메뉴 건너뛰기




Volumn 23, Issue 12, 2011, Pages 4298-4317

Erratum: The RPT2 Subunit of the 26S Proteasome Directs Complex Assembly, Histone Dynamics, and Gametophyte and Sporophyte Development in Arabidopsis (The Plant Cell, (2011) 23: 12 (4298–4317) DOI: 10.1105/tpc.111.089482);The RPT2 subunit of the 26S proteasome directs complex assembly, histone dynamics, and gametophyte and sporophyte development in arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 84863012234     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1093/plcell/koac170     Document Type: Erratum
Times cited : (43)

References (87)
  • 1
    • 84907126147 scopus 로고
    • Differential staining of aborted and nonaborted pollen
    • Alexander, M.P. (1969). Differential staining of aborted and nonaborted pollen. Stain Technol. 44: 117-122.
    • (1969) Stain Technol , vol.44 , pp. 117-122
    • Alexander, M.P.1
  • 2
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., et al. (2003). Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301: 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1
  • 4
    • 0242290313 scopus 로고    scopus 로고
    • Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote
    • Boisson, B., Giglione, C., and Meinnel, T. (2003). Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote. J. Biol. Chem. 278: 43418-43429.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43418-43429
    • Boisson, B.1    Giglione, C.2    Meinnel, T.3
  • 5
    • 77955485244 scopus 로고    scopus 로고
    • Affinity purification of the Arabidopsis 26S proteasome reveals a diverse array of plant proteolytic complexes
    • Book, A.J., Gladman, N.P., Lee, S.S., Scalf, M., Smith, L.M., and Vierstra, R.D. (2010). Affinity purification of the Arabidopsis 26S proteasome reveals a diverse array of plant proteolytic complexes. J. Biol. Chem. 285: 25554-25569.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25554-25569
    • Book, A.J.1    Gladman, N.P.2    Lee, S.S.3    Scalf, M.4    Smith, L.M.5    Vierstra, R.D.6
  • 7
    • 33644878524 scopus 로고    scopus 로고
    • The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for embryogenesis
    • Brukhin, V., Gheyselinck, J., Gagliardini, V., Genschik, P., and Grossniklaus, U. (2005). The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for embryogenesis. Plant Cell 17: 2723-2737.
    • (2005) Plant Cell , vol.17 , pp. 2723-2737
    • Brukhin, V.1    Gheyselinck, J.2    Gagliardini, V.3    Genschik, P.4    Grossniklaus, U.5
  • 8
    • 57749114640 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination in the chromatin of FLOWERING LOCUS C regulates flowering time in Arabidopsis
    • Cao, Y., Dai, Y., Cui, S., and Ma, L. (2008). Histone H2B monoubiquitination in the chromatin of FLOWERING LOCUS C regulates flowering time in Arabidopsis. Plant Cell 20: 2586-2602.
    • (2008) Plant Cell , vol.20 , pp. 2586-2602
    • Cao, Y.1    Dai, Y.2    Cui, S.3    Ma, L.4
  • 9
    • 38949197834 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 regulates the cell cycle but not cell fate during male gametogenesis in Arabidopsis thaliana
    • Chen, Z., Tan, J.L., Ingouff, M., Sundaresan, V., and Berger, F. (2008). Chromatin assembly factor 1 regulates the cell cycle but not cell fate during male gametogenesis in Arabidopsis thaliana. Development 135: 65-73.
    • (2008) Development , vol.135 , pp. 65-73
    • Chen, Z.1    Tan, J.L.2    Ingouff, M.3    Sundaresan, V.4    Berger, F.5
  • 10
    • 7944224836 scopus 로고    scopus 로고
    • Proteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variant
    • Collins, K.A., Furuyama, S., and Biggins, S. (2004). Proteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variant. Curr. Biol. 14: 1968-1972.
    • (2004) Curr. Biol. , vol.14 , pp. 1968-1972
    • Collins, K.A.1    Furuyama, S.2    Biggins, S.3
  • 11
    • 58149522909 scopus 로고    scopus 로고
    • Making copies of chromatin: The challenge of nucleosomal organization and epigenetic information
    • Corpet, A., and Almouzni, G. (2009). Making copies of chromatin: The challenge of nucleosomal organization and epigenetic information. Trends Cell Biol. 19: 29-41.
    • (2009) Trends Cell Biol , vol.19 , pp. 29-41
    • Corpet, A.1    Almouzni, G.2
  • 12
    • 0142245636 scopus 로고    scopus 로고
    • A Gateway cloning vector set for high-throughput functional analysis of genes in planta
    • Curtis, M.D., and Grossniklaus, U. (2003). A Gateway cloning vector set for high-throughput functional analysis of genes in planta. Plant Physiol. 133: 462-469.
    • (2003) Plant Physiol , vol.133 , pp. 462-469
    • Curtis, M.D.1    Grossniklaus, U.2
  • 13
    • 34249820562 scopus 로고    scopus 로고
    • Repression of flowering in Arabidopsis requires activation of FLOWERING LOCUS C expression by the histone variant H2A.Z
    • Deal, R.B., Topp, C.N., McKinney, E.C., and Meagher, R.B. (2007). Repression of flowering in Arabidopsis requires activation of FLOWERING LOCUS C expression by the histone variant H2A.Z. Plant Cell 19: 74-83.
    • (2007) Plant Cell , vol.19 , pp. 74-83
    • Deal, R.B.1    Topp, C.N.2    McKinney, E.C.3    Meagher, R.B.4
  • 15
  • 16
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser, S., Chandler-Militello, D., Müller, B., Hanna, J., and Finley, D. (2004). Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279: 26817-26822.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Müller, B.3    Hanna, J.4    Finley, D.5
  • 18
    • 0038396218 scopus 로고    scopus 로고
    • The age of the Arabidopsis thaliana genome duplication
    • Ermolaeva, M.D., Wu, M., Eisen, J.A., and Salzberg, S.L. (2003). The age of the Arabidopsis thaliana genome duplication. Plant Mol. Biol. 51: 859-866.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 859-866
    • Ermolaeva, M.D.1    Wu, M.2    Eisen, J.A.3    Salzberg, S.L.4
  • 19
    • 44949192769 scopus 로고    scopus 로고
    • Control of trichome branching by chromatin assembly factor-1
    • Exner, V., Gruissem, W., and Hennig, L. (2008). Control of trichome branching by chromatin assembly factor-1. BMC Plant Biol. 8: 54-65.
    • (2008) BMC Plant Biol , vol.8 , pp. 54-65
    • Exner, V.1    Gruissem, W.2    Hennig, L.3
  • 20
    • 33751507011 scopus 로고    scopus 로고
    • Chromatin assembly factor CAF-1 is required for cellular differentiation during plant development
    • Exner, V., Taranto, P., Schönrock, N., Gruissem, W., and Hennig, L. (2006). Chromatin assembly factor CAF-1 is required for cellular differentiation during plant development. Development 133: 4163-4172.
    • (2006) Development , vol.133 , pp. 4163-4172
    • Exner, V.1    Taranto, P.2    Schönrock, N.3    Gruissem, W.4    Hennig, L.5
  • 21
    • 77950363988 scopus 로고    scopus 로고
    • The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis
    • Farmer, L.M., Book, A.J., Lee, K.H., Lin, Y.L., Fu, H., and Vierstra, R.D. (2010). The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis. Plant Cell 22: 124-142.
    • (2010) Plant Cell , vol.22 , pp. 124-142
    • Farmer, L.M.1    Book, A.J.2    Lee, K.H.3    Lin, Y.L.4    Fu, H.5    Vierstra, R.D.6
  • 22
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. (2009). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78: 477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 23
    • 34250650034 scopus 로고    scopus 로고
    • The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell cycle regulation during early leaf and root growth
    • Fleury, D., et al. (2007). The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell cycle regulation during early leaf and root growth. Plant Cell 19: 417-432.
    • (2007) Plant Cell , vol.19 , pp. 417-432
    • Fleury, D.1
  • 24
    • 34548829882 scopus 로고    scopus 로고
    • Isolation of Arabidopsis nuclei and measurement of gene transcription rates using nuclear run-on assays
    • Folta, K.M., and Kaufman, L.S. (2006). Isolation of Arabidopsis nuclei and measurement of gene transcription rates using nuclear run-on assays. Nat. Protoc. 1: 3094-3100.
    • (2006) Nat. Protoc. , vol.1 , pp. 3094-3100
    • Folta, K.M.1    Kaufman, L.S.2
  • 25
    • 0033152697 scopus 로고    scopus 로고
    • Structural and functional analysis of the six regulatory particle triple-A ATPase subunits from the Arabidopsis 26S proteasome
    • Fu, H., Doelling, J.H., Rubin, D.M., and Vierstra, R.D. (1999). Structural and functional analysis of the six regulatory particle triple-A ATPase subunits from the Arabidopsis 26S proteasome. Plant J. 18: 529-539.
    • (1999) Plant J , vol.18 , pp. 529-539
    • Fu, H.1    Doelling, J.H.2    Rubin, D.M.3    Vierstra, R.D.4
  • 26
    • 77955276666 scopus 로고    scopus 로고
    • Proteasomal recognition of ubiquitylated substrates
    • Fu, H., Lin, Y.L., and Fatimababy, A.S. (2010). Proteasomal recognition of ubiquitylated substrates. Trends Plant Sci. 15: 375-386.
    • (2010) Trends Plant Sci , vol.15 , pp. 375-386
    • Fu, H.1    Lin, Y.L.2    Fatimababy, A.S.3
  • 27
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1
    • Fu, H., Sadis, S., Rubin, D.M., Glickman, M.H., van Nocker, S., Finley, D., and Vierstra, R.D. (1998). Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273: 1970-1981.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1981
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.H.4    van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 28
    • 78049264771 scopus 로고    scopus 로고
    • The 26S proteasome: Assembly and function of a destructive machine
    • Gallastegui, N., and Groll, M. (2010). The 26S proteasome: Assembly and function of a destructive machine. Trends Biochem. Sci. 35: 634-642.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 634-642
    • Gallastegui, N.1    Groll, M.2
  • 29
    • 64749106137 scopus 로고    scopus 로고
    • The Arabidopsis proteasome RPT5 subunits are essential for gametophyte development and show accession-dependent redundancy
    • Gallois, J.L., Guyon-Debast, A., Lécureuil, A., Vezon, D., Carpentier, V., Bonhomme, S., and Guerche, P. (2009). The Arabidopsis proteasome RPT5 subunits are essential for gametophyte development and show accession-dependent redundancy. Plant Cell 21: 442-459.
    • (2009) Plant Cell , vol.21 , pp. 442-459
    • Gallois, J.L.1    Guyon-Debast, A.2    Lécureuil, A.3    Vezon, D.4    Carpentier, V.5    Bonhomme, S.6    Guerche, P.7
  • 30
  • 31
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M.H., Rubin, D.M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V.A., and Finley, D. (1998). A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94: 615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 32
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez, F., Delahodde, A., Kodadek, T., and Johnston, S.A. (2002). Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296: 548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 34
    • 0142091385 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo
    • Höek, M., and Stillman, B. (2003). Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo. Proc. Natl. Acad. Sci. USA 100: 12183-12188.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 12183-12188
    • Höek, M.1    Stillman, B.2
  • 35
    • 33750992171 scopus 로고    scopus 로고
    • The proteolytic function of the Arabidopsis 26S proteasome is required for specifying leaf adaxial identity
    • Huang, W., Pi, L., Liang, W., Xu, B., Wang, H., Cai, R., and Huang, H. (2006). The proteolytic function of the Arabidopsis 26S proteasome is required for specifying leaf adaxial identity. Plant Cell 18: 2479-2492.
    • (2006) Plant Cell , vol.18 , pp. 2479-2492
    • Huang, W.1    Pi, L.2    Liang, W.3    Xu, B.4    Wang, H.5    Cai, R.6    Huang, H.7
  • 37
    • 79951850741 scopus 로고    scopus 로고
    • Defining the geometry of the two-component proteasome degron
    • Inobe, T., Fishbain, S., Prakash, S., and Matouschek, A. (2011). Defining the geometry of the two-component proteasome degron. Nat. Chem. Biol. 7: 161-167.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 161-167
    • Inobe, T.1    Fishbain, S.2    Prakash, S.3    Matouschek, A.4
  • 38
    • 0035846902 scopus 로고    scopus 로고
    • FASCIATA genes for chromatin assembly factor-1 in Arabidopsis maintain the cellular organization of apical meristems
    • Kaya, H., Shibahara, K.I., Taoka, K.I., Iwabuchi, M., Stillman, B., and Araki, T. (2001). FASCIATA genes for chromatin assembly factor-1 in Arabidopsis maintain the cellular organization of apical meristems. Cell 104: 131-142.
    • (2001) Cell , vol.104 , pp. 131-142
    • Kaya, H.1    Shibahara, K.I.2    Taoka, K.I.3    Iwabuchi, M.4    Stillman, B.5    Araki, T.6
  • 39
    • 33751001765 scopus 로고    scopus 로고
    • The chromatin assembly factor subunit FASCIATA1 is involved in homologous recombination in plants
    • Kirik, A., Pecinka, A., Wendeler, E., and Reiss, B. (2006). The chromatin assembly factor subunit FASCIATA1 is involved in homologous recombination in plants. Plant Cell 18: 2431-2442.
    • (2006) Plant Cell , vol.18 , pp. 2431-2442
    • Kirik, A.1    Pecinka, A.2    Wendeler, E.3    Reiss, B.4
  • 40
    • 77449127817 scopus 로고    scopus 로고
    • No splicing, no dicing: Non-proteolytic roles of the ubiquitin-proteasome system in transcription
    • Kodadek, T. (2010). No splicing, no dicing: Non-proteolytic roles of the ubiquitin-proteasome system in transcription. J. Biol. Chem. 285: 2221-2226.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2221-2226
    • Kodadek, T.1
  • 41
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Köhler, A., Cascio, P., Leggett, D.S., Woo, K.M., Goldberg, A.L., and Finley, D. (2001). The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7: 1143-1152.
    • (2001) Mol. Cell. , vol.7 , pp. 1143-1152
    • Köhler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 42
    • 37249080675 scopus 로고    scopus 로고
    • 26S proteasome regulatory particle mutants have increased oxidative stress tolerance
    • Kurepa, J., Toh-E, A., and Smalle, J.A. (2008). 26S proteasome regulatory particle mutants have increased oxidative stress tolerance. Plant J. 53: 102-114.
    • (2008) Plant J , vol.53 , pp. 102-114
    • Kurepa, J.1    Toh-E, A.2    Smalle, J.A.3
  • 43
    • 66149141767 scopus 로고    scopus 로고
    • Loss of 26S proteasome function leads to increased cell size and decreased cell number in Arabidopsis shoot organs
    • Kurepa, J., Wang, S., Li, Y., Zaitlin, D., Pierce, A.J., and Smalle, J.A. (2009). Loss of 26S proteasome function leads to increased cell size and decreased cell number in Arabidopsis shoot organs. Plant Physiol. 150: 178-189.
    • (2009) Plant Physiol , vol.150 , pp. 178-189
    • Kurepa, J.1    Wang, S.2    Li, Y.3    Zaitlin, D.4    Pierce, A.J.5    Smalle, J.A.6
  • 44
    • 0026461099 scopus 로고
    • Characterization of three shoot apical meristem mutants of Arabidopsis thaliana
    • Leyser, H.M., and Furner, I.J. (1992). Characterization of three shoot apical meristem mutants of Arabidopsis thaliana. Development 116: 397-403.
    • (1992) Development , vol.116 , pp. 397-403
    • Leyser, H.M.1    Furner, I.J.2
  • 45
    • 0037013215 scopus 로고    scopus 로고
    • An easily dissociated 26S proteasome catalyzes an essential ubiquitin-mediated protein degradation pathway in Trypanosoma brucei
    • Li, Z., Zou, C.B., Yao, Y., Hoyt, M.A., McDonough, S., Mackey, Z.B., Coffino, P., and Wang, C.C. (2002). An easily dissociated 26S proteasome catalyzes an essential ubiquitin-mediated protein degradation pathway in Trypanosoma brucei. J. Biol. Chem. 277: 15486-15498.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15486-15498
    • Li, Z.1    Zou, C.B.2    Yao, Y.3    Hoyt, M.A.4    McDonough, S.5    Mackey, Z.B.6    Coffino, P.7    Wang, C.C.8
  • 46
    • 34250620427 scopus 로고    scopus 로고
    • The absence of histone H2B monoubiquitination in the Arabidopsis hub1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy
    • Liu, Y., Koornneef, M., and Soppe, W.J. (2007). The absence of histone H2B monoubiquitination in the Arabidopsis hub1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy. Plant Cell 19: 433-444.
    • (2007) Plant Cell , vol.19 , pp. 433-444
    • Liu, Y.1    Koornneef, M.2    Soppe, W.J.3
  • 47
    • 78951476162 scopus 로고    scopus 로고
    • Overlapping regulation of CenH3 localization and histone H3 turnover by CAF-1 and HIR proteins in Saccharomyces cerevisiae
    • Lopes da Rosa, J., Holik, J., Green, E.M., Rando, O.J., and Kaufman, P.D. (2011). Overlapping regulation of CenH3 localization and histone H3 turnover by CAF-1 and HIR proteins in Saccharomyces cerevisiae. Genetics 187: 9-19.
    • (2011) Genetics , vol.187 , pp. 9-19
    • Lopes da Rosa, J.1    Holik, J.2    Green, E.M.3    Rando, O.J.4    Kaufman, P.D.5
  • 48
    • 77957802887 scopus 로고    scopus 로고
    • Dysfunction of chromatin assembly factor 1 induces shortening of telomeres and loss of 45S rDNA in Arabidopsis thaliana
    • Mozgová, I., Mokroš, P., and Fajkus, J. (2010). Dysfunction of chromatin assembly factor 1 induces shortening of telomeres and loss of 45S rDNA in Arabidopsis thaliana. Plant Cell 22: 2768-2780.
    • (2010) Plant Cell , vol.22 , pp. 2768-2780
    • Mozgová, I.1    Mokroš, P.2    Fajkus, J.3
  • 50
    • 80054702676 scopus 로고    scopus 로고
    • Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response
    • Park, S., Kim, W., Tian, G., Gygi, S.P., and Finley, D. (2011). Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J. Biol. Chem. 286: 36652-36666.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36652-36666
    • Park, S.1    Kim, W.2    Tian, G.3    Gygi, S.P.4    Finley, D.5
  • 51
    • 67149121057 scopus 로고    scopus 로고
    • Hexameric assembly of the proteasomal ATPases is templated through their C termini
    • Park, S., Roelofs, J., Kim, W., Robert, J., Schmidt, M., Gygi, S.P., and Finley, D. (2009). Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459: 866-870.
    • (2009) Nature , vol.459 , pp. 866-870
    • Park, S.1    Roelofs, J.2    Kim, W.3    Robert, J.4    Schmidt, M.5    Gygi, S.P.6    Finley, D.7
  • 52
    • 42949096020 scopus 로고    scopus 로고
    • Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases
    • Rabl, J., Smith, D.M., Yu, Y., Chang, S.C., Goldberg, A.L., and Cheng, Y. (2008). Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases. Mol. Cell 30: 360-368.
    • (2008) Mol. Cell. , vol.30 , pp. 360-368
    • Rabl, J.1    Smith, D.M.2    Yu, Y.3    Chang, S.C.4    Goldberg, A.L.5    Cheng, Y.6
  • 53
    • 36549012155 scopus 로고    scopus 로고
    • The many faces of chromatin assembly factor 1
    • Ramirez-Parra, E., and Gutierrez, C. (2007). The many faces of chromatin assembly factor 1. Trends Plant Sci. 12: 570-576.
    • (2007) Trends Plant Sci , vol.12 , pp. 570-576
    • Ramirez-Parra, E.1    Gutierrez, C.2
  • 54
    • 11144246930 scopus 로고    scopus 로고
    • Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of Arabidopsis CDC48
    • Rancour, D.M., Park, S., Knight, S.D., and Bednarek, S.Y. (2004). Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of Arabidopsis CDC48. J. Biol. Chem. 279: 54264-54274.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54264-54274
    • Rancour, D.M.1    Park, S.2    Knight, S.D.3    Bednarek, S.Y.4
  • 56
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S., and Finley, D. (1998). Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17: 4909-4919.
    • (1998) EMBO J , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 57
    • 79953789985 scopus 로고    scopus 로고
    • Arabidopsis thaliana 26S proteasome subunits RPT2a and RPT5a are crucial for zinc deficiency-tolerance
    • Sakamoto, T., Kamiya, T., Sako, K., Yamaguchi, J., Yamagami, M., and Fujiwara, T. (2011). Arabidopsis thaliana 26S proteasome subunits RPT2a and RPT5a are crucial for zinc deficiency-tolerance. Biosci. Biotechnol. Biochem. 75: 561-567.
    • (2011) Biosci. Biotechnol. Biochem. , vol.75 , pp. 561-567
    • Sakamoto, T.1    Kamiya, T.2    Sako, K.3    Yamaguchi, J.4    Yamagami, M.5    Fujiwara, T.6
  • 58
    • 77955844908 scopus 로고    scopus 로고
    • Control of endoreduplication of trichomes by RPT2, a subunit of the 19S proteasome regulatory particle in Arabidopsis
    • Sako, K., Maki, Y., Imai, K.K., Aoyama, T., Goto, D.B., and Yamaguchi, J. (2010). Control of endoreduplication of trichomes by RPT2, a subunit of the 19S proteasome regulatory particle in Arabidopsis. J. Plant Res. 123: 701-706.
    • (2010) J. Plant Res. , vol.123 , pp. 701-706
    • Sako, K.1    Maki, Y.2    Imai, K.K.3    Aoyama, T.4    Goto, D.B.5    Yamaguchi, J.6
  • 59
    • 67649696034 scopus 로고    scopus 로고
    • Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis
    • Saracco, S.A., Hansson, M., Scalf, M., Walker, J.M., Smith, L.M., and Vierstra, R.D. (2009). Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 59: 344-358.
    • (2009) Plant J , vol.59 , pp. 344-358
    • Saracco, S.A.1    Hansson, M.2    Scalf, M.3    Walker, J.M.4    Smith, L.M.5    Vierstra, R.D.6
  • 61
    • 0036124032 scopus 로고    scopus 로고
    • Identification of the 19S regulatory particle subunits from the rice 26S proteasome
    • Shibahara, T., Kawasaki, H., and Hirano, H. (2002). Identification of the 19S regulatory particle subunits from the rice 26S proteasome. Eur. J. Biochem. 269: 1474-1483.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1474-1483
    • Shibahara, T.1    Kawasaki, H.2    Hirano, H.3
  • 62
    • 0346218256 scopus 로고    scopus 로고
    • Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome
    • Shibahara, T., Kawasaki, H., and Hirano, H. (2004). Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome. Arch. Biochem. Biophys. 421: 34-41.
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 34-41
    • Shibahara, T.1    Kawasaki, H.2    Hirano, H.3
  • 63
    • 68249094946 scopus 로고    scopus 로고
    • Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis
    • Singh, R.K., Kabbaj, M.H., Paik, J., and Gunjan, A. (2009). Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat. Cell Biol. 11: 925-933.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 925-933
    • Singh, R.K.1    Kabbaj, M.H.2    Paik, J.3    Gunjan, A.4
  • 65
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling
    • Smalle, J.A., Kurepa, J., Yang, P., Emborg, T.J., Babiychuk, E., Kushnir, S., and Vierstra, R.D. (2003). The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling. Plant Cell 15: 965-980.
    • (2003) Plant Cell , vol.15 , pp. 965-980
    • Smalle, J.A.1    Kurepa, J.2    Yang, P.3    Emborg, T.J.4    Babiychuk, E.5    Kushnir, S.6    Vierstra, R.D.7
  • 66
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle, J.A., and Vierstra, R.D. (2004). The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55: 555-590.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.A.1    Vierstra, R.D.2
  • 67
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the carboxyl-termini of the proteasomal ATPases in the a-ring of the 20S proteasome opens the gate for substrate entry
    • Smith, D.M., Chang, S.C., Park, S., Finley, D., Cheng, Y., and Goldberg, A.L. (2007). Docking of the carboxyl-termini of the proteasomal ATPases in the a-ring of the 20S proteasome opens the gate for substrate entry. Mol. Cell 27: 731-744.
    • (2007) Mol. Cell. , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 68
    • 79951707743 scopus 로고    scopus 로고
    • ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle
    • Smith, D.M., Fraga, H., Reis, C., Kafri, G., and Goldberg, A.L. (2011). ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144: 526-538.
    • (2011) Cell , vol.144 , pp. 526-538
    • Smith, D.M.1    Fraga, H.2    Reis, C.3    Kafri, G.4    Goldberg, A.L.5
  • 69
    • 35348960506 scopus 로고    scopus 로고
    • CAF-1 is essential for Drosophila development and involved in the maintenance of epigenetic memory
    • Song, Y., He, F., Xie, G., Guo, X., Xu, Y., Chen, Y., Liang, X., Stagljar, I., Egli, D., Ma, J., and Jiao, R. (2007). CAF-1 is essential for Drosophila development and involved in the maintenance of epigenetic memory. Dev. Biol. 311: 213-222.
    • (2007) Dev. Biol. , vol.311 , pp. 213-222
    • Song, Y.1    He, F.2    Xie, G.3    Guo, X.4    Xu, Y.5    Chen, Y.6    Liang, X.7    Stagljar, I.8    Egli, D.9    Ma, J.10    Jiao, R.11
  • 70
    • 70349515988 scopus 로고    scopus 로고
    • Regulation of leaf organ size by the Arabidopsis RPT2a 19S proteasome subunit
    • Sonoda, Y., Sako, K., Maki, Y., Yamazaki, N., Yamamoto, H., Ikeda, A., and Yamaguchi, J. (2009). Regulation of leaf organ size by the Arabidopsis RPT2a 19S proteasome subunit. Plant J. 60: 68-78.
    • (2009) Plant J , vol.60 , pp. 68-78
    • Sonoda, Y.1    Sako, K.2    Maki, Y.3    Yamazaki, N.4    Yamamoto, H.5    Ikeda, A.6    Yamaguchi, J.7
  • 71
    • 70450188170 scopus 로고    scopus 로고
    • Protein lipid modifications in signaling and subcellular targeting
    • Sorek, N., Bloch, D., and Yalovsky, S. (2009). Protein lipid modifications in signaling and subcellular targeting. Curr. Opin. Plant Biol. 12: 714-720.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 714-720
    • Sorek, N.1    Bloch, D.2    Yalovsky, S.3
  • 72
    • 34250025664 scopus 로고    scopus 로고
    • Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination
    • Sridhar, V.V., Kapoor, A., Zhang, K., Zhu, J., Zhou, T., Hasegawa, P.M., Bressan, R.A., and Zhu, J.K. (2007). Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination. Nature 447: 735-738.
    • (2007) Nature , vol.447 , pp. 735-738
    • Sridhar, V.V.1    Kapoor, A.2    Zhang, K.3    Zhu, J.4    Zhou, T.5    Hasegawa, P.M.6    Bressan, R.A.7    Zhu, J.K.8
  • 73
    • 33846128464 scopus 로고    scopus 로고
    • Essential role of chromatin assembly factor-1-mediated rapid nucleosome assembly for DNA replication and cell division in vertebrate cells
    • Takami, Y., Ono, T., Fukagawa, T., Shibahara, K.I., and Nakayama, T. (2007). Essential role of chromatin assembly factor-1-mediated rapid nucleosome assembly for DNA replication and cell division in vertebrate cells. Mol. Biol. Cell 18: 129-141.
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 129-141
    • Takami, Y.1    Ono, T.2    Fukagawa, T.3    Shibahara, K.I.4    Nakayama, T.5
  • 74
    • 72049110968 scopus 로고    scopus 로고
    • ARABIDOPSIS TRITHORAX-RELATED7 is required for methylation of lysine 4 of histone H3 and for transcriptional activation of FLOWERING LOCUS C
    • Tamada, Y., Yun, J.Y., Woo, S.C., and Amasino, R.M. (2009). ARABIDOPSIS TRITHORAX-RELATED7 is required for methylation of lysine 4 of histone H3 and for transcriptional activation of FLOWERING LOCUS C. Plant Cell 21: 3257-3269.
    • (2009) Plant Cell , vol.21 , pp. 3257-3269
    • Tamada, Y.1    Yun, J.Y.2    Woo, S.C.3    Amasino, R.M.4
  • 76
    • 77951945222 scopus 로고    scopus 로고
    • Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: Implications for proteasome structure and assembly
    • Tomko, R.J., Funakoshi, M., Schneider, K., Wang, J., and Hochstrasser, M. (2010). Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: Implications for proteasome structure and assembly. Mol. Cell 38: 393-403.
    • (2010) Mol. Cell. , vol.38 , pp. 393-403
    • Tomko, R.J.1    Funakoshi, M.2    Schneider, K.3    Wang, J.4    Hochstrasser, M.5
  • 77
    • 80052900728 scopus 로고    scopus 로고
    • Arabidopsis RPT2a encoding the 26S proteasome subunit is required for various aspects of root meristem maintenance, and regulates gametogenesis redundantly with its homolog, RPT2b
    • Ueda, M., Matsui, K., Ishiguro, S., Kato, T., Tabata, S., Kobayashi, M., Seki, M., Shinozaki, K., and Okada, K. (2011). Arabidopsis RPT2a encoding the 26S proteasome subunit is required for various aspects of root meristem maintenance, and regulates gametogenesis redundantly with its homolog, RPT2b. Plant Cell Physiol. 52: 1628-1640.
    • (2011) Plant Cell Physiol , vol.52 , pp. 1628-1640
    • Ueda, M.1    Matsui, K.2    Ishiguro, S.3    Kato, T.4    Tabata, S.5    Kobayashi, M.6    Seki, M.7    Shinozaki, K.8    Okada, K.9
  • 78
    • 2542602913 scopus 로고    scopus 로고
    • The HALTED ROOT gene encoding the 26S proteasome subunit RPT2a is essential for the maintenance of Arabidopsis meristems
    • Ueda, M., Matsui, K., Ishiguro, S., Sano, R., Wada, T., Paponov, I., Palme, K., and Okada, K. (2004). The HALTED ROOT gene encoding the 26S proteasome subunit RPT2a is essential for the maintenance of Arabidopsis meristems. Development 131: 2101-2111.
    • (2004) Development , vol.131 , pp. 2101-2111
    • Ueda, M.1    Matsui, K.2    Ishiguro, S.3    Sano, R.4    Wada, T.5    Paponov, I.6    Palme, K.7    Okada, K.8
  • 79
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • van Nocker, S., Deveraux, Q., Rechsteiner, M., and Vierstra, R.D. (1996). Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. USA 93: 856-860.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 856-860
    • van Nocker, S.1    Deveraux, Q.2    Rechsteiner, M.3    Vierstra, R.D.4
  • 80
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., Aravind, L., Oania, R., McDonald, W.H., Yates III, J.R., Koonin, E.V., and Deshaies, R.J. (2002). Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298: 611-615.
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 81
    • 67349254570 scopus 로고    scopus 로고
    • The ubiquitin-26S proteasome system at the nexus of plant biology
    • Vierstra, R.D. (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
  • 82
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P., and Baumeister, W. (1999). The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68: 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 83
    • 34147172470 scopus 로고    scopus 로고
    • A ubiquitin-based vector for the co-ordinated synthesis of multiple proteins in plants
    • Walker, J.M., and Vierstra, R.D. (2007). A ubiquitin-based vector for the co-ordinated synthesis of multiple proteins in plants. Plant Biotechnol. J. 5: 413-421.
    • (2007) Plant Biotechnol. J. , vol.5 , pp. 413-421
    • Walker, J.M.1    Vierstra, R.D.2
  • 84
    • 70349918653 scopus 로고    scopus 로고
    • The Arabidopsis 26S proteasome subunit RPN1a is required for optimal plant growth and stress responses
    • Wang, S., Kurepa, J., and Smalle, J.A. (2009). The Arabidopsis 26S proteasome subunit RPN1a is required for optimal plant growth and stress responses. Plant Cell Physiol. 50: 1721-1725.
    • (2009) Plant Cell Physiol , vol.50 , pp. 1721-1725
    • Wang, S.1    Kurepa, J.2    Smalle, J.A.3
  • 85
    • 1342346597 scopus 로고    scopus 로고
    • Purification of the Arabidopsis 26S proteasome: Biochemical and molecular analyses revealed the presence of multiple isoforms
    • Yang, P., Fu, H., Walker, J.M., Papa, C.M., Smalle, J.A., Ju, Y.M., and Vierstra, R.D. (2004). Purification of the Arabidopsis 26S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 279: 6401-6413.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6401-6413
    • Yang, P.1    Fu, H.2    Walker, J.M.3    Papa, C.M.4    Smalle, J.A.5    Ju, Y.M.6    Vierstra, R.D.7
  • 87
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmermann, P., Hirsch-Hoffmann, M., Hennig, L., and Gruissem, W. (2004). GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136: 2621-2632.
    • (2004) Plant Physiol , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.