메뉴 건너뛰기




Volumn 139, Issue 4, 2005, Pages 1597-1611

Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; GENES; PROTEINS;

EID: 33644993733     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.105.067983     Document Type: Article
Times cited : (330)

References (61)
  • 1
    • 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
  • 2
    • 0030800865 scopus 로고    scopus 로고
    • Yeast DNA repair protein Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities
    • Bailly V, Lauder S, Prakash S, Prakash L (1997) Yeast DNA repair protein Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J Biol Chem 272: 23360-23365
    • (1997) J Biol Chem , vol.272 , pp. 23360-23365
    • Bailly, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 3
    • 0027675474 scopus 로고
    • Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana
    • Bartling D, Rehling P, Weiler EW (1993) Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana. Plant Mol Biol 23: 387-396
    • (1993) Plant Mol Biol , vol.23 , pp. 387-396
    • Bartling, D.1    Rehling, P.2    Weiler, E.W.3
  • 4
    • 0033212969 scopus 로고    scopus 로고
    • UPL1 and 2, two 405 kDa ubiquitin-protein ligases from Arabidopsis thaliana related to the HECT-domain protein family
    • Bates PW, Vierstra RD (1999) UPL1 and 2, two 405 kDa ubiquitin-protein ligases from Arabidopsis thaliana related to the HECT-domain protein family. Plant J 20: 183-195
    • (1999) Plant J , vol.20 , pp. 183-195
    • Bates, P.W.1    Vierstra, R.D.2
  • 5
    • 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
  • 6
    • 0036851183 scopus 로고    scopus 로고
    • Molecular characterization of plant ubiquitin-conjugating enzymes belonging to the UbcP4/E2-C/UBCx/UbcH10 gene family
    • Criqui MC, de Almeida Engler J, Camasses A, Capron A, Parmentier Y, Inze D, Genschik P (2002) Molecular characterization of plant ubiquitin-conjugating enzymes belonging to the UbcP4/E2-C/UBCx/UbcH10 gene family. Plant Physiol 130: 1230-1240
    • (2002) Plant Physiol , vol.130 , pp. 1230-1240
    • Criqui, M.C.1    De Almeida Engler, J.2    Camasses, A.3    Capron, A.4    Parmentier, Y.5    Inze, D.6    Genschik, P.7
  • 7
    • 0033592946 scopus 로고    scopus 로고
    • The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1
    • Del Pozo C, Estelle M (1999) The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1. Proc Natl Acad Sci USA 96: 15342-15347
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 15342-15347
    • Del Pozo, C.1    Estelle, M.2
  • 8
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the I kappa B kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, Yang LY, Braun A, You JX, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the I kappa B kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103: 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.Y.4    Braun, A.5    You, J.X.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 9
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM (2000) Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 275: 8945-8951
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 10
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • Fang S, Weissman AM (2004) A field guide to ubiquitylation. Cell Mol life Sci 61: 1546-1561
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 11
    • 0027239790 scopus 로고
    • The RING finger: A novel protein sequence motif related to the zinc finger
    • Freemont PS (1993) The RING finger: a novel protein sequence motif related to the zinc finger. Ann N Y Acad Sci 684: 174-192
    • (1993) Ann N Y Acad Sci , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 12
    • 0025977953 scopus 로고
    • A novel cysteine-rich sequence motif
    • Freemont PS, Hanson IM, Trowsdale J (1991) A novel cysteine-rich sequence motif. Cell 64: 483-484
    • (1991) Cell , vol.64 , pp. 483-484
    • Freemont, P.S.1    Hanson, I.M.2    Trowsdale, J.3
  • 13
    • 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
  • 14
    • 0027582362 scopus 로고
    • Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana
    • Girod PA, Carpenter TB, van Nocker S, Sullivan ML, Vierstra RD (1993) Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana. Plant J 3: 545-552
    • (1993) Plant J , vol.3 , pp. 545-552
    • Girod, P.A.1    Carpenter, T.B.2    Van Nocker, S.3    Sullivan, M.L.4    Vierstra, R.D.5
  • 15
    • 0027388957 scopus 로고
    • A major ubiquitin conjugation system in wheat germ extracts involves a 15-kDa ubiquitin-conjugating enzyme (E2) homologous to the yeast UBC4/UBC5 gene products
    • Girad PA, Vierstra RD (1993) A major ubiquitin conjugation system in wheat germ extracts involves a 15-kDa ubiquitin-conjugating enzyme (E2) homologous to the yeast UBC4/UBC5 gene products. J Biol Chem 268: 955-960
    • (1993) J Biol Chem , vol.268 , pp. 955-960
    • Girad, P.A.1    Vierstra, R.D.2
  • 16
    • 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
  • 18
    • 0036015059 scopus 로고    scopus 로고
    • Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8)
    • Hardtke CS, Okamoto H, Stoop-Myer C, Deng XW (2002) Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8). Plant J 30: 385-394
    • (2002) Plant J , vol.30 , pp. 385-394
    • Hardtke, C.S.1    Okamoto, H.2    Stoop-Myer, C.3    Deng, X.W.4
  • 20
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419: 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 21
    • 0032475896 scopus 로고    scopus 로고
    • Widespread occurrence of a highly conserved RING-H2 zinc finger motif in the model plant Arabidopsis thaliana
    • Jensen RB, Jensen KL, Jespersen HM, Skriver K (1998) Widespread occurrence of a highly conserved RING-H2 zinc finger motif in the model plant Arabidopsis thaliana. FEBS Lett 436: 283-287
    • (1998) FEBS Lett , vol.436 , pp. 283-287
    • Jensen, R.B.1    Jensen, K.L.2    Jespersen, H.M.3    Skriver, K.4
  • 22
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch S, McGrath JP, Varshavsky A (1987) The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329: 131-134
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 23
    • 3442900482 scopus 로고    scopus 로고
    • Human disorders of ubiquitination and proteasomal degradation
    • Jiang YH, Beaudet AL (2004) Human disorders of ubiquitination and proteasomal degradation. Curr Opin Pediatr 16: 419-426
    • (2004) Curr Opin Pediatr , vol.16 , pp. 419-426
    • Jiang, Y.H.1    Beaudet, A.L.2
  • 26
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress
    • Kurepa J, Walker JM, Smalle J, Gosink MM, Davis SJ, Durham TL, Sung DY, Vierstra RD (2003) The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J Biol Chem 278: 6862-6872
    • (2003) J Biol Chem , vol.278 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.Y.7    Vierstra, R.D.8
  • 29
    • 0032941754 scopus 로고    scopus 로고
    • Yeast mutants affecting possible quality control of plasma membrane proteins
    • Li Y, Kane T, Tipper C, Spatrick P, Jenness DD (1999) Yeast mutants affecting possible quality control of plasma membrane proteins. Mol Cell Biol 19: 3588-3599
    • (1999) Mol Cell Biol , vol.19 , pp. 3588-3599
    • Li, Y.1    Kane, T.2    Tipper, C.3    Spatrick, P.4    Jenness, D.D.5
  • 30
    • 0026692943 scopus 로고
    • cDNA cloning of a novel human ubiquitin carrier protein. An antigenic domain specifically recognized by endemic pemphigus foliaceus autoantibodies is encoded in a secondary reading frame of this human epidermal transcript
    • Liu Z, Diaz LA, Haas AL, Giudice GJ (1992) cDNA cloning of a novel human ubiquitin carrier protein. An antigenic domain specifically recognized by endemic pemphigus foliaceus autoantibodies is encoded in a secondary reading frame of this human epidermal transcript. J Biol Chem 267: 15829-15835
    • (1992) J Biol Chem , vol.267 , pp. 15829-15835
    • Liu, Z.1    Diaz, L.A.2    Haas, A.L.3    Giudice, G.J.4
  • 32
    • 24344488725 scopus 로고    scopus 로고
    • Organ-specific expression of Arabidopsis genome during development
    • Ma L, Sun N, Liu X, Jiao Y, Zhao H, Deng XW (2005) Organ-specific expression of Arabidopsis genome during development. Plant Physiol 138: 80-91
    • (2005) Plant Physiol , vol.138 , pp. 80-91
    • Ma, L.1    Sun, N.2    Liu, X.3    Jiao, Y.4    Zhao, H.5    Deng, X.W.6
  • 33
    • 4644344039 scopus 로고    scopus 로고
    • The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation
    • Mathe E, Kraft C, Giet R, Deak P, Peters JM, Glover DM (2004) The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation. Curr Biol 14: 1723-1733
    • (2004) Curr Biol , vol.14 , pp. 1723-1733
    • Mathe, E.1    Kraft, C.2    Giet, R.3    Deak, P.4    Peters, J.M.5    Glover, D.M.6
  • 34
    • 0037252518 scopus 로고    scopus 로고
    • Identification and characterization of the ARIADNE gene family in Arabidopsis: A group of putative E3 ligases
    • Mladek C, Guger K, Hauser MT (2003) Identification and characterization of the ARIADNE gene family in Arabidopsis: a group of putative E3 ligases. Plant Physiol 131: 27-40
    • (2003) Plant Physiol , vol.131 , pp. 27-40
    • Mladek, C.1    Guger, K.2    Hauser, M.T.3
  • 35
    • 0842264053 scopus 로고    scopus 로고
    • A large complement of the predicted Arabidopsis ARM repeat proteins are members of the U-box E3 ubiquitin ligase family
    • Mudgil Y, Shiu SH, Stone SL, Salt JN, Goring DR (2004) A large complement of the predicted Arabidopsis ARM repeat proteins are members of the U-box E3 ubiquitin ligase family. Plant Physiol 134: 59-66
    • (2004) Plant Physiol , vol.134 , pp. 59-66
    • Mudgil, Y.1    Shiu, S.H.2    Stone, S.L.3    Salt, J.N.4    Goring, D.R.5
  • 37
    • 0030858902 scopus 로고    scopus 로고
    • CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter
    • Rothofsky ML, Lin SL (1997) CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter. Gene 195: 141-149
    • (1997) Gene , vol.195 , pp. 141-149
    • Rothofsky, M.L.1    Lin, S.L.2
  • 38
    • 0031962188 scopus 로고
    • Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells
    • Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, et al (1993) Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells. Mol Cell Biol 18: 576-589
    • (1993) Mol Cell Biol , vol.18 , pp. 576-589
    • Sancho, E.1    Vilá, M.R.2    Sánchez-Pulido, L.3    Lozano, J.J.4    Paciucci, R.5    Nadal, M.6    Fox, M.7    Harvey, C.8    Bercovich, B.9    Loukili, N.10
  • 40
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell JD, Hicke L (2003) Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J Biol Chem 278: 35857-35860
    • (2003) J Biol Chem , vol.278 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 41
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • Shi CS, Kehrl JH (2003) Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2). J Biol Chem 278: 15429-15434
    • (2003) J Biol Chem , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 45
    • 0027537635 scopus 로고
    • Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+
    • Sullivan ML, Vierstra RD (1993) Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+. J Biol Chem 268: 8777-8780
    • (1993) J Biol Chem , vol.268 , pp. 8777-8780
    • Sullivan, M.L.1    Vierstra, R.D.2
  • 46
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun L, Chen ZJ (2004) The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 16: 119-126
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 47
    • 0036500015 scopus 로고    scopus 로고
    • Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis
    • Suzuki G, Yanagawa Y, Kwok SF, Matsui M, Deng X-W (2002) Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis. Genes Dev 16: 554-559
    • (2002) Genes Dev , vol.16 , pp. 554-559
    • Suzuki, G.1    Yanagawa, Y.2    Kwok, S.F.3    Matsui, M.4    Deng, X.-W.5
  • 48
    • 0035661566 scopus 로고    scopus 로고
    • APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex
    • Tang Z, Li B, Bharadwaj R, Zhu H, Ozkan E, Hakala K, Deisenhufer J, Yu H (2001) APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol Biol Cell 12: 3839-3851
    • (2001) Mol Biol Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Li, B.2    Bharadwaj, R.3    Zhu, H.4    Ozkan, E.5    Hakala, K.6    Deisenhufer, J.7    Yu, H.8
  • 49
    • 0030175281 scopus 로고    scopus 로고
    • Members of two gene families encoding ubiquitin-conjugating enzymes, AtUBCl-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed
    • Thoma S, Sullivan ML, Vierstra RD (1996) Members of two gene families encoding ubiquitin-conjugating enzymes, AtUBCl-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed. Plant Mol Biol 31: 493-505
    • (1996) Plant Mol Biol , vol.31 , pp. 493-505
    • Thoma, S.1    Sullivan, M.L.2    Vierstra, R.D.3
  • 50
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 52
    • 1342268375 scopus 로고    scopus 로고
    • The roles of ubiquitin and lipids in protein sorting along the endocytic pathway
    • Umebayashi K (2003) The roles of ubiquitin and lipids in protein sorting along the endocytic pathway. Cell Struct Funct 28: 443-453
    • (2003) Cell Struct Funct , vol.28 , pp. 443-453
    • Umebayashi, K.1
  • 53
    • 0027428769 scopus 로고
    • Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway
    • Van Nocker S, Vierstra RD (1993) Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway. J Biol Chem 268: 24766-24773
    • (1993) J Biol Chem , vol.268 , pp. 24766-24773
    • Van Nocker, S.1    Vierstra, R.D.2
  • 54
    • 17544365083 scopus 로고    scopus 로고
    • The Arabidopsis thaliana UBC7/13/14 gene encode a family of multiubiquitin chain-forming E2 enzymes
    • Van Nocker S, Walker JM, Vierstra RD (1996) The Arabidopsis thaliana UBC7/13/14 gene encode a family of multiubiquitin chain-forming E2 enzymes. J Biol Chem 271: 12150-12158
    • (1996) J Biol Chem , vol.271 , pp. 12150-12158
    • Van Nocker, S.1    Walker, J.M.2    Vierstra, R.D.3
  • 55
    • 0042818412 scopus 로고    scopus 로고
    • The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p
    • Wood A, Schneider J, Dover J, Johnston M, Shilatifard A (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278: 34739-34742
    • (2003) J Biol Chem , vol.278 , pp. 34739-34742
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 57
    • 0037068470 scopus 로고    scopus 로고
    • SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin signals
    • Xie Q, Guo HS, Dallman G, Fang SY, Weissman AM, Chua NH (2002) SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin signals. Nature 419: 167-170
    • (2002) Nature , vol.419 , pp. 167-170
    • Xie, Q.1    Guo, H.S.2    Dallman, G.3    Fang, S.Y.4    Weissman, A.M.5    Chua, N.H.6
  • 59
    • 22344447315 scopus 로고    scopus 로고
    • The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation
    • Zhang X, Garreton V, Chua H-H (2005) The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation. Genes Dev 19: 1535-1543
    • (2005) Genes Dev , vol.19 , pp. 1535-1543
    • Zhang, X.1    Garreton, V.2    Chua, H.-H.3
  • 61
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmerman P, Hirsch-Hoffmann M, Hennig L, Gruissem W (2004) GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol 136: 2621-2632
    • (2004) Plant Physiol , vol.136 , pp. 2621-2632
    • Zimmerman, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.