메뉴 건너뛰기




Volumn 160, Issue 1, 2012, Pages 72-82

Ubiquitin and plant viruses, let's play together!

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84866050952     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.112.201905     Document Type: Article
Times cited : (100)

References (84)
  • 1
    • 27244458549 scopus 로고    scopus 로고
    • Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol
    • Aparicio F, Thomas CL, Lederer C, Niu Y, Wang D, Maule AJ (2005) Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol. Plant Physiol 138: 529-536.
    • (2005) Plant Physiol , vol.138 , pp. 529-536
    • Aparicio, F.1    Thomas, C.L.2    Lederer, C.3    Niu, Y.4    Wang, D.5    Maule, A.J.6
  • 2
    • 0030465409 scopus 로고    scopus 로고
    • Induction of HSP70 and polyubiquitin expression associated with plant virus replication
    • Aranda MA, Escaler M, Wang D, Maule AJ (1996) Induction of HSP70 and polyubiquitin expression associated with plant virus replication. Proc Natl Acad Sci USA 93: 15289-15293.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15289-15293
    • Aranda, M.A.1    Escaler, M.2    Wang, D.3    Maule, A.J.4
  • 4
    • 0025685244 scopus 로고
    • Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations and necrotic lesions in a higher plant
    • Bachmair A, Becker F, Masterson RV, Schell J (1990) Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations and necrotic lesions in a higher plant. EMBO J 9: 4543-4549.
    • (1990) EMBO J , vol.9 , pp. 4543-4549
    • Bachmair, A.1    Becker, F.2    Masterson, R.V.3    Schell, J.4
  • 5
    • 0035209519 scopus 로고    scopus 로고
    • Ubiquitylation in plants: A post-genomic look at a post-translational modification
    • Bachmair A, Novatchkova M, Potuschak T, Eisenhaber F (2001) Ubiquitylation in plants: a post-genomic look at a post-translational modification. Trends Plant Sci 6: 463-470.
    • (2001) Trends Plant Sci , vol.6 , pp. 463-470
    • Bachmair, A.1    Novatchkova, M.2    Potuschak, T.3    Eisenhaber, F.4
  • 6
    • 74549189980 scopus 로고    scopus 로고
    • A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus
    • Barajas D, Jiang Y, Nagy PD (2009a) A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus. PLoS Pathog 5: e1000705.
    • (2009) PLoS Pathog , vol.5
    • Barajas, D.1    Jiang, Y.2    Nagy, P.D.3
  • 7
    • 70350320561 scopus 로고    scopus 로고
    • The Nedd4-type Rsp5p ubiquitin ligase inhibits tombusvirus replication by regulating degradation of the p92 replication protein and decreasing the activity of the tombusvirus replicase
    • Barajas D, Li Z, Nagy PD (2009b) The Nedd4-type Rsp5p ubiquitin ligase inhibits tombusvirus replication by regulating degradation of the p92 replication protein and decreasing the activity of the tombusvirus replicase. J Virol 83: 11751-11764.
    • (2009) J Virol , vol.83 , pp. 11751-11764
    • Barajas, D.1    Li, Z.2    Nagy, P.D.3
  • 8
    • 75749102524 scopus 로고    scopus 로고
    • Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein
    • Barajas D, Nagy PD (2010) Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein. Virology 397: 358-368.
    • (2010) Virology , vol.397 , pp. 358-368
    • Barajas, D.1    Nagy, P.D.2
  • 9
    • 34548474870 scopus 로고    scopus 로고
    • The polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation
    • Baumberger N, Tsai C-H, Lie M, Havecker E, Baulcombe DC (2007) The polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation. Curr Biol 17: 1609-1614.
    • (2007) Curr Biol , vol.17 , pp. 1609-1614
    • Baumberger, N.1    Tsai, C.-H.2    Lie, M.3    Havecker, E.4    Baulcombe, D.C.5
  • 10
    • 0000810989 scopus 로고
    • Altered response to viral infection by tobacco plants perturbed in ubiquitin system
    • Becker F, Buschfeld E, Schell J, Bachmair A (1993) Altered response to viral infection by tobacco plants perturbed in ubiquitin system. Plant J 3: 875-881.
    • (1993) Plant J , vol.3 , pp. 875-881
    • Becker, F.1    Buschfeld, E.2    Schell, J.3    Bachmair, A.4
  • 12
    • 78049473996 scopus 로고    scopus 로고
    • The ubiquitinproteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection
    • Camborde L, Planchais S, Tournier V, Jakubiec A, Drugeon G, Lacassagne E, Pflieger S, Chenon M, Jupin I (2010) The ubiquitinproteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection. Plant Cell 22: 3142-3152.
    • (2010) Plant Cell , vol.22 , pp. 3142-3152
    • Camborde, L.1    Planchais, S.2    Tournier, V.3    Jakubiec, A.4    Drugeon, G.5    Lacassagne, E.6    Pflieger, S.7    Chenon, M.8    Jupin, I.9
  • 13
    • 1542317734 scopus 로고    scopus 로고
    • Interaction between a geminivirus replication protein and the plant sumoylation system
    • Castillo AG, Kong LJ, Hanley-Bowdoin L, Bejarano ER (2004) Interaction between a geminivirus replication protein and the plant sumoylation system. J Virol 78: 2758-2769.
    • (2004) J Virol , vol.78 , pp. 2758-2769
    • Castillo, A.G.1    Kong, L.J.2    Hanley-Bowdoin, L.3    Bejarano, E.R.4
  • 14
    • 2442604466 scopus 로고    scopus 로고
    • Viral virulence protein suppresses RNA silencing-mediated defense but upregulates the role of microRNA in host gene expression
    • Chen J, Li WX, Xie D, Peng JR, Ding SW (2004) Viral virulence protein suppresses RNA silencing-mediated defense but upregulates the role of microRNA in host gene expression. Plant Cell 16: 1302-1313.
    • (2004) Plant Cell , vol.16 , pp. 1302-1313
    • Chen, J.1    Li, W.X.2    Xie, D.3    Peng, J.R.4    Ding, S.W.5
  • 15
    • 84856468838 scopus 로고    scopus 로고
    • A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity
    • Chenon M, Camborde L, Cheminant S, Jupin I (2012) A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity. EMBO J 31: 741-753.
    • (2012) EMBO J , vol.31 , pp. 741-753
    • Chenon, M.1    Camborde, L.2    Cheminant, S.3    Jupin, I.4
  • 16
    • 77955255337 scopus 로고    scopus 로고
    • The silencing suppressor P25 of Potato virus X interacts with Argonaute1 and mediates its degradation through the proteasome pathway
    • Chiu MH, Chen IH, Baulcombe DC, Tsai CH (2010) The silencing suppressor P25 of Potato virus X interacts with Argonaute1 and mediates its degradation through the proteasome pathway. Mol Plant Pathol 11: 641-649.
    • (2010) Mol Plant Pathol , vol.11 , pp. 641-649
    • Chiu, M.H.1    Chen, I.H.2    Baulcombe, D.C.3    Tsai, C.H.4
  • 18
    • 77950953211 scopus 로고    scopus 로고
    • Polerovirus protein P0 prevents the assembly of small RNA-containing RISC complexes and leads to degradation of ARGONAUTE1
    • Csorba T, Lózsa R, Hutvágner G, Burgyán J (2010) Polerovirus protein P0 prevents the assembly of small RNA-containing RISC complexes and leads to degradation of ARGONAUTE1. Plant J 62: 463-472.
    • (2010) Plant J , vol.62 , pp. 463-472
    • Csorba, T.1    Lózsa, R.2    Hutvágner, G.3    Burgyán, J.4
  • 19
    • 75149157140 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome system in plant-pathogen interactions: A neverending hide-and-seek game
    • Dielen A-S, Badaoui S, Candresse T, German-Retana S (2010) The ubiquitin/26S proteasome system in plant-pathogen interactions: a neverending hide-and-seek game. Mol Plant Pathol 11: 293-308.
    • (2010) Mol Plant Pathol , vol.11 , pp. 293-308
    • Dielen, A.-S.1    Badaoui, S.2    Candresse, T.3    German-Retana, S.4
  • 20
    • 77956170809 scopus 로고    scopus 로고
    • RNA-based antiviral immunity
    • Ding SW (2010) RNA-based antiviral immunity. Nat Rev Immunol 10: 632-644.
    • (2010) Nat Rev Immunol , vol.10 , pp. 632-644
    • Ding, S.W.1
  • 21
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • Dreher K, Callis J (2007) Ubiquitin, hormones and biotic stress in plants. Ann Bot (Lond) 99: 787-822.
    • (2007) Ann Bot (Lond) , vol.99 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 22
    • 0036936858 scopus 로고    scopus 로고
    • Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway
    • Drugeon G, Jupin I (2002) Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway. J Gen Virol 83: 3187-3197.
    • (2002) J Gen Virol , vol.83 , pp. 3187-3197
    • Drugeon, G.1    Jupin, I.2
  • 23
    • 0024041480 scopus 로고
    • Tobacco mosaic virus particles contain ubiquitinated coat protein subunits
    • Dunigan DD, Dietzgen RG, Schoelz JE, Zaitlin M (1988) Tobacco mosaic virus particles contain ubiquitinated coat protein subunits. Virology 165: 310-312.
    • (1988) Virology , vol.165 , pp. 310-312
    • Dunigan, D.D.1    Dietzgen, R.G.2    Schoelz, J.E.3    Zaitlin, M.4
  • 24
    • 66449130348 scopus 로고    scopus 로고
    • Interaction with a host ubiquitin-conjugating enzyme is required for the pathogenicity of a geminiviral DNA beta satellite
    • Eini O, Dogra S, Selth LA, Dry IB, Randles JW, Rezaian MA (2009) Interaction with a host ubiquitin-conjugating enzyme is required for the pathogenicity of a geminiviral DNA beta satellite. Mol Plant Microbe Interact 22: 737-746.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 737-746
    • Eini, O.1    Dogra, S.2    Selth, L.A.3    Dry, I.B.4    Randles, J.W.5    Rezaian, M.A.6
  • 25
    • 84857788515 scopus 로고    scopus 로고
    • The Enamovirus P0 protein is a silencing suppressor which inhibits local and systemic RNA silencing through AGO1 degradation
    • Fusaro AF, Correa RL, Nakasugi K, Jackson C, Kawchuk L, Vaslin MFS, Waterhouse PM (2012) The Enamovirus P0 protein is a silencing suppressor which inhibits local and systemic RNA silencing through AGO1 degradation. Virology 426: 178-187.
    • (2012) Virology , vol.426 , pp. 178-187
    • Fusaro, A.F.1    Correa, R.L.2    Nakasugi, K.3    Jackson, C.4    Kawchuk, L.5    Vaslin, M.F.S.6    Waterhouse, P.M.7
  • 26
    • 0037143725 scopus 로고    scopus 로고
    • The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis
    • Gagne JM, Downes BP, Shiu SH, Durski AM, Vierstra RD (2002) The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc Natl Acad Sci USA 99: 11519-11524.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11519-11524
    • Gagne, J.M.1    Downes, B.P.2    Shiu, S.H.3    Durski, A.M.4    Vierstra, R.D.5
  • 27
    • 80051948564 scopus 로고    scopus 로고
    • Systematic identification of novel, essential host genes affecting bromovirus RNA replication
    • Gancarz BL, Hao L, He Q, Newton MA, Ahlquist P (2011) Systematic identification of novel, essential host genes affecting bromovirus RNA replication. PLoS ONE 6: e23988.
    • (2011) PLoS ONE , vol.6
    • Gancarz, B.L.1    Hao, L.2    He, Q.3    Newton, M.A.4    Ahlquist, P.5
  • 28
    • 0035983836 scopus 로고    scopus 로고
    • Functional analysis of a DNA-shuffled movement protein reveals that microtubules are dispensable for the cellto-cell movement of Tobacco mosaic virus
    • Gillespie T, Boevink P, Haupt S, Roberts AG, Toth R, Valentine T, Chapman S, Oparka KJ (2002) Functional analysis of a DNA-shuffled movement protein reveals that microtubules are dispensable for the cellto-cell movement of Tobacco mosaic virus. Plant Cell 14: 1207-1222.
    • (2002) Plant Cell , vol.14 , pp. 1207-1222
    • Gillespie, T.1    Boevink, P.2    Haupt, S.3    Roberts, A.G.4    Toth, R.5    Valentine, T.6    Chapman, S.7    Oparka, K.J.8
  • 29
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 30
    • 0025289848 scopus 로고
    • Ubiquitinated conjugates are found in preparations of several plant viruses
    • Hazelwood D, Zaitlin M (1990) Ubiquitinated conjugates are found in preparations of several plant viruses. Virology 177: 352-356.
    • (1990) Virology , vol.177 , pp. 352-356
    • Hazelwood, D.1    Zaitlin, M.2
  • 31
    • 0034662167 scopus 로고    scopus 로고
    • Evidence for phosphorylation and ubiquitinylation of the turnip yellow mosaic virus RNA-dependent RNA polymerase domain expressed in a baculovirus-insect cell system
    • Héricourt F, Blanc S, Redeker V, Jupin I (2000) Evidence for phosphorylation and ubiquitinylation of the turnip yellow mosaic virus RNA-dependent RNA polymerase domain expressed in a baculovirus-insect cell system. Biochem J 349: 417-425.
    • (2000) Biochem J , vol.349 , pp. 417-425
    • Héricourt, F.1    Blanc, S.2    Redeker, V.3    Jupin, I.4
  • 32
    • 44949242505 scopus 로고    scopus 로고
    • Regulation of cullin RING ligases
    • Hotton SK, Callis J (2008) Regulation of cullin RING ligases. Annu Rev Plant Biol 59: 467-489.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 467-489
    • Hotton, S.K.1    Callis, J.2
  • 33
    • 79955642715 scopus 로고    scopus 로고
    • The cullin-RING ubiquitin-protein ligases
    • Hua Z, Vierstra RD (2009) The cullin-RING ubiquitin-protein ligases. Annu Rev Plant Biol 62: 299-334.
    • (2009) Annu Rev Plant Biol , vol.62 , pp. 299-334
    • Hua, Z.1    Vierstra, R.D.2
  • 34
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda F, Dikic I (2008) Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep 9: 536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 35
    • 67649391002 scopus 로고    scopus 로고
    • Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection
    • Isaacson MK, Ploegh HL (2009) Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection. Cell Host Microbe 5: 559-570.
    • (2009) Cell Host Microbe , vol.5 , pp. 559-570
    • Isaacson, M.K.1    Ploegh, H.L.2
  • 36
    • 0038540537 scopus 로고    scopus 로고
    • Misfolded plant virus proteins: Elicitors and targets of ubiquitylation
    • Jockusch H, Wiegand C (2003) Misfolded plant virus proteins: elicitors and targets of ubiquitylation. FEBS Lett 545: 229-232.
    • (2003) FEBS Lett , vol.545 , pp. 229-232
    • Jockusch, H.1    Wiegand, C.2
  • 37
    • 42749085697 scopus 로고    scopus 로고
    • Mutational analysis of PVX TGBp3 links subcellular accumulation and protein turnover
    • Ju H-J, Ye C-M, Verchot-Lubicz J (2008) Mutational analysis of PVX TGBp3 links subcellular accumulation and protein turnover. Virology 375: 103-117.
    • (2008) Virology , vol.375 , pp. 103-117
    • Ju, H.-J.1    Ye, C.-M.2    Verchot-Lubicz, J.3
  • 38
    • 0034870426 scopus 로고    scopus 로고
    • Degradation signals within both terminal domains of the cauliflower mosaic virus capsid protein precursor
    • Karsies A, Hohn T, Leclerc D (2001) Degradation signals within both terminal domains of the cauliflower mosaic virus capsid protein precursor. Plant J 27: 335-343.
    • (2001) Plant J , vol.27 , pp. 335-343
    • Karsies, A.1    Hohn, T.2    Leclerc, D.3
  • 39
    • 84865836123 scopus 로고    scopus 로고
    • Ubiquitin-mediated Control of Plant Hormone Signaling
    • (in Press)
    • Kelley DR, Estelle M (2012) Ubiquitin-mediated control of plant hormone signaling. Plant Physiol (in press).
    • (2012) Plant Physiol
    • Kelley, D.R.1    Estelle, M.2
  • 40
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbé S (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 42
    • 34247093872 scopus 로고    scopus 로고
    • The nanovirus-encoded Clink protein affects plant cell cycle regulation through interaction with the retinoblastoma-related protein
    • Lageix S, Catrice O, Deragon J-M, Gronenborn B, Pélissier T, Ramírez BC (2007) The nanovirus-encoded Clink protein affects plant cell cycle regulation through interaction with the retinoblastoma-related protein. J Virol 81: 4177-4185.
    • (2007) J Virol , vol.81 , pp. 4177-4185
    • Lageix, S.1    Catrice, O.2    Deragon, J.-M.3    Gronenborn, B.4    Pélissier, T.5    Ramírez, B.C.6
  • 43
    • 61349141825 scopus 로고    scopus 로고
    • RKP, a RING finger E3 ligase induced by BSCTV C4 protein, affects geminivirus infection by regulation of the plant cell cycle
    • Lai J, Chen H, Teng K, Zhao Q, Zhang Z, Li Y, Liang L, Xia R, Wu Y, Guo H, et al (2009) RKP, a RING finger E3 ligase induced by BSCTV C4 protein, affects geminivirus infection by regulation of the plant cell cycle. Plant J 57: 905-917.
    • (2009) Plant J , vol.57 , pp. 905-917
    • Lai, J.1    Chen, H.2    Teng, K.3    Zhao, Q.4    Zhang, Z.5    Li, Y.6    Liang, L.7    Xia, R.8    Wu, Y.9    Guo, H.10
  • 45
    • 47049126717 scopus 로고    scopus 로고
    • Cdc34p ubiquitinconjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein
    • Li Z, Barajas D, Panavas T, Herbst DA, Nagy PD (2008) Cdc34p ubiquitinconjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein. J Virol 82: 6911-6926.
    • (2008) J Virol , vol.82 , pp. 6911-6926
    • Li, Z.1    Barajas, D.2    Panavas, T.3    Herbst, D.A.4    Nagy, P.D.5
  • 46
    • 85052276713 scopus 로고    scopus 로고
    • Geminivirus C2 protein might be the key player for geminiviral co-option of SCF-mediated ubiquitination
    • Lozano-Durán R, Bejarano ER (2011) Geminivirus C2 protein might be the key player for geminiviral co-option of SCF-mediated ubiquitination. Plant Signal Behav 6: 999-1001.
    • (2011) Plant Signal Behav , vol.6 , pp. 999-1001
    • Lozano-Durán, R.1    Bejarano, E.R.2
  • 47
    • 79955635174 scopus 로고    scopus 로고
    • Geminiviruses subvert ubiquitination by altering CSN-mediated derubylation of SCF E3 ligase complexes and inhibit jasmonate signaling in Arabidopsis thaliana
    • Lozano-Durán R, Rosas-Díaz T, Gusmaroli G, Luna AP, Taconnat L, Deng XW, Bejarano ER (2011a) Geminiviruses subvert ubiquitination by altering CSN-mediated derubylation of SCF E3 ligase complexes and inhibit jasmonate signaling in Arabidopsis thaliana. Plant Cell 23: 1014-1032.
    • (2011) Plant Cell , vol.23 , pp. 1014-1032
    • Lozano-Durán, R.1    Rosas-Díaz, T.2    Gusmaroli, G.3    Luna, A.P.4    Taconnat, L.5    Deng, X.W.6    Bejarano, E.R.7
  • 48
    • 79960821694 scopus 로고    scopus 로고
    • Identification of host genes involved in geminivirus infection using a reverse genetics approach
    • Lozano-Durán R, Rosas-Díaz T, Luna AP, Bejarano ER (2011b) Identification of host genes involved in geminivirus infection using a reverse genetics approach. PLoS ONE 6: e22383.
    • (2011) PLoS ONE , vol.6
    • Lozano-Durán, R.1    Rosas-Díaz, T.2    Luna, A.P.3    Bejarano, E.R.4
  • 49
    • 29244440855 scopus 로고    scopus 로고
    • Plant viral movement proteins: Agents for cell-to-cell trafficking of viral genomes
    • Lucas WJ (2006) Plant viral movement proteins: agents for cell-to-cell trafficking of viral genomes. Virology 344: 169-184.
    • (2006) Virology , vol.344 , pp. 169-184
    • Lucas, W.J.1
  • 50
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • Makarova KS, Aravind L, Koonin EV (2000) A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem Sci 25: 50-52.
    • (2000) Trends Biochem Sci , vol.25 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 51
    • 84865847703 scopus 로고    scopus 로고
    • Ubiquitination During Plant Immune Signaling
    • (in Press)
    • Marino D, Peeters N, Rivas S (2012) Ubiquitination during plant immune signaling. Plant Physiol (in press).
    • (2012) Plant Physiol
    • Marino, D.1    Peeters, N.2    Rivas, S.3
  • 53
    • 0001730306 scopus 로고
    • Virus movement in infected plants
    • Maule AJ (1991) Virus movement in infected plants. Plant Sci 9: 457-473.
    • (1991) Plant Sci , vol.9 , pp. 457-473
    • Maule, A.J.1
  • 54
    • 18844455755 scopus 로고    scopus 로고
    • Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses
    • Panavas T, Serviene E, Brasher J, Nagy PD (2005) Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses. Proc Natl Acad Sci USA 102: 7326-7331.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7326-7331
    • Panavas, T.1    Serviene, E.2    Brasher, J.3    Nagy, P.D.4
  • 56
    • 0035264589 scopus 로고    scopus 로고
    • Detection and subcellular localization of the turnip yellow mosaic virus 66K replication protein in infected cells
    • Prod'homme D, Le Panse S, Drugeon G, Jupin I (2001) Detection and subcellular localization of the turnip yellow mosaic virus 66K replication protein in infected cells. Virology 281: 88-101.
    • (2001) Virology , vol.281 , pp. 88-101
    • Prod'homme, D.1    Le Panse, S.2    Drugeon, G.3    Jupin, I.4
  • 57
    • 65449183853 scopus 로고    scopus 로고
    • Viral avoidance and exploitation of the ubiquitin system
    • Randow F, Lehner PJ (2009) Viral avoidance and exploitation of the ubiquitin system. Nat Cell Biol 11: 527-534.
    • (2009) Nat Cell Biol , vol.11 , pp. 527-534
    • Randow, F.1    Lehner, P.J.2
  • 58
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21: 267-271.
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 59
    • 0034099838 scopus 로고    scopus 로고
    • Degradation of tobacco mosaic virus movement protein by the 26S proteasome
    • Reichel C, Beachy RN (2000) Degradation of tobacco mosaic virus movement protein by the 26S proteasome. J Virol 74: 3330-3337.
    • (2000) J Virol , vol.74 , pp. 3330-3337
    • Reichel, C.1    Beachy, R.N.2
  • 60
    • 41849083802 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases
    • Ren H, Santner A, del Pozo JC, Murray JA, Estelle M (2008) Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases. Plant J 53: 705-716.
    • (2008) Plant J , vol.53 , pp. 705-716
    • Ren, H.1    Santner, A.2    del Pozo, J.C.3    Murray, J.A.4    Estelle, M.5
  • 62
    • 77149153062 scopus 로고    scopus 로고
    • The COP9 signalosome and its role in plant development
    • Schwechheimer C, Isono E (2010) The COP9 signalosome and its role in plant development. Eur J Cell Biol 89: 157-162.
    • (2010) Eur J Cell Biol , vol.89 , pp. 157-162
    • Schwechheimer, C.1    Isono, E.2
  • 63
    • 31144456704 scopus 로고    scopus 로고
    • Screening of the yeast yTHC collection identifies essential host factors affecting tombusvirus RNA recombination
    • Serviene E, Jiang Y, Cheng CP, Baker J, Nagy PD (2006) Screening of the yeast yTHC collection identifies essential host factors affecting tombusvirus RNA recombination. J Virol 80: 1231-1241.
    • (2006) J Virol , vol.80 , pp. 1231-1241
    • Serviene, E.1    Jiang, Y.2    Cheng, C.P.3    Baker, J.4    Nagy, P.D.5
  • 64
    • 27144443077 scopus 로고    scopus 로고
    • Targeting of host-cell ubiquitin pathways by viruses
    • Shackelford J, Pagano JS (2005) Targeting of host-cell ubiquitin pathways by viruses. Essays Biochem 41: 139-156.
    • (2005) Essays Biochem , vol.41 , pp. 139-156
    • Shackelford, J.1    Pagano, J.S.2
  • 65
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith MH, Ploegh HL, Weissman JS (2011) Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334: 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 66
    • 64749086697 scopus 로고    scopus 로고
    • The cytosolic protein response as a subcomponent of the wider heat shock response in Arabidopsis
    • Sugio A, Dreos R, Aparicio F, Maule AJ (2009) The cytosolic protein response as a subcomponent of the wider heat shock response in Arabidopsis. Plant Cell 21: 642-654.
    • (2009) Plant Cell , vol.21 , pp. 642-654
    • Sugio, A.1    Dreos, R.2    Aparicio, F.3    Maule, A.J.4
  • 67
    • 26044454390 scopus 로고    scopus 로고
    • The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones
    • Takizawa M, Goto A, Watanabe Y (2005) The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones. Mol Cells 19: 228-231.
    • (2005) Mol Cells , vol.19 , pp. 228-231
    • Takizawa, M.1    Goto, A.2    Watanabe, Y.3
  • 68
    • 84863590335 scopus 로고    scopus 로고
    • The P25 pathogenicity factor of BNYVV targets the sugar beet 26S proteasome involved in the induction of a hypersensitive resistance response via interaction with an F-box protein
    • Thiel H, Hleibieh K, Gilmer D, Varrelmann M (2012) The P25 pathogenicity factor of BNYVV targets the sugar beet 26S proteasome involved in the induction of a hypersensitive resistance response via interaction with an F-box protein. Mol Plant Microbe Interact 25: 1058-1072.
    • (2012) Mol Plant Microbe Interact , vol.25 , pp. 1058-1072
    • Thiel, H.1    Hleibieh, K.2    Gilmer, D.3    Varrelmann, M.4
  • 69
    • 67650482223 scopus 로고    scopus 로고
    • Identification of Beet necrotic yellow vein virus P25 pathogenicity factor-interacting sugar beet proteins that represent putative virus targets or components of plant resistance
    • Thiel H, Varrelmann M (2009) Identification of Beet necrotic yellow vein virus P25 pathogenicity factor-interacting sugar beet proteins that represent putative virus targets or components of plant resistance. Mol Plant Microbe Interact 22: 999-1010.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 999-1010
    • Thiel, H.1    Varrelmann, M.2
  • 70
    • 80053486846 scopus 로고    scopus 로고
    • To gate, or not to gate: Regulatory mechanisms for intercellular protein transport and virus movement in plants
    • Ueki S, Citovsky V (2011) To gate, or not to gate: regulatory mechanisms for intercellular protein transport and virus movement in plants. Mol Plant 4: 782-793.
    • (2011) Mol Plant , vol.4 , pp. 782-793
    • Ueki, S.1    Citovsky, V.2
  • 71
    • 59149107480 scopus 로고    scopus 로고
    • The SUMO system: An overview
    • Ulrich HD (2009) The SUMO system: an overview. Methods Mol Biol 497: 3-16.
    • (2009) Methods Mol Biol , vol.497 , pp. 3-16
    • Ulrich, H.D.1
  • 72
    • 46149088681 scopus 로고    scopus 로고
    • Plant ARGONAUTES
    • Vaucheret H (2008) Plant ARGONAUTES. Trends Plant Sci 13: 350-358.
    • (2008) Trends Plant Sci , vol.13 , pp. 350-358
    • Vaucheret, H.1
  • 73
    • 67349254570 scopus 로고    scopus 로고
    • The ubiquitin-26S proteasome system at the nexus of plant biology
    • Vierstra RD (2009) The ubiquitin-26S proteasome system at the nexus of plant biology. Nat Rev Mol Cell Biol 10: 385-397.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 385-397
    • Vierstra, R.D.1
  • 74
    • 51849097747 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control and the unfolded protein response: Insights from plants
    • Vitale A, Boston RS (2008) Endoplasmic reticulum quality control and the unfolded protein response: insights from plants. Traffic 9: 1581-1588.
    • (2008) Traffic , vol.9 , pp. 1581-1588
    • Vitale, A.1    Boston, R.S.2
  • 75
    • 34547866723 scopus 로고    scopus 로고
    • Intracellular trafficking of Potato leafroll virus movement protein in transgenic Arabidopsis
    • Vogel F, Hofius D, Sonnewald U (2007) Intracellular trafficking of Potato leafroll virus movement protein in transgenic Arabidopsis. Traffic 8: 1205-1214.
    • (2007) Traffic , vol.8 , pp. 1205-1214
    • Vogel, F.1    Hofius, D.2    Sonnewald, U.3
  • 76
    • 0034730318 scopus 로고    scopus 로고
    • A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana
    • Voinnet O, Lederer C, Baulcombe DC (2000) A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana. Cell 103: 157-167.
    • (2000) Cell , vol.103 , pp. 157-167
    • Voinnet, O.1    Lederer, C.2    Baulcombe, D.C.3
  • 77
    • 79956061717 scopus 로고    scopus 로고
    • Intersection of the multivesicular body pathway and lipid homeostasis in RNA replication by a positive-strand RNA virus
    • Wang X, Diaz A, Hao L, Gancarz B, den Boon JA, Ahlquist P (2011) Intersection of the multivesicular body pathway and lipid homeostasis in RNA replication by a positive-strand RNA virus. J Virol 85: 5494-5503.
    • (2011) J Virol , vol.85 , pp. 5494-5503
    • Wang, X.1    Diaz, A.2    Hao, L.3    Gancarz, B.4    den Boon, J.A.5    Ahlquist, P.6
  • 78
    • 0037261908 scopus 로고    scopus 로고
    • Diverse RNA viruses elicit the expression of common sets of genes in susceptible Arabidopsis thaliana plants
    • Whitham SA, Quan S, Chang HS, Cooper B, Estes B, Zhu T, Wang X, Hou YM (2003) Diverse RNA viruses elicit the expression of common sets of genes in susceptible Arabidopsis thaliana plants. Plant J 33: 271-283.
    • (2003) Plant J , vol.33 , pp. 271-283
    • Whitham, S.A.1    Quan, S.2    Chang, H.S.3    Cooper, B.4    Estes, B.5    Zhu, T.6    Wang, X.7    Hou, Y.M.8
  • 79
    • 33845441117 scopus 로고    scopus 로고
    • Dissecting the ubiquitin pathway by mass spectrometry
    • Xu P, Peng J (2006) Dissecting the ubiquitin pathway by mass spectrometry. Biochim Biophys Acta 1764: 1940-1947.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1940-1947
    • Xu, P.1    Peng, J.2
  • 81
    • 79958043215 scopus 로고    scopus 로고
    • The unfolded protein response is triggered by a plant viral movement protein
    • Ye C, Dickman MB, Whitham SA, Payton M, Verchot J (2011) The unfolded protein response is triggered by a plant viral movement protein. Plant Physiol 156: 741-755.
    • (2011) Plant Physiol , vol.156 , pp. 741-755
    • Ye, C.1    Dickman, M.B.2    Whitham, S.A.3    Payton, M.4    Verchot, J.5
  • 82
    • 79961181356 scopus 로고    scopus 로고
    • Role of unfolded protein response in plant virus infection
    • Ye C, Verchot J (2011) Role of unfolded protein response in plant virus infection. Plant Signal Behav 6: 1212-1215.
    • (2011) Plant Signal Behav , vol.6 , pp. 1212-1215
    • Ye, C.1    Verchot, J.2
  • 83
    • 33745618707 scopus 로고    scopus 로고
    • Ubiquitination-mediated protein degradation and modification: An emerging theme in plant-microbe interactions
    • Zeng LR, Vega-Sánchez ME, Zhu T, Wang GL (2006) Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions. Cell Res 16: 413-426.
    • (2006) Cell Res , vol.16 , pp. 413-426
    • Zeng, L.R.1    Vega-Sánchez, M.E.2    Zhu, T.3    Wang, G.L.4
  • 84
    • 79952292398 scopus 로고    scopus 로고
    • BSCTV C2 attenuates the degradation of SAMDC1 to suppress DNA methylation-mediated gene silencing in Arabidopsis
    • Zhang Z, Chen H, Huang X, Xia R, Zhao Q, Lai J, Teng K, Li Y, Liang L, Du Q, et al (2011) BSCTV C2 attenuates the degradation of SAMDC1 to suppress DNA methylation-mediated gene silencing in Arabidopsis. Plant Cell 23: 273-288.
    • (2011) Plant Cell , vol.23 , pp. 273-288
    • Zhang, Z.1    Chen, H.2    Huang, X.3    Xia, R.4    Zhao, Q.5    Lai, J.6    Teng, K.7    Li, Y.8    Liang, L.9    Du, Q.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.