E.J.2    Amari, K.3    Heinlein, M.4
  • 9
    • 34547819726 scopus 로고    scopus 로고
    • Validation of microtubule-associated Tobacco mosaic virus RNA movement and involvement of microtubule-aligned particle trafficking
    • Boyko V, Hu Q, Seemanpillai M, Ashby J, Heinlein M. 2007. Validation of microtubule-associated Tobacco mosaic virus RNA movement and involvement of microtubule-aligned particle trafficking. Plant J. 51:589-603. http://dx.doi.org/10.1111/j.1365-313X.2007.03163.x.
    • (2007) Plant J. , vol.51 , pp. 589-603
    • Boyko, V.1    Hu, Q.2    Seemanpillai, M.3    Ashby, J.4    Heinlein, M.5
  • 10
    • 56149089390 scopus 로고    scopus 로고
    • Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata
    • Sambade A, Brandner K, Hofmann C, Seemanpillai M, Mutterer J, Heinlein M. 2008. Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata. Traffic 9:2073-2088. http://dx.doi.org/10.1111/j.1600-0854.2008.00824.x.
    • (2008) Traffic , vol.9 , pp. 2073-2088
    • Sambade, A.1    Brandner, K.2    Hofmann, C.3    Seemanpillai, M.4    Mutterer, J.5    Heinlein, M.6
  • 11
    • 0032530963 scopus 로고    scopus 로고
    • Tobacco mosaic virus infection induces severe morphological changes of the endoplasmic reticulum
    • Reichel C, Beachy RN. 1998. Tobacco mosaic virus infection induces severe morphological changes of the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 95:11169-11174. http://dx.doi.org/10.1073/pnas.95.19 .11169.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11169-11174
    • Reichel, C.1    Beachy, R.N.2
  • 12
    • 0034231287 scopus 로고    scopus 로고
    • Role of P30 in replication and spread of TMV
    • Beachy RN, Heinlein M. 2000. Role of P30 in replication and spread of TMV. Traffic 1:540-544. http://dx.doi.org/10.1034/j.1600-0854.2000 .010703.x.
    • (2000) Traffic , vol.1 , pp. 540-544
    • Beachy, R.N.1    Heinlein, M.2
  • 13
    • 0242489811 scopus 로고    scopus 로고
    • Replication of tobacco mosaic virus on endoplasmic reticulum and role of the cytoskeleton and virus movement protein in intracellular distribution of viral RNA
    • Mas P, Beachy RN. 1999. Replication of tobacco mosaic virus on endoplasmic reticulum and role of the cytoskeleton and virus movement protein in intracellular distribution of viral RNA. J. Cell Biol. 147:945-958. http://dx.doi.org/10.1083/jcb.147.5.945.
    • (1999) J. Cell Biol. , vol.147 , pp. 945-958
    • Mas, P.1    Beachy, R.N.2
  • 14
    • 0031769602 scopus 로고    scopus 로고
    • Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection
    • Heinlein M, Padgett HS, Gens JS, Pickard BG, Casper SJ, Epel BL, Beachy RN. 1998. Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection. Plant Cell 10:1107-1120. http://dx.doi.org /10.1105/tpc.10.7.1107.
    • (1998) Plant Cell , vol.10 , pp. 1107-1120
    • Heinlein, M.1    Padgett, H.S.2    Gens, J.S.3    Pickard, B.G.4    Casper, S.J.5    Epel, B.L.6    Beachy, R.N.7
  • 15
    • 0034691078 scopus 로고    scopus 로고
    • Recombinant tobacco mosaic virus movement protein is an RNA-binding, alphahelical membrane protein
    • Brill LM, Nunn RS, Kahn TW, Yeager M, Beachy RN. 2000. Recombinant tobacco mosaic virus movement protein is an RNA-binding, alphahelical membrane protein. Proc. Natl. Acad. Sci. U. S. A. 97:7112-7117. http://dx.doi.org/10.1073/pnas.130187897.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7112-7117
    • Brill, L.M.1    Nunn, R.S.2    Kahn, T.W.3    Yeager, M.4    Beachy, R.N.5
  • 16
    • 33747334567 scopus 로고    scopus 로고
    • Domains of tobacco mosaic virus movement protein essential for its membrane association
    • Fujiki M, Kawakami S, Kim RW, Beachy RN. 2006. Domains of tobacco mosaic virus movement protein essential for its membrane association. J. Gen. Virol. 87:2699-2707. http://dx.doi.org/10.1099/vir.0.81936-0.
    • (2006) J. Gen. Virol. , vol.87 , pp. 2699-2707
    • Fujiki, M.1    Kawakami, S.2    Kim, R.W.3    Beachy, R.N.4
  • 17
    • 34247256783 scopus 로고    scopus 로고
    • MPB2C, a microtubule-associated plant factor, is required for microtubular accumulation of tobacco mosaic virus movement protein in plants
    • Curin M, Ojangu EL, Trutnyeva K, Ilau B, Truve E, Waigmann E. 2007. MPB2C, a microtubule-associated plant factor, is required for microtubular accumulation of tobacco mosaic virus movement protein in plants. Plant Physiol. 143:801-811. http://dx.doi.org/10.1104/pp.106.091488.
    • (2007) Plant Physiol. , vol.143 , pp. 801-811
    • Curin, M.1    Ojangu, E.L.2    Trutnyeva, K.3    Ilau, B.4    Truve, E.5    Waigmann, E.6
  • 18
    • 67349191497 scopus 로고    scopus 로고
    • Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus
    • Shimizu T, Yoshii A, Sakurai K, Hamada K, Yamaji Y, Suzuki M, Namba S, Hibi T. 2009. Identification of a novel tobacco DnaJ-like protein that interacts with the movement protein of tobacco mosaic virus. Arch. Virol. 154:959-967. http://dx.doi.org/10.1007/s00705-009-0397-6.
    • (2009) Arch. Virol. , vol.154 , pp. 959-967
    • Shimizu, T.1    Yoshii, A.2    Sakurai, K.3    Hamada, K.4    Yamaji, Y.5    Suzuki, M.6    Namba, S.7    Hibi, T.8
  • 19
    • 0034161265 scopus 로고    scopus 로고
    • Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement
    • Chen MH, Sheng J, Hind G, Handa AK, Citovsky V. 2000. Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement. EMBO J. 19: 913-920. http://dx.doi.org/10.1093/emboj/19.5.913.
    • (2000) EMBO J. , vol.19 , pp. 913-920
    • Chen, M.H.1    Sheng, J.2    Hind, G.3    Handa, A.K.4    Citovsky, V.5
  • 20
    • 0036893184 scopus 로고    scopus 로고
    • Novel N gene-associated, temperatureindependent resistance to the movement of tobacco mosaic virus vectors neutralized by a cucumber mosaic virus RNA1 transgene
    • Canto T, Palukaitis P. 2002. Novel N gene-associated, temperatureindependent resistance to the movement of tobacco mosaic virus vectors neutralized by a cucumber mosaic virus RNA1 transgene. J. Virol. 76: 12908-12916. http://dx.doi.org/10.1128/JVI.76.24.12908-12916.2002.
    • (2002) J. Virol. , vol.76 , pp. 12908-12916
    • Canto, T.1    Palukaitis, P.2
  • 21
    • 66149100998 scopus 로고    scopus 로고
    • Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein
    • Martinez-Gil L, Sanchez-Navarro JA, Cruz A, Pallas V, Perez-Gil J, Mingarro I. 2009. Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein. J. Virol. 83: 5535-5543. http://dx.doi.org/10.1128/JVI.00393-09.
    • (2009) J. Virol. , vol.83 , pp. 5535-5543
    • Martinez-Gil, L.1    Sanchez-Navarro, J.A.2    Cruz, A.3    Pallas, V.4    Perez-Gil, J.5    Mingarro, I.6
  • 23
    • 55549108720 scopus 로고    scopus 로고
    • The surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membrane
    • Martinez-Gil L, Perez-Gil J, Mingarro I. 2008. The surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membrane. Biophys. J. 95:L36-38. http://dx.doi.org /10.1529/biophysj.108.138602.
    • (2008) Biophys. J. , vol.95
    • Martinez-Gil, L.1    Perez-Gil, J.2    Mingarro, I.3
  • 24
    • 23244439546 scopus 로고    scopus 로고
    • Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement
    • Herranz MC, Sanchez-Navarro JA, Sauri A, Mingarro I, Pallas V. 2005. Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement. Virology 339:31-41. http://dx.doi.org/10.1016/j .virol.2005.05.020.
    • (2005) Virology , vol.339 , pp. 31-41
    • Herranz, M.C.1    Sanchez-Navarro, J.A.2    Sauri, A.3    Mingarro, I.4    Pallas, V.5
  • 26
    • 33744784810 scopus 로고    scopus 로고
    • In vitro and in vivo mapping of the Prunus necrotic ringspot virus coat protein C-terminal dimerization domain by bimolecular fluorescence complementation
    • Aparicio F, Sanchez-Navarro JA, Pallas V. 2006. In vitro and in vivo mapping of the Prunus necrotic ringspot virus coat protein C-terminal dimerization domain by bimolecular fluorescence complementation. J. Gen. Virol. 87:1745-1750. http://dx.doi.org/10.1099/vir.0.81696-0.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1745-1750
    • Aparicio, F.1    Sanchez-Navarro, J.A.2    Pallas, V.3
  • 27
    • 1842457749 scopus 로고    scopus 로고
    • Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum
    • Peremyslov VV, Pan YW, Dolja VV. 2004. Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum. J. Virol. 78:3704-3709. http://dx.doi.org/10.1128 /JVI.78.7.3704-3709.2004.
    • (2004) J. Virol. , vol.78 , pp. 3704-3709
    • Peremyslov, V.V.1    Pan, Y.W.2    Dolja, V.V.3
  • 28
    • 0032006057 scopus 로고    scopus 로고
    • Stop-transfer function of pseudorandom amino acid segments during translocation across prokaryotic and eukaryotic membranes
    • Saaf A, Wallin E, von Heijne G. 1998. Stop-transfer function of pseudorandom amino acid segments during translocation across prokaryotic and eukaryotic membranes. Eur. J. Biochem. 251:821-829. http://dx.doi.org /10.1046/j.1432-1327.1998.2510821.x.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 821-829
    • Saaf, A.1    Wallin, E.2    von Heijne, G.3
  • 29
    • 34848883056 scopus 로고    scopus 로고
    • Membrane insertion and topology of the p7B movement protein of Melon Necrotic Spot Virus (MNSV)
    • Martinez-Gil L, Sauri A, Vilar M, Pallas V, Mingarro I. 2007. Membrane insertion and topology of the p7B movement protein of Melon Necrotic Spot Virus (MNSV). Virology 367:348-357. http://dx.doi.org/10.1016/j .virol.2007.06.006.
    • (2007) Virology , vol.367 , pp. 348-357
    • Martinez-Gil, L.1    Sauri, A.2    Vilar, M.3    Pallas, V.4    Mingarro, I.5
  • 31
    • 79951680382 scopus 로고    scopus 로고
    • Membrane insertion and topology of the translocating chain-associating membrane protein (TRAM)
    • Tamborero S, Vilar M, Martinez-Gil L, Johnson AE, Mingarro I. 2011. Membrane insertion and topology of the translocating chain-associating membrane protein (TRAM). J. Mol. Biol. 406:571-582. http://dx.doi.org /10.1016/j.jmb.2011.01.009.
    • (2011) J. Mol. Biol. , vol.406 , pp. 571-582
    • Tamborero, S.1    Vilar, M.2    Martinez-Gil, L.3    Johnson, A.E.4    Mingarro, I.5
  • 32
    • 84857439394 scopus 로고    scopus 로고
    • Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix
    • Ojemalm K, Halling KK, Nilsson I, von Heijne G. 2012. Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix. Mol. Cell 45:529-540. http://dx.doi .org/10.1016/j.molcel.2011.12.024.
    • (2012) Mol. Cell , vol.45 , pp. 529-540
    • Ojemalm, K.1    Halling, K.K.2    Nilsson, I.3    von Heijne, G.4
  • 33
    • 84873405886 scopus 로고    scopus 로고
    • Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion
    • Bano-Polo M, Martinez-Gil L, Wallner B, Nieva JL, Elofsson A, Mingarro I. 2013. Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion. J. Mol. Biol. 425:830-840. http://dx.doi.org/10.1016/j.jmb.2012.12.001.
    • (2013) J. Mol. Biol. , vol.425 , pp. 830-840
    • Bano-Polo, M.1    Martinez-Gil, L.2    Wallner, B.3    Nieva, J.L.4    Elofsson, A.5    Mingarro, I.6
  • 34
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 35
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola TK. 2008. Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu. Rev. Biophys. 37:465-487. http://dx.doi.org/10.1146/annurev.biophys.37.032807 .125842.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 36
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gafvelin G, Sakaguchi M, Andersson H, von Heijne G. 1997. Topological rules for membrane protein assembly in eukaryotic cells. J. Biol. Chem. 272:6119-6127. http://dx.doi.org/10.1074/jbc.272.10.6119.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6119-6127
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    von Heijne, G.4
  • 37
    • 0042313962 scopus 로고    scopus 로고
    • Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
    • Goder V, Spiess M. 2003. Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. EMBO J. 22:3645-3653. http://dx .doi.org/10.1093/emboj/cdg361.
    • (2003) EMBO J. , vol.22 , pp. 3645-3653
    • Goder, V.1    Spiess, M.2
  • 38
    • 61449167824 scopus 로고    scopus 로고
    • Viral membrane protein topology is dictated by multiple determinants in its sequence
    • Sauri A, Tamborero S, Martinez-Gil L, Johnson AE, Mingarro I. 2009. Viral membrane protein topology is dictated by multiple determinants in its sequence. J. Mol. Biol. 387:113-128. http://dx.doi.org/10.1016/j.jmb .2009.01.063.
    • (2009) J. Mol. Biol. , vol.387 , pp. 113-128
    • Sauri, A.1    Tamborero, S.2    Martinez-Gil, L.3    Johnson, A.E.4    Mingarro, I.5
  • 40
    • 34548238709 scopus 로고    scopus 로고
    • A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication
    • Netherton C, Moffat K, Brooks E, Wileman T. 2007. A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication. Adv. Virus Res. 70:101-182. http://dx.doi.org/10 .1016/S0065-3527(07)70004-0.
    • (2007) Adv. Virus Res. , vol.70 , pp. 101-182
    • Netherton, C.1    Moffat, K.2    Brooks, E.3    Wileman, T.4
  • 41
    • 55349092040 scopus 로고    scopus 로고
    • Localization of the carnation Italian ringspot virus replication protein p36 to the mitochondrial outer membrane is mediated by an internal targeting signal and the TOM complex
    • Hwang YT, McCartney AW, Gidda SK, Mullen RT. 2008. Localization of the carnation Italian ringspot virus replication protein p36 to the mitochondrial outer membrane is mediated by an internal targeting signal and the TOM complex. BMC Cell Biol. 9:54. http://dx.doi.org/10.1186/1471-2121-9-54.
    • (2008) BMC Cell Biol. , vol.9 , pp. 54
    • Hwang, Y.T.1    McCartney, A.W.2    Gidda, S.K.3    Mullen, R.T.4
  • 42
    • 70449659058 scopus 로고    scopus 로고
    • Plant viruses spread by diffusion on ER-associated movement-protein-rafts through plasmodesmata gated by viral induced host beta-1,3-glucanases
    • Epel BL. 2009. Plant viruses spread by diffusion on ER-associated movement-protein-rafts through plasmodesmata gated by viral induced host beta-1,3-glucanases. Semin. Cell Dev. Biol. 20:1074-1081. http://dx.doi .org/10.1016/j.semcdb.2009.05.010.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 1074-1081
    • Epel, B.L.1
  • 43
    • 0037189492 scopus 로고    scopus 로고
    • Insertion and topology of a plant viral movement protein in the endoplasmic reticulum membrane
    • Vilar M, Sauri A, Monne M, Marcos JF, von Heijne G, Perez-Paya E, Mingarro I. 2002. Insertion and topology of a plant viral movement protein in the endoplasmic reticulum membrane. J. Biol. Chem. 277:23447-23452. http://dx.doi.org/10.1074/jbc.M202935200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23447-23452
    • Vilar, M.1    Sauri, A.2    Monne, M.3    Marcos, J.F.4    von Heijne, G.5    Perez-Paya, E.6    Mingarro, I.7
  • 44
    • 77951985719 scopus 로고    scopus 로고
    • Membrane insertion and biogenesis of the Turnip crinkle virus p9 movement protein
    • Martinez-Gil L, Johnson AE, Mingarro I. 2010. Membrane insertion and biogenesis of the Turnip crinkle virus p9 movement protein. J. Virol. 84:5520-5527. http://dx.doi.org/10.1128/JVI.00125-10.
    • (2010) J. Virol. , vol.84 , pp. 5520-5527
    • Martinez-Gil, L.1    Johnson, A.E.2    Mingarro, I.3
  • 45
    • 79960397172 scopus 로고    scopus 로고
    • Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement
    • Genoves A, Pallas V, Navarro JA. 2011. Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement. J. Virol. 85:7797-7809. http://dx.doi.org/10.1128/JVI.02465-10.
    • (2011) J. Virol. , vol.85 , pp. 7797-7809
    • Genoves, A.1    Pallas, V.2    Navarro, J.A.3
  • 46
    • 77952681783 scopus 로고    scopus 로고
    • Binding of monoclonal antibodies to the movement protein (MP) of Tobacco mosaic virus: influence of subcellular MP localization and phosphorylation
    • Tyulkina LG, Karger EM, Sheveleva AA, Atabekov JG. 2010. Binding of monoclonal antibodies to the movement protein (MP) of Tobacco mosaic virus: influence of subcellular MP localization and phosphorylation. J. Gen. Virol. 91:1621-1628. http://dx.doi.org/10.1099/vir.0.018002-0.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1621-1628
    • Tyulkina, L.G.1    Karger, E.M.2    Sheveleva, A.A.3    Atabekov, J.G.4
  • 47
    • 0033769694 scopus 로고    scopus 로고
    • Function of microtubules in intercellular transport of plant virus RNA
    • Boyko V, Ferralli J, Ashby J, Schellenbaum P, Heinlein M. 2000. Function of microtubules in intercellular transport of plant virus RNA. Nat. Cell Biol. 2:826-832. http://dx.doi.org/10.1038/35041072.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 826-832
    • Boyko, V.1    Ferralli, J.2    Ashby, J.3    Schellenbaum, P.4    Heinlein, M.5
  • 48
    • 33748646985 scopus 로고    scopus 로고
    • Tobacco mosaic virus movement protein functions as a structural microtubule-associated protein
    • Ashby J, Boutant E, Seemanpillai M, Groner A, Sambade A, Ritzenthaler C, Heinlein M. 2006. Tobacco mosaic virus movement protein functions as a structural microtubule-associated protein. J. Virol. 80:8329-8344. http://dx.doi.org/10.1128/JVI.00540-06.
    • (2006) J. Virol. , vol.80 , pp. 8329-8344
    • Ashby, J.1    Boutant, E.2    Seemanpillai, M.3    Groner, A.4    Sambade, A.5    Ritzenthaler, C.6    Heinlein, M.7
  • 49
    • 0025064239 scopus 로고
    • The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein
    • Citovsky V, Knorr D, Schuster G, Zambryski P. 1990. The P30 movement protein of tobacco mosaic virus is a single-strand nucleic acid binding protein. Cell 60:637-647. http://dx.doi.org/10.1016/0092-8674(90) 90667-4.
    • (1990) Cell , vol.60 , pp. 637-647
    • Citovsky, V.1    Knorr, D.2    Schuster, G.3    Zambryski, P.4
  • 50
    • 34247548749 scopus 로고    scopus 로고
    • The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains two independent single resistancebreaking domains
    • Strasser M, Pfitzner AJ. 2007. The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains two independent single resistancebreaking domains. Arch. Virol. 152:903-914. http://dx.doi.org/10.1007 /s00705-006-0915-8.
    • (2007) Arch. Virol. , vol.152 , pp. 903-914
    • Strasser, M.1    Pfitzner, A.J.2
  • 52
    • 0032213491 scopus 로고    scopus 로고
    • Calreticulin expression in plant cells: developmental regulation, tissue specificity and intracellular distribution
    • Borisjuk N, Sitailo L, Adler K, Malysheva L, Tewes A, Borisjuk L, Manteuffel R. 1998. Calreticulin expression in plant cells: developmental regulation, tissue specificity and intracellular distribution. Planta 206: 504-514. http://dx.doi.org/10.1007/s004250050427.
    • (1998) Planta , vol.206 , pp. 504-514
    • Borisjuk, N.1    Sitailo, L.2    Adler, K.3    Malysheva, L.4    Tewes, A.5    Borisjuk, L.6    Manteuffel, R.7
  • 53
    • 67249103669 scopus 로고    scopus 로고
    • Calreticulin: conserved protein and diverse functions in plants
    • Jia XY, He LH, Jing RL, Li RZ. 2009. Calreticulin: conserved protein and diverse functions in plants. Physiol. Plant 136:127-138. http://dx.doi.org /10.1111/j.1399-3054.2009.01223.x.
    • (2009) Physiol. Plant , vol.136 , pp. 127-138
    • Jia, X.Y.1    He, L.H.2    Jing, R.L.3    Li, R.Z.4
  • 54
    • 0141675998 scopus 로고    scopus 로고
    • Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells
    • Laporte C, Vetter G, Loudes AM, Robinson DG, Hillmer S, Stussi-Garaud C, Ritzenthaler C. 2003. Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells. Plant Cell 15:2058-2075. http://dx.doi.org/10.1105/tpc.013896.
    • (2003) Plant Cell , vol.15 , pp. 2058-2075
    • Laporte, C.1    Vetter, G.2    Loudes, A.M.3    Robinson, D.G.4    Hillmer, S.5    Stussi-Garaud, C.6    Ritzenthaler, C.7
  • 55
    • 0033971647 scopus 로고    scopus 로고
    • The '30K' superfamily of viral movement proteins
    • Melcher U. 2000. The '30K' superfamily of viral movement proteins. J. Gen. Virol. 81:257-266.
    • (2000) J. Gen. Virol. , vol.81 , pp. 257-266
    • Melcher, U.1
  • 56
    • 32944464131 scopus 로고    scopus 로고
    • Cell-to-cell movement of alfalfa mosaic virus can be mediated by the movement proteins of ilar-, bromo-, cucumo-, tobamo-and comoviruses and does not require virion formation
    • Sanchez-Navarro JA, Carmen Herranz M, Pallas V. 2006. Cell-to-cell movement of alfalfa mosaic virus can be mediated by the movement proteins of ilar-, bromo-, cucumo-, tobamo-and comoviruses and does not require virion formation. Virology 346:66-73. http://dx.doi.org/10.1016 /j.virol.2005.10.024.
    • (2006) Virology , vol.346 , pp. 66-73
    • Sanchez-Navarro, J.A.1    Carmen Herranz, M.2    Pallas, V.3
  • 57
    • 77950478379 scopus 로고    scopus 로고
    • Caulimoviridae tubule-guided transport is dictated by movement protein properties
    • Sanchez-Navarro J, Fajardo T, Zicca S, Pallas V, Stavolone L. 2010. Caulimoviridae tubule-guided transport is dictated by movement protein properties. J. Virol. 84:4109-4112. http://dx.doi.org/10.1128/JVI.02543-09.
    • (2010) J. Virol. , vol.84 , pp. 4109-4112
    • Sanchez-Navarro, J.1    Fajardo, T.2    Zicca, S.3    Pallas, V.4    Stavolone, L.5
  • 58
    • 84874092134 scopus 로고    scopus 로고
    • Systemic transport of Alfalfa mosaic virus can be mediated by the movement proteins of several viruses assigned to five genera of the 30K family
    • Fajardo TV, Peiro A, Pallas V, Sanchez-Navarro J. 2013. Systemic transport of Alfalfa mosaic virus can be mediated by the movement proteins of several viruses assigned to five genera of the 30K family. J. Gen. Virol. 94:677-681. http://dx.doi.org/10.1099/vir.0.048793-0.
    • (2013) J. Gen. Virol. , vol.94 , pp. 677-681
    • Fajardo, T.V.1    Peiro, A.2    Pallas, V.3    Sanchez-Navarro, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.