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Volumn 160, Issue 1, 2012, Pages 2-14

The expanding universe of ubiquitin and ubiquitin-like modifiers

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EID: 84865855321     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.112.200667     Document Type: Review
Times cited : (165)

References (146)
  • 1
    • 69349103147 scopus 로고    scopus 로고
    • Function and regulation of macroautophagy in plants
    • Bassham DC (2009) Function and regulation of macroautophagy in plants. Biochim Biophys Acta 1793: 1397-1403.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1397-1403
    • Bassham, D.C.1
  • 3
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW (2010) Network organization of the human autophagy system. Nature 466: 68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 4
    • 77955485244 scopus 로고    scopus 로고
    • Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes
    • Book AJ, Gladman NP, Lee SS, Scalf M, Smith LM, Vierstra RD (2010) Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes. J Biol Chem 285: 25554-25569.
    • (2010) J Biol Chem , pp. 25554
    • Book, A.J.1    Gladman, N.P.2    Lee, S.S.3    Scalf, M.4    Smith, L.M.5    Vierstra, R.D.6
  • 5
    • 78549285675 scopus 로고    scopus 로고
    • Darwin KH (2010) "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates
    • Burns KE, Cerda-Maira FA, Wang T, Li H, Bishai WR, Darwin KH (2010) "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. Mol Cell 39: 821-827.
    • Mol Cell , vol.39 , pp. 821-827
    • Burns, K.E.1    Cerda-Maira, F.A.2    Wang, T.3    Li, H.4    Bishai, W.R.5
  • 6
    • 84859229690 scopus 로고    scopus 로고
    • The natural history of ubiquitin and ubiquitin-related domains
    • Burroughs AM, Iyer LM, Aravind L (2012) The natural history of ubiquitin and ubiquitin-related domains. Front Biosci 17: 1433-1460.
    • (2012) Front Biosci , vol.17 , pp. 1433-1460
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 7
    • 0028836104 scopus 로고
    • Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia
    • Callis J, Carpenter T, Sun CW, Vierstra RD (1995) Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia. Genetics 139: 921-939.
    • (1995) Genetics , vol.139 , pp. 921-939
    • Callis, J.1    Carpenter, T.2    Sun, C.W.3    Vierstra, R.D.4
  • 8
    • 0025370073 scopus 로고
    • Ubiquitin extension proteins of Arabidopsis thaliana: Structure, localization, and expression of their promoters in transgenic tobacco
    • Callis J, Raasch JA, Vierstra RD (1990) Ubiquitin extension proteins of Arabidopsis thaliana: structure, localization, and expression of their promoters in transgenic tobacco. J Biol Chem 265: 12486-12493.
    • (1990) J Biol Chem , vol.265 , pp. 12486-12493
    • Callis, J.1    Raasch, J.A.2    Vierstra, R.D.3
  • 9
    • 77950956398 scopus 로고    scopus 로고
    • ATG8 lipidation and ATG8-mediated autophagy in Arabidopsis require ATG12 expressed from the differentially controlled ATG12A and ATG12B loci
    • Chung T, Phillips AR, Vierstra RD (2010) ATG8 lipidation and ATG8-mediated autophagy in Arabidopsis require ATG12 expressed from the differentially controlled ATG12A and ATG12B loci. Plant J 62: 483-493.
    • (2010) Plant J , vol.62 , pp. 483-493
    • Chung, T.1    Phillips, A.R.2    Vierstra, R.D.3
  • 10
    • 58449118073 scopus 로고    scopus 로고
    • The ATG autophagic conjugation system in maize: ATG transcripts and abundance of the ATG8-lipid adduct are regulated by development and nutrient availability
    • Chung T, Suttangkakul A, Vierstra RD (2009) The ATG autophagic conjugation system in maize: ATG transcripts and abundance of the ATG8-lipid adduct are regulated by development and nutrient availability. Plant Physiol 149: 220-234.
    • (2009) Plant Physiol , vol.149 , pp. 220-234
    • Chung, T.1    Suttangkakul, A.2    Vierstra, R.D.3
  • 11
    • 33748758712 scopus 로고    scopus 로고
    • SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis
    • Colby T, Matthäi A, Boeckelmann A, Stuible HP (2006) SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis. Plant Physiol 142: 318-332.
    • (2006) Plant Physiol , vol.142 , pp. 318-332
    • Colby, T.1    Matthäi, A.2    Boeckelmann, A.3    Stuible, H.P.4
  • 12
    • 57749100154 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis
    • Conti L, Price G, O'Donnell E, Schwessinger B, Dominy P, Sadanandom A (2008) Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis. Plant Cell 20: 2894-2908.
    • (2008) Plant Cell , vol.20 , pp. 2894-2908
    • Conti, L.1    Price, G.2    O'Donnell, E.3    Schwessinger, B.4    Dominy, P.5    Sadanandom, A.6
  • 13
    • 61649110496 scopus 로고    scopus 로고
    • Protein isoprenylation: The fat of the matter
    • Crowell DN, Huizinga DH (2009) Protein isoprenylation: the fat of the matter. Trends Plant Sci 14: 163-170.
    • (2009) Trends Plant Sci , vol.14 , pp. 163-170
    • Crowell, D.N.1    Huizinga, D.H.2
  • 14
    • 14544269435 scopus 로고    scopus 로고
    • Genetic and chemical analyses of the action mechanisms of sirtinol in Arabidopsis
    • Dai X, Hayashi K, Nozaki H, Cheng Y, Zhao Y (2005) Genetic and chemical analyses of the action mechanisms of sirtinol in Arabidopsis. Proc Natl Acad Sci USA 102: 3129-3134.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3129-3134
    • Dai, X.1    Hayashi, K.2    Nozaki, H.3    Cheng, Y.4    Zhao, Y.5
  • 15
    • 0036009784 scopus 로고    scopus 로고
    • AXR1-ECR1-dependent conjugation of RUB1 to the Arabidopsis cullin AtCUL1 is required for auxin response
    • del Pozo JC, Dharmasiri S, Hellmann H, Walker L, Gray WM, Estelle M (2002) AXR1-ECR1-dependent conjugation of RUB1 to the Arabidopsis cullin AtCUL1 is required for auxin response. Plant Cell 14: 421-433.
    • (2002) Plant Cell , vol.14 , pp. 421-433
    • del Pozo, J.C.1    Dharmasiri, S.2    Hellmann, H.3    Walker, L.4    Gray, W.M.5    Estelle, M.6
  • 16
    • 0033592946 scopus 로고    scopus 로고
    • The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1
    • del Pozo JC, 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, J.C.1    Estelle, M.2
  • 17
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro JM, Rodriguez MS, Hay RT (1998) SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 2: 233-239.
    • (1998) Mol Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 18
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitinlike modification in polarized morphogenesis
    • Dittmar GA, Wilkinson CR, Jedrzejewski PT, Finley D (2002) Role of a ubiquitinlike modification in polarized morphogenesis. Science 295: 2442-2446.
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.1    Wilkinson, C.R.2    Jedrzejewski, P.T.3    Finley, D.4
  • 19
    • 0037031843 scopus 로고    scopus 로고
    • The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana
    • Doelling JH, Walker JM, Friedman EM, Thompson AR, Vierstra RD (2002) The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana. J Biol Chem 277: 33105-33114.
    • (2002) J Biol Chem , vol.277 , pp. 33105-33114
    • Doelling, J.H.1    Walker, J.M.2    Friedman, E.M.3    Thompson, A.R.4    Vierstra, R.D.5
  • 20
    • 0034795089 scopus 로고    scopus 로고
    • The ubiquitinspecific protease UBP14 is essential for early embryo development in Arabidopsis thaliana
    • Doelling JH, Yan N, Kurepa J, Walker J, Vierstra RD (2001) The ubiquitinspecific protease UBP14 is essential for early embryo development in Arabidopsis thaliana. Plant J 27: 393-405.
    • (2001) Plant J , vol.27 , pp. 393-405
    • Doelling, J.H.1    Yan, N.2    Kurepa, J.3    Walker, J.4    Vierstra, R.D.5
  • 21
    • 79955387574 scopus 로고    scopus 로고
    • Arabidopsis membrane-anchored ubiquitin-fold (MUB) proteins localize a specific subset of ubiquitin-conjugating (E2) enzymes to the plasma membrane
    • Dowil RT, Lu X, Saracco SA, Vierstra RD, Downes BP (2011) Arabidopsis membrane-anchored ubiquitin-fold (MUB) proteins localize a specific subset of ubiquitin-conjugating (E2) enzymes to the plasma membrane. J Biol Chem 286: 14913-14921.
    • (2011) J Biol Chem , vol.286 , pp. 14913-14921
    • Dowil, R.T.1    Lu, X.2    Saracco, S.A.3    Vierstra, R.D.4    Downes, B.P.5
  • 22
    • 18044364830 scopus 로고    scopus 로고
    • Post-translational regulation in plants employing a diverse set of polypeptide tags
    • Downes B, Vierstra RD (2005) Post-translational regulation in plants employing a diverse set of polypeptide tags. Biochem Soc Trans 33: 393-399.
    • (2005) Biochem Soc Trans , vol.33 , pp. 393-399
    • Downes, B.1    Vierstra, R.D.2
  • 23
    • 33748742143 scopus 로고    scopus 로고
    • MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation
    • Downes BP, Saracco SA, Lee SS, Crowell DN, Vierstra RD (2006) MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. J Biol Chem 281: 27145-27157.
    • (2006) J Biol Chem , vol.281 , pp. 27145-27157
    • Downes, B.P.1    Saracco, S.A.2    Lee, S.S.3    Crowell, D.N.4    Vierstra, R.D.5
  • 24
    • 0141567486 scopus 로고    scopus 로고
    • The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development
    • Downes BP, Stupar RM, Gingerich DJ, Vierstra RD (2003) The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development. Plant J 35: 729-742.
    • (2003) Plant J , vol.35 , pp. 729-742
    • Downes, B.P.1    Stupar, R.M.2    Gingerich, D.J.3    Vierstra, R.D.4
  • 25
    • 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
  • 26
    • 78049234670 scopus 로고    scopus 로고
    • Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes
    • Elrouby N, Coupland G (2010) Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes. Proc Natl Acad Sci USA 107: 17415-17420.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17415-17420
    • Elrouby, N.1    Coupland, G.2
  • 27
    • 77950363988 scopus 로고    scopus 로고
    • The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis
    • Farmer LM, Book AJ, Lee KH, Lin YL, Fu H, Vierstra RD (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
  • 28
    • 75149172775 scopus 로고    scopus 로고
    • Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis
    • Fatimababy AS, Lin YL, Usharani R, Radjacommare R, Wang HT, Tsai HL, Lee Y, Fu H (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277: 796-816.
    • (2010) FEBS J , vol.277 , pp. 796-816
    • Fatimababy, A.S.1    Lin, Y.L.2    Usharani, R.3    Radjacommare, R.4    Wang, H.T.5    Tsai, H.L.6    Lee, Y.7    Fu, H.8
  • 29
    • 3142732890 scopus 로고    scopus 로고
    • Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/ proteasome-mediated protein degradation
    • Feng S, Shen Y, Sullivan JA, Rubio V, Xiong Y, Sun TP, Deng XW (2004) Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/ proteasome-mediated protein degradation. Plant Cell 16: 1870-1882.
    • (2004) Plant Cell , vol.16 , pp. 1870-1882
    • Feng, S.1    Shen, Y.2    Sullivan, J.A.3    Rubio, V.4    Xiong, Y.5    Sun, T.P.6    Deng, X.W.7
  • 30
    • 23944491295 scopus 로고    scopus 로고
    • Arabidopsis has two redundant Cullin3 proteins that are essential for embryo development and that interact with RBX1 and BTB proteins to form multisubunit E3 ubiquitin ligase complexes in vivo
    • Figueroa P, Gusmaroli G, Serino G, Habashi J, Ma L, Shen Y, Feng S, Bostick M, Callis J, Hellmann H, et al (2005) Arabidopsis has two redundant Cullin3 proteins that are essential for embryo development and that interact with RBX1 and BTB proteins to form multisubunit E3 ubiquitin ligase complexes in vivo. Plant Cell 17: 1180-1195.
    • (2005) Plant Cell , vol.17 , pp. 1180-1195
    • Figueroa, P.1    Gusmaroli, G.2    Serino, G.3    Habashi, J.4    Ma, L.5    Shen, Y.6    Feng, S.7    Bostick, M.8    Callis, J.9    Hellmann, H.10
  • 31
    • 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
  • 32
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley D, Bartel B, Varshavsky A (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338: 394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 34
    • 77955276666 scopus 로고    scopus 로고
    • Proteasomal recognition of ubiquitylated substrates
    • Fu H, Lin YL, Fatimababy AS (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
  • 35
    • 38349152489 scopus 로고    scopus 로고
    • In vitro reconstitution of plant Atg8 and Atg12 conjugation systems essential for autophagy
    • Fujioka Y, Noda NN, Fujii K, Yoshimoto K, Ohsumi Y, Inagaki F (2008) In vitro reconstitution of plant Atg8 and Atg12 conjugation systems essential for autophagy. J Biol Chem 283: 1921-1928.
    • (2008) J Biol Chem , vol.283 , pp. 1921-1928
    • Fujioka, Y.1    Noda, N.N.2    Fujii, K.3    Yoshimoto, K.4    Ohsumi, Y.5    Inagaki, F.6
  • 36
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • Furukawa K, Mizushima N, Noda T, Ohsumi Y (2000) A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J Biol Chem 275: 7462-7465.
    • (2000) J Biol Chem , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 37
    • 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
  • 38
    • 84861869979 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes in transcription
    • Geng F, Wenzel S, Tansey WP (2012) Ubiquitin and proteasomes in transcription. Annu Rev Biochem 81: 177-201.
    • (2012) Annu Rev Biochem , vol.81 , pp. 177-201
    • Geng, F.1    Wenzel, S.2    Tansey, W.P.3
  • 39
    • 21444450086 scopus 로고    scopus 로고
    • Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis
    • Gingerich DJ, Gagne JM, Salter DW, Hellmann H, Estelle M, Ma LG, Vierstra RD (2005) Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis. J Biol Chem 280: 18810-18821.
    • (2005) J Biol Chem , vol.280 , pp. 18810-18821
    • Gingerich, D.J.1    Gagne, J.M.2    Salter, D.W.3    Hellmann, H.4    Estelle, M.5    Ma, L.G.6    Vierstra, R.D.7
  • 40
    • 0142216125 scopus 로고    scopus 로고
    • Attachment of the ubiquitinrelated protein Urm1p to the antioxidant protein Ahp1p
    • Goehring AS, Rivers DM, Sprague GF Jr (2003) Attachment of the ubiquitinrelated protein Urm1p to the antioxidant protein Ahp1p. Eukaryot Cell 2: 930-936.
    • (2003) Eukaryot Cell , vol.2 , pp. 930-936
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 42
    • 0035983934 scopus 로고    scopus 로고
    • Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene
    • Hanaoka H, Noda T, Shirano Y, Kato T, Hayashi H, Shibata D, Tabata S, Ohsumi Y (2002) Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene. Plant Physiol 129: 1181-1193.
    • (2002) Plant Physiol , vol.129 , pp. 1181-1193
    • Hanaoka, H.1    Noda, T.2    Shirano, Y.3    Kato, T.4    Hayashi, H.5    Shibata, D.6    Tabata, S.7    Ohsumi, Y.8
  • 43
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper JW, Schulman BA (2006) Structural complexity in ubiquitin recognition. Cell 124: 1133-1136.
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 46
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M (2009) Origin and function of ubiquitin-like proteins. Nature 458: 422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 48
    • 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
  • 49
    • 79955642715 scopus 로고    scopus 로고
    • The cullin-RING ubiquitin-protein ligases
    • Hua Z, Vierstra RD (2011) The cullin-RING ubiquitin-protein ligases. Annu Rev Plant Biol 62: 299-334.
    • (2011) Annu Rev Plant Biol , vol.62 , pp. 299-334
    • Hua, Z.1    Vierstra, R.D.2
  • 50
    • 79551550373 scopus 로고    scopus 로고
    • Phylogenetic comparison of F-box (FBX) gene superfamily within the plant kingdom reveals divergent evolutionary histories indicative of genomic drift
    • Hua Z, Zou C, Shiu SH, Vierstra RD (2011) Phylogenetic comparison of F-box (FBX) gene superfamily within the plant kingdom reveals divergent evolutionary histories indicative of genomic drift. PLoS ONE 6: e16219.
    • (2011) PLoS ONE , vol.6
    • Hua, Z.1    Zou, C.2    Shiu, S.H.3    Vierstra, R.D.4
  • 52
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: A new regulator of NF-kappaB activation
    • Iwai K, Tokunaga F (2009) Linear polyubiquitination: a new regulator of NF-kappaB activation. EMBO Rep 10: 706-713.
    • (2009) EMBO Rep , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 53
    • 79551497252 scopus 로고    scopus 로고
    • Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii
    • Jeong YJ, Jeong BC, Song HK (2011) Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii. Biochem Biophys Res Commun 405: 112-117.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 112-117
    • Jeong, Y.J.1    Jeong, B.C.2    Song, H.K.3
  • 54
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T, Lamark T (2011) Selective autophagy mediated by autophagic adapter proteins. Autophagy 7: 279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 55
    • 44449129585 scopus 로고    scopus 로고
    • A targeted proteomic analysis of the ubiquitin-like modifier Nedd8 and associated proteins
    • Jones J, Wu K, Yang Y, Guerrero C, Nillegoda N, Pan ZQ, Huang L (2008) A targeted proteomic analysis of the ubiquitin-like modifier Nedd8 and associated proteins. J Proteome Res 7: 1274-1287.
    • (2008) J Proteome Res , vol.7 , pp. 1274-1287
    • Jones, J.1    Wu, K.2    Yang, Y.3    Guerrero, C.4    Nillegoda, N.5    Pan, Z.Q.6    Huang, L.7
  • 57
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 59
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky DJ (2007) Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 8: 931-937.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 62
    • 33644993733 scopus 로고    scopus 로고
    • Genome analysis and functional characterization of the E2 and RINGtype E3 ligase ubiquitination enzymes of Arabidopsis
    • Kraft E, Stone SL, Ma L, Su N, Gao Y, Lau OS, Deng XW, Callis J (2005) Genome analysis and functional characterization of the E2 and RINGtype E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol 139: 1597-1611.
    • (2005) Plant Physiol , vol.139 , pp. 1597-1611
    • Kraft, E.1    Stone, S.L.2    Ma, L.3    Su, N.4    Gao, Y.5    Lau, O.S.6    Deng, X.W.7    Callis, J.8
  • 64
    • 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
  • 65
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H (2001) Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414: 325-329.
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 67
    • 43549110569 scopus 로고    scopus 로고
    • Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases
    • Lee JH, Terzaghi W, Gusmaroli G, Charron JB, Yoon HJ, Chen H, He YJ, Xiong Y, Deng XW (2008) Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases. Plant Cell 20: 152-167.
    • (2008) Plant Cell , vol.20 , pp. 152-167
    • Lee, J.H.1    Terzaghi, W.2    Gusmaroli, G.3    Charron, J.B.4    Yoon, H.J.5    Chen, H.6    He, Y.J.7    Xiong, Y.8    Deng, X.W.9
  • 71
    • 84865596150 scopus 로고    scopus 로고
    • Autophagy: A multifaceted intracellular system for bulk and selective recycling
    • (in press)
    • Li F, Vierstra RD (2012) Autophagy: a multifaceted intracellular system for bulk and selective recycling. Trends Plant Sci (in press).
    • (2012) Trends Plant Sci
    • Li, F.1    Vierstra, R.D.2
  • 73
    • 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, Soppe WJ (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
  • 74
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu Y, Schiff M, Czymmek K, Tallóczy Z, Levine B, Dinesh-Kumar SP (2005) Autophagy regulates programmed cell death during the plant innate immune response. Cell 121: 567-577.
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Tallóczy, Z.4    Levine, B.5    Dinesh-Kumar, S.P.6
  • 76
    • 34247342702 scopus 로고    scopus 로고
    • Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants
    • Maor R, Jones A, Nühse TS, Studholme DJ, Peck SC, Shirasu K (2007) Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants. Mol Cell Proteomics 6: 601-610.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 601-610
    • Maor, R.1    Jones, A.2    Nühse, T.S.3    Studholme, D.J.4    Peck, S.C.5    Shirasu, K.6
  • 77
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis MJ, Coutavas E, Blobel G (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 135: 1457-1470.
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 78
    • 84860469639 scopus 로고    scopus 로고
    • mRNA export and sumoylation: Lessons from plants
    • Meier I (2012) mRNA export and sumoylation: lessons from plants. Biochim Biophys Acta 1819: 531-537.
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 531
    • Meier, I.1
  • 79
    • 78049235116 scopus 로고    scopus 로고
    • Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis
    • Miller MJ, Barrett-Wilt GA, Hua Z, Vierstra RD (2010) Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc Natl Acad Sci USA 107: 16512-16517.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16512-16517
    • Miller, M.J.1    Barrett-Wilt, G.A.2    Hua, Z.3    Vierstra, R.D.4
  • 80
    • 85043062004 scopus 로고    scopus 로고
    • Quantitative proteomics reveal factors regulating RNA biology as dynamic targets of stressinduced SUMOylation in Arabidopsis
    • (in press)
    • Miller MJ, Scalf M, Smith LM, Vierstra RD (2012) Quantitative proteomics reveal factors regulating RNA biology as dynamic targets of stressinduced SUMOylation in Arabidopsis. Mol Cell Proteomics (in press).
    • (2012) Mol Cell Proteomics
    • Miller, M.J.1    Scalf, M.2    Smith, L.M.3    Vierstra, R.D.4
  • 83
    • 34848870906 scopus 로고    scopus 로고
    • Sumoylation, a post-translational regulatory process in plants
    • Miura K, Jin JB, Hasegawa PM (2007a) Sumoylation, a post-translational regulatory process in plants. Curr Opin Plant Biol 10: 495-502.
    • (2007) Curr Opin Plant Biol , vol.10 , pp. 495-502
    • Miura, K.1    Jin, J.B.2    Hasegawa, P.M.3
  • 85
    • 65249184459 scopus 로고    scopus 로고
    • Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling
    • Miura K, Lee J, Jin JB, Yoo CY, Miura T, Hasegawa PM (2009) Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling. Proc Natl Acad Sci USA 106: 5418-5423.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5418-5423
    • Miura, K.1    Lee, J.2    Jin, J.B.3    Yoo, C.Y.4    Miura, T.5    Hasegawa, P.M.6
  • 87
    • 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
  • 88
    • 0141625301 scopus 로고    scopus 로고
    • Structural determinants for the binding of ubiquitin-like domains to the proteasome
    • Mueller TD, Feigon J (2003) Structural determinants for the binding of ubiquitin-like domains to the proteasome. EMBO J 22: 4634-4645.
    • (2003) EMBO J , vol.22 , pp. 4634-4645
    • Mueller, T.D.1    Feigon, J.2
  • 89
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D, Riezman H (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315: 201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 90
    • 84865714121 scopus 로고    scopus 로고
    • Arabidopsis molybdopterin biosynthesis protein Cnx5 collaborates with the ubiquitin-like protein Urm11 in the thio-modification of tRNA
    • (in press)
    • Nakai Y, Harada A, Hashiguchi Y, Nakai M, Hayashi H (2012) Arabidopsis molybdopterin biosynthesis protein Cnx5 collaborates with the ubiquitin-like protein Urm11 in the thio-modification of tRNA. J Biol Chem (in press).
    • (2012) J Biol Chem
    • Nakai, Y.1    Harada, A.2    Hashiguchi, Y.3    Nakai, M.4    Hayashi, H.5
  • 92
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda NN, Ohsumi Y, Inagaki F (2010) Atg8-family interacting motif crucial for selective autophagy. FEBS Lett 584: 1379-1385.
    • (2010) FEBS Lett , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 94
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi Y (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nat Rev Mol Cell Biol 2: 211-216.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 95
    • 79960172953 scopus 로고    scopus 로고
    • Cysteine ubiquitination of PTS1 receptor Pex5p regulates Pex5p recycling
    • Okumoto K, Misono S, Miyata N, Matsumoto Y, Mukai S, Fujiki Y (2011) Cysteine ubiquitination of PTS1 receptor Pex5p regulates Pex5p recycling. Traffic 12: 1067-1083.
    • (2011) Traffic , vol.12 , pp. 1067-1083
    • Okumoto, K.1    Misono, S.2    Miyata, N.3    Matsumoto, Y.4    Mukai, S.5    Fujiki, Y.6
  • 96
    • 79960596484 scopus 로고    scopus 로고
    • Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1
    • Park BS, Song JT, Seo HS (2011) Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1. Nat Commun 2: 400.
    • (2011) Nat Commun , vol.2 , pp. 400
    • Park, B.S.1    Song, J.T.2    Seo, H.S.3
  • 97
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitinlike protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH (2008) Ubiquitinlike protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322: 1104-1107.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 98
    • 79952129481 scopus 로고    scopus 로고
    • Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress
    • Petroski MD, Salvesen GS, Wolf DA (2011) Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress. Proc Natl Acad Sci USA 108: 1749-1750.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1749-1750
    • Petroski, M.D.1    Salvesen, G.S.2    Wolf, D.A.3
  • 99
    • 45149130031 scopus 로고    scopus 로고
    • The ATG12-conjugating enzyme ATG10 is essential for autophagic vesicle formation in Arabidopsis thaliana
    • Phillips AR, Suttangkakul A, Vierstra RD (2008) The ATG12-conjugating enzyme ATG10 is essential for autophagic vesicle formation in Arabidopsis thaliana. Genetics 178: 1339-1353.
    • (2008) Genetics , vol.178 , pp. 1339-1353
    • Phillips, A.R.1    Suttangkakul, A.2    Vierstra, R.D.3
  • 102
    • 0032567404 scopus 로고    scopus 로고
    • The Rub family of ubiquitin-like proteins: Crystal structure of Arabidopsis Rub1 and expression of multiple Rubs in Arabidopsis
    • Rao-Naik C, delaCruz W, Laplaza JM, Tan S, Callis J, Fisher AJ (1998) The Rub family of ubiquitin-like proteins: crystal structure of Arabidopsis Rub1 and expression of multiple Rubs in Arabidopsis. J Biol Chem 273: 34976-34982.
    • (1998) J Biol Chem , vol.273 , pp. 34976-34982
    • Rao-Naik, C.1    Delacruz, W.2    Laplaza, J.M.3    Tan, S.4    Callis, J.5    Fisher, A.J.6
  • 103
    • 77950401024 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates plant hormone signaling
    • Santner A, Estelle M (2010) The ubiquitin-proteasome system regulates plant hormone signaling. Plant J 61: 1029-1040.
    • (2010) Plant J , vol.61 , pp. 1029-1040
    • Santner, A.1    Estelle, M.2
  • 104
    • 67649696034 scopus 로고    scopus 로고
    • Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis
    • Saracco SA, Hansson M, Scalf M, Walker JM, Smith LM, Vierstra RD (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
  • 105
    • 34548691835 scopus 로고    scopus 로고
    • Genetic analysis of SUMOylation in Arabidopsis: Conjugation of SUMO1 and SUMO2 to nuclear proteins is essential
    • Saracco SA, Miller MJ, Kurepa J, Vierstra RD (2007) Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol 145: 119-134.
    • (2007) Plant Physiol , vol.145 , pp. 119-134
    • Saracco, S.A.1    Miller, M.J.2    Kurepa, J.3    Vierstra, R.D.4
  • 107
    • 0036801543 scopus 로고    scopus 로고
    • Multiple ubiquitin ligasemediated processes require COP9 signalosome and AXR1 function
    • Schwechheimer C, Serino G, Deng XW (2002) Multiple ubiquitin ligasemediated processes require COP9 signalosome and AXR1 function. Plant Cell 14: 2553-2563.
    • (2002) Plant Cell , vol.14 , pp. 2553-2563
    • Schwechheimer, C.1    Serino, G.2    Deng, X.W.3
  • 109
    • 0036124032 scopus 로고    scopus 로고
    • Identification of the 19S regulatory particle subunits from the rice 26S proteasome
    • Shibahara T, Kawasaki H, 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
  • 110
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu Y, Okuda-Shimizu Y, Hendershot LM (2010) Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol Cell 40: 917-926.
    • (2010) Mol Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 111
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle J, Vierstra RD (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.1    Vierstra, R.D.2
  • 114
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E (2009) Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 16: 647-651.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 647-651
    • Striebel, F.1    Imkamp, F.2    Sutter, M.3    Steiner, M.4    Mamedov, A.5    Weber-Ban, E.6
  • 115
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H, Leverson JD, Hunter T (2007) Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J 26: 4102-4112.
    • (2007) EMBO J , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 116
    • 82755166963 scopus 로고    scopus 로고
    • The ATG1/ATG13 protein kinase complex is both a regulator and a target of autophagic recycling in Arabidopsis
    • Suttangkakul A, Li F, Chung T, Vierstra RD (2011) The ATG1/ATG13 protein kinase complex is both a regulator and a target of autophagic recycling in Arabidopsis. Plant Cell 23: 3761-3779.
    • (2011) Plant Cell , vol.23 , pp. 3761-3779
    • Suttangkakul, A.1    Li, F.2    Chung, T.3    Vierstra, R.D.4
  • 117
    • 33644590635 scopus 로고    scopus 로고
    • The crystal structure of plant ATG12 and its biological implication in autophagy
    • Suzuki NN, Yoshimoto K, Fujioka Y, Ohsumi Y, Inagaki F (2005) The crystal structure of plant ATG12 and its biological implication in autophagy. Autophagy 1: 119-126.
    • (2005) Autophagy , vol.1 , pp. 119-126
    • Suzuki, N.N.1    Yoshimoto, K.2    Fujioka, Y.3    Ohsumi, Y.4    Inagaki, F.5
  • 118
    • 80052363973 scopus 로고    scopus 로고
    • Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic receptor NBR1 and p62/SQSTM1
    • Svenning S, Lamark T, Krause K, Johansen T (2011) Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic receptor NBR1 and p62/SQSTM1. Autophagy 7: 1-18.
    • (2011) Autophagy , vol.7 , pp. 1-18
    • Svenning, S.1    Lamark, T.2    Krause, K.3    Johansen, T.4
  • 120
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham MH, Matic I, Mann M, Hay RT (2011) Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal 4: rs4.
    • (2011) Sci Signal , vol.4 , Issue.4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 123
    • 33644594726 scopus 로고    scopus 로고
    • Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and ATG12 conjugation pathways
    • Thompson AR, Doelling JH, Suttangkakul A, Vierstra RD (2005) Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and ATG12 conjugation pathways. Plant Physiol 138: 2097-2110.
    • (2005) Plant Physiol , vol.138 , pp. 2097-2110
    • Thompson, A.R.1    Doelling, J.H.2    Suttangkakul, A.3    Vierstra, R.D.4
  • 124
    • 14744281878 scopus 로고    scopus 로고
    • Autophagic recycling: Lessons from yeast help define the process in plants
    • Thompson AR, Vierstra RD (2005) Autophagic recycling: lessons from yeast help define the process in plants. Curr Opin Plant Biol 8: 165-173.
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 165-173
    • Thompson, A.R.1    Vierstra, R.D.2
  • 125
    • 33645930028 scopus 로고    scopus 로고
    • Protein aggregates are transported to vacuoles by a macroautophagic mechanism in nutrient-starved plant cells
    • Toyooka K, Moriyasu Y, Goto Y, Takeuchi M, Fukuda H, Matsuoka K (2006) Protein aggregates are transported to vacuoles by a macroautophagic mechanism in nutrient-starved plant cells. Autophagy 2: 96-106.
    • (2006) Autophagy , vol.2 , pp. 96-106
    • Toyooka, K.1    Moriyasu, Y.2    Goto, Y.3    Takeuchi, M.4    Fukuda, H.5    Matsuoka, K.6
  • 126
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich HD, Walden H (2010) Ubiquitin signalling in DNA replication and repair. Nat Rev Mol Cell Biol 11: 479-489.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 128
    • 77955898187 scopus 로고    scopus 로고
    • Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense
    • van den Burg HA, Kini RK, Schuurink RC, Takken FLW (2010) Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense. Plant Cell 22: 1998-2016.
    • (2010) Plant Cell , vol.22 , pp. 1998-2016
    • van den Burg, H.A.1    Kini, R.K.2    Schuurink, R.C.3    Takken, F.L.W.4
  • 130
    • 79953100002 scopus 로고    scopus 로고
    • The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism
    • Vanhee C, Zapotoczny G, Masquelier D, Ghislain M, Batoko H (2011) The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism. Plant Cell 23: 785-805.
    • (2011) Plant Cell , vol.23 , pp. 785-805
    • Vanhee, C.1    Zapotoczny, G.2    Masquelier, D.3    Ghislain, M.4    Batoko, H.5
  • 131
    • 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
  • 133
    • 60249083823 scopus 로고    scopus 로고
    • Autophagy plays a role in chloroplast degradation during senescence in individually darkened leaves
    • Wada S, Ishida H, Izumi M, Yoshimoto K, Ohsumi Y, Mae T, Makino A (2009) Autophagy plays a role in chloroplast degradation during senescence in individually darkened leaves. Plant Physiol 149: 885-893.
    • (2009) Plant Physiol , vol.149 , pp. 885-893
    • Wada, S.1    Ishida, H.2    Izumi, M.3    Yoshimoto, K.4    Ohsumi, Y.5    Mae, T.6    Makino, A.7
  • 134
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • Wang C, Xi J, Begley TP, Nicholson LK (2001) Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat Struct Biol 8: 47-51.
    • (2001) Nat Struct Biol , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.P.3    Nicholson, L.K.4
  • 135
    • 78549254832 scopus 로고    scopus 로고
    • Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation
    • Wang T, Darwin KH, Li H (2010) Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. Nat Struct Mol Biol 17: 1352-1357.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1352-1357
    • Wang, T.1    Darwin, K.H.2    Li, H.3
  • 136
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake VM, Workman JL (2008) Histone ubiquitination: triggering gene activity. Mol Cell 29: 653-663.
    • (2008) Mol Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 137
    • 11144276022 scopus 로고    scopus 로고
    • Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast
    • Wilkinson CR, Dittmar GA, Ohi MD, Uetz P, Jones N, Finley D (2004) Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. Curr Biol 14: 2283-2288.
    • (2004) Curr Biol , vol.14 , pp. 2283-2288
    • Wilkinson, C.R.1    Dittmar, G.A.2    Ohi, M.D.3    Uetz, P.4    Jones, N.5    Finley, D.6
  • 138
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson KA, Henley JM (2010) Mechanisms, regulation and consequences of protein SUMOylation. Biochem J 428: 133-145.
    • (2010) Biochem J , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 139
    • 33846378524 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis
    • Xiong Y, Contento AL, Nguyen PQ, Bassham DC (2007) Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis. Plant Physiol 143: 291-299.
    • (2007) Plant Physiol , vol.143 , pp. 291-299
    • Xiong, Y.1    Contento, A.L.2    Nguyen, P.Q.3    Bassham, D.C.4
  • 141
  • 142
    • 0034512691 scopus 로고    scopus 로고
    • The ubiquitin-specific protease family from Arabidopsis: AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine
    • Yan N, Doelling JH, Falbel TG, Durski AM, Vierstra RD (2000) The ubiquitin-specific protease family from Arabidopsis: AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine. Plant Physiol 124: 1828-1843.
    • (2000) Plant Physiol , vol.124 , pp. 1828-1843
    • Yan, N.1    Doelling, J.H.2    Falbel, T.G.3    Durski, A.M.4    Vierstra, R.D.5
  • 143
    • 14744268915 scopus 로고    scopus 로고
    • Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy
    • Yoshimoto K, Hanaoka H, Sato S, Kato T, Tabata S, Noda T, Ohsumi Y (2004) Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy. Plant Cell 16: 2967-2983.
    • (2004) Plant Cell , vol.16 , pp. 2967-2983
    • Yoshimoto, K.1    Hanaoka, H.2    Sato, S.3    Kato, T.4    Tabata, S.5    Noda, T.6    Ohsumi, Y.7
  • 145
    • 0042431612 scopus 로고    scopus 로고
    • SIR1, an upstream component in auxin signaling identified by chemical genetics
    • Zhao Y, Dai X, Blackwell HE, Schreiber SL, Chory J (2003) SIR1, an upstream component in auxin signaling identified by chemical genetics. Science 301: 1107-1110.
    • (2003) Science , vol.301 , pp. 1107-1110
    • Zhao, Y.1    Dai, X.2    Blackwell, H.E.3    Schreiber, S.L.4    Chory, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.