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Volumn 279, Issue 4, 2008, Pages 371-383

SUMO-conjugating enzyme (Sce) and FK506-binding protein (FKBP) encoding rice (Oryza sativa L.) genes: Genome-wide analysis, expression studies and evidence for their involvement in abiotic stress response

Author keywords

FK506 binding protein (FKBP); High temperature; Nuclear localization; Peptidyl prolyl cis trans isomerase (PPIase); Rice; Stress regulation; SUMO conjugating enzyme (Sce)

Indexed keywords

CELL PROTEIN; CHAPERONE; COMPLEMENTARY DNA; ENZYME; FK 506 BINDING PROTEIN; PEPTIDYLPROLYL ISOMERASE; PROTEIN UBC9; SUMO CONJUGATING ENZYME; SUMO PROTEIN;

EID: 43349086177     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-008-0318-5     Document Type: Article
Times cited : (64)

References (61)
  • 1
    • 0037342584 scopus 로고    scopus 로고
    • Molecular characterization of rice hsp101: Complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types
    • Agarwal M, Sahi C, Katiyar-Agarwal S, Agarwal S, Young T, Gallie DR, Sharma VM, Ganesan K, Grover A (2003) Molecular characterization of rice hsp101: complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types. Plant Mol Biol 51:543-553
    • (2003) Plant Mol Biol , vol.51 , pp. 543-553
    • Agarwal, M.1    Sahi, C.2    Katiyar-Agarwal, S.3    Agarwal, S.4    Young, T.5    Gallie, D.R.6    Sharma, V.M.7    Ganesan, K.8    Grover, A.9
  • 4
    • 0033393804 scopus 로고    scopus 로고
    • Cyclophilins and their possible role in the stress response
    • Andreeva L, Heads R, Green CJ (1999) Cyclophilins and their possible role in the stress response. Int J Exp Pathol 80:305-315
    • (1999) Int J Exp Pathol , vol.80 , pp. 305-315
    • Andreeva, L.1    Heads, R.2    Green, C.J.3
  • 5
    • 11944261508 scopus 로고    scopus 로고
    • Comparative analysis of the hspA mutant and wildtype Synechocystis sp. strain PCC6803 under salt stress: Evaluation of the role of hspA in salt stress management
    • Asadulghani, Nitta K, Kaneko Y, Kojima K, Fukuzawa H, Kosaka H, Nakamoto H (2004) Comparative analysis of the hspA mutant and wildtype Synechocystis sp. strain PCC6803 under salt stress: evaluation of the role of hspA in salt stress management. Arch Microbiol 182:487-497
    • (2004) Arch Microbiol , vol.182 , pp. 487-497
    • Asadulghani1    Nitta, K.2    Kaneko, Y.3    Kojima, K.4    Fukuzawa, H.5    Kosaka, H.6    Nakamoto, H.7
  • 6
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston RS, Viitanen PV, Vierling E (1996) Molecular chaperones and protein folding in plants. Plant Mol Biol 32:191-222
    • (1996) Plant Mol Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0036702796 scopus 로고    scopus 로고
    • The involvement of mammalian and plant FK506-binding proteins (FKBPs) in development
    • Breiman A, Camus I (2002) The involvement of mammalian and plant FK506-binding proteins (FKBPs) in development. Transgenic Res 11:321-335
    • (2002) Transgenic Res , vol.11 , pp. 321-335
    • Breiman, A.1    Camus, I.2
  • 10
    • 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
  • 11
    • 0036914106 scopus 로고    scopus 로고
    • Analyzing protein-protein interactions with the yeast two-hybrid system
    • Causier B, Davies B (2004) Analyzing protein-protein interactions with the yeast two-hybrid system. Plant Mol Biol 50:855-870
    • (2004) Plant Mol Biol , vol.50 , pp. 855-870
    • Causier, B.1    Davies, B.2
  • 12
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 13
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson CM (2004) Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 15:3-16
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 14
    • 0346121808 scopus 로고    scopus 로고
    • Differential distribution of the cognate and heat-stress-induced isoforms of high Mr cis-trans prolyl peptidyl isomerase (FKBP) in the cytoplasm and nucleoplasm
    • Dwivedi RS, Breiman A, Herman EM (2003) Differential distribution of the cognate and heat-stress-induced isoforms of high Mr cis-trans prolyl peptidyl isomerase (FKBP) in the cytoplasm and nucleoplasm. J Exp Bot 54:2679-2689
    • (2003) J Exp Bot , vol.54 , pp. 2679-2689
    • Dwivedi, R.S.1    Breiman, A.2    Herman, E.M.3
  • 15
    • 0021958921 scopus 로고
    • G-substitution to A-substitution in the distal CCAAT box of the gamma-globin gene in Greek hereditary persistence of fetal hemoglobin
    • Gelinas R, Endlich B, Pfeiffer C, Yagi M, Stamatoyannopoulos G (1985) G-substitution to A-substitution in the distal CCAAT box of the gamma-globin gene in Greek hereditary persistence of fetal hemoglobin. Nature 313:323-325
    • (1985) Nature , vol.313 , pp. 323-325
    • Gelinas, R.1    Endlich, B.2    Pfeiffer, C.3    Yagi, M.4    Stamatoyannopoulos, G.5
  • 16
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • Gill G (2005) Something about SUMO inhibits transcription. Curr Opin Genet Dev 15:536-541
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 536-541
    • Gill, G.1
  • 17
    • 0035209361 scopus 로고    scopus 로고
    • FKBPs: At the crossroads of folding and transduction
    • Harrar Y, Bellini C, Faure JD (2001) FKBPs: at the crossroads of folding and transduction. Trends Plant Sci 6:426-431
    • (2001) Trends Plant Sci , vol.6 , pp. 426-431
    • Harrar, Y.1    Bellini, C.2    Faure, J.D.3
  • 18
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and sub-cellular localization of GFP are required to mark transgenic Arabidopsis plants brightly
    • Haseloff J, Siemering KR, Prasher DC, Hodges S (1997) Removal of a cryptic intron and sub-cellular localization of GFP are required to mark transgenic Arabidopsis plants brightly. Proc Natl Acad Sci 94:2122-2127
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodges, S.4
  • 19
    • 1942501867 scopus 로고    scopus 로고
    • Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis
    • He Z, Li L, Luan S (2004) Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis. Plant Physiol 134:1-20
    • (2004) Plant Physiol , vol.134 , pp. 1-20
    • He, Z.1    Li, L.2    Luan, S.3
  • 20
    • 3543001076 scopus 로고    scopus 로고
    • Identification of Xenopus heat shock transcription factor-2: Conserved role of sumoylation in regulating deoxyribonucleic acid-binding activity of heat shock transcription factor-2 proteins
    • Hilgarth RS, Murphy LA, O'Connor CM, Clark JA, Park-Sarge OK, Sarge KD (2004) Identification of Xenopus heat shock transcription factor-2: conserved role of sumoylation in regulating deoxyribonucleic acid-binding activity of heat shock transcription factor-2 proteins. Cell Stress Chaperones 9:214-220
    • (2004) Cell Stress Chaperones , vol.9 , pp. 214-220
    • Hilgarth, R.S.1    Murphy, L.A.2    O'Connor, C.M.3    Clark, J.A.4    Park-Sarge, O.K.5    Sarge, K.D.6
  • 21
    • 34547495865 scopus 로고    scopus 로고
    • Perception and transduction of abscisic acid signals: Keys to the function of the versatile plant hormone ABA
    • Hirayama T, Shinozaki K (2007) Perception and transduction of abscisic acid signals: keys to the function of the versatile plant hormone ABA. Trends Plant Sci 12:343-351
    • (2007) Trends Plant Sci , vol.12 , pp. 343-351
    • Hirayama, T.1    Shinozaki, K.2
  • 22
    • 0034725918 scopus 로고    scopus 로고
    • All in the ubiquitin family
    • Hochstrasser M (2000) All in the ubiquitin family. Science 289:563-564
    • (2000) Science , vol.289 , pp. 563-564
    • Hochstrasser, M.1
  • 24
    • 0032063540 scopus 로고    scopus 로고
    • A maize FK506-sensitive immunophilin, mzFKBP-66, is a peptidylproline cis-trans-isomerase that interacts with calmodulin and a 36-kDa cytoplasmic protein
    • Hueros G, Rahfeld J, Salamini F, Thompson R (1998) A maize FK506-sensitive immunophilin, mzFKBP-66, is a peptidylproline cis-trans-isomerase that interacts with calmodulin and a 36-kDa cytoplasmic protein. Planta 205:121-131
    • (1998) Planta , vol.205 , pp. 121-131
    • Hueros, G.1    Rahfeld, J.2    Salamini, F.3    Thompson, R.4
  • 25
    • 0032489328 scopus 로고    scopus 로고
    • Cloning and developmental expression of a nuclear ubiquitin-conjugating enzyme (DmUbc9) that interacts with small heat shock proteins in Drosophila melanogaster
    • Joanisse DR, Inaguma Y, Tanguay RM (1998) Cloning and developmental expression of a nuclear ubiquitin-conjugating enzyme (DmUbc9) that interacts with small heat shock proteins in Drosophila melanogaster. Biochem Biophys Res Commun 244:102-109
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 102-109
    • Joanisse, D.R.1    Inaguma, Y.2    Tanguay, R.M.3
  • 26
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson ES (2004) Protein modification by SUMO. Annu Rev Biochem 73:355-382
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 27
    • 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
  • 28
    • 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
  • 30
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    • Lois LM, Lima CD (2005) Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J 24:439-451
    • (2005) EMBO J , vol.24 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 31
    • 0037781038 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis
    • Lois LM, Lima CD, Chua NH (2003) Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell 15:1347-1359
    • (2003) Plant Cell , vol.15 , pp. 1347-1359
    • Lois, L.M.1    Lima, C.D.2    Chua, N.H.3
  • 32
    • 32644466192 scopus 로고    scopus 로고
    • The expression of the large rice FK506 binding proteins demonstrate tissue specificity and heat stress responsiveness
    • Magiri EN, Farchi-Pistany O, Avni A, Breiman A (2006) The expression of the large rice FK506 binding proteins demonstrate tissue specificity and heat stress responsiveness. Plant Sci 170:695-704
    • (2006) Plant Sci , vol.170 , pp. 695-704
    • Magiri, E.N.1    Farchi-Pistany, O.2    Avni, A.3    Breiman, A.4
  • 34
    • 0031857049 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA corresponding to a stress activated cyclophilin gene in Solanum commersoni
    • Meza-Zepeda LA, Bando MM, Palva ET, Heino P (1998) Isolation and characterization of a cDNA corresponding to a stress activated cyclophilin gene in Solanum commersoni. J Exp Bot 49:1451-1452
    • (1998) J Exp Bot , vol.49 , pp. 1451-1452
    • Meza-Zepeda, L.A.1    Bando, M.M.2    Palva, E.T.3    Heino, P.4
  • 35
    • 0033230242 scopus 로고    scopus 로고
    • Protein folding in the plant cell
    • Miernyk JA (1999) Protein folding in the plant cell. Plant Physiol 121:695-703
    • (1999) Plant Physiol , vol.121 , pp. 695-703
    • Miernyk, J.A.1
  • 36
    • 0033615705 scopus 로고    scopus 로고
    • Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation
    • Morris DP, Phatnani HP, Greenleaf AL (1999) Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation. J Biol Chem 274:31583-31587
    • (1999) J Biol Chem , vol.274 , pp. 31583-31587
    • Morris, D.P.1    Phatnani, H.P.2    Greenleaf, A.L.3
  • 37
    • 33645349063 scopus 로고    scopus 로고
    • Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation
    • Mueller JW, Kessler D, Neumann D, Stratmann T, Papatheodorou P, Hartmann-Fatu C, Bayer P (2006) Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation. BMC Mol Biol 7:9
    • (2006) BMC Mol Biol , vol.7 , pp. 9
    • Mueller, J.W.1    Kessler, D.2    Neumann, D.3    Stratmann, T.4    Papatheodorou, P.5    Hartmann-Fatu, C.6    Bayer, P.7
  • 39
    • 0026349605 scopus 로고
    • The anaerobic responsive element contains two GC-rich sequences essential for binding a nuclear protein and hypoxic activation of the maize Adh1 promoter
    • Olive MR, Peacock WJ, Dennis ES (1991) The anaerobic responsive element contains two GC-rich sequences essential for binding a nuclear protein and hypoxic activation of the maize Adh1 promoter. Nucleic Acids Res 19:7053-7060
    • (1991) Nucleic Acids Res , vol.19 , pp. 7053-7060
    • Olive, M.R.1    Peacock, W.J.2    Dennis, E.S.3
  • 40
    • 0029856744 scopus 로고    scopus 로고
    • Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants
    • Owens-Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P (1996) Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants. Biochem 35:15249-15255
    • (1996) Biochem , vol.35 , pp. 15249-15255
    • Owens-Grillo, J.K.1    Stancato, L.F.2    Hoffmann, K.3    Pratt, W.B.4    Krishna, P.5
  • 41
    • 33644836920 scopus 로고    scopus 로고
    • Leafing through the genomes of our major crop plants: Strategies for capturing unique information
    • Paterson AH (2006) Leafing through the genomes of our major crop plants: strategies for capturing unique information. Nat Rev Genet 7:174-184
    • (2006) Nat Rev Genet , vol.7 , pp. 174-184
    • Paterson, A.H.1
  • 42
    • 0036300965 scopus 로고    scopus 로고
    • Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport
    • Pichler A, Melchoir F (2002) Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport. Traffic 3:381-387
    • (2002) Traffic , vol.3 , pp. 381-387
    • Pichler, A.1    Melchoir, F.2
  • 43
    • 19344375177 scopus 로고    scopus 로고
    • Plant immunophilins: Functional versatility beyond protein maturation
    • Romano P, Gray J, Horton P, Luan S (2005) Plant immunophilins: functional versatility beyond protein maturation. New Phytol 166:753-769
    • (2005) New Phytol , vol.166 , pp. 753-769
    • Romano, P.1    Gray, J.2    Horton, P.3    Luan, S.4
  • 44
    • 0038531176 scopus 로고    scopus 로고
    • Isolation and expression analysis of salt stress-associated ESTs from contrasting rice cultivars using a PCR-based subtraction method
    • Sahi C, Agarwal M, Reddy MK, Sopory SK, Grover A (2003) Isolation and expression analysis of salt stress-associated ESTs from contrasting rice cultivars using a PCR-based subtraction method. Theor Appl Genet 106:620-628
    • (2003) Theor Appl Genet , vol.106 , pp. 620-628
    • Sahi, C.1    Agarwal, M.2    Reddy, M.K.3    Sopory, S.K.4    Grover, A.5
  • 45
    • 33747793998 scopus 로고    scopus 로고
    • Salt stress response in rice: Genetics, molecular biology, and comparative genomics
    • Sahi C, Singh A, Kumar K, Blumwald E, Grover A (2006) Salt stress response in rice: genetics, molecular biology, and comparative genomics. Funct Integr Genomics 6:263-284
    • (2006) Funct Integr Genomics , vol.6 , pp. 263-284
    • Sahi, C.1    Singh, A.2    Kumar, K.3    Blumwald, E.4    Grover, A.5
  • 46
    • 34447324661 scopus 로고    scopus 로고
    • Meiosis and ubiquitin-related modifier (SUMO)-conjugating enzyme, Ubc9
    • Sakaguchi K, Koshiyama A, Iwabata K (2007) Meiosis and ubiquitin-related modifier (SUMO)-conjugating enzyme, Ubc9. FEBS J 274:3519-3531
    • (2007) FEBS J , vol.274 , pp. 3519-3531
    • Sakaguchi, K.1    Koshiyama, A.2    Iwabata, K.3
  • 48
    • 34548691835 scopus 로고    scopus 로고
    • Genetic analysis of sumoylation in Arabidopsis: Heat-induced conjugation of SUMO1 and 2 is essential
    • (in press). doi:10.1104/pp.107.102285
    • Saracco SA, Miller MJ, Kurepa J, Vierstra RD (2008) Genetic analysis of sumoylation in Arabidopsis: heat-induced conjugation of SUMO1 and 2 is essential. Plant Physiol (in press). doi:10.1104/pp.107.102285
    • (2008) Plant Physiol
    • Saracco, S.A.1    Miller, M.J.2    Kurepa, J.3    Vierstra, R.D.4
  • 49
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA 95:5857-5864
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 51
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and N-phase cyclins
    • Seufert W, Futcher B, Jentsch S (1995) Role of a ubiquitin-conjugating enzyme in degradation of S- and N-phase cyclins. Nature 373:78-81
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 52
    • 33846010183 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and transcription: Is there a twist in the tail?
    • Shaw PE (2007) Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail? EMBO Rep 8:40-45
    • (2007) EMBO Rep , vol.8 , pp. 40-45
    • Shaw, P.E.1
  • 55
    • 27544478621 scopus 로고    scopus 로고
    • The sequence of rice chromosome 11 and 12, rich in disease resistance genes and recent gene duplications
    • The Rice Chromosomes 11, 12 Sequencing Consortia
    • The Rice Chromosomes 11, 12 Sequencing Consortia (2005) The sequence of rice chromosome 11 and 12, rich in disease resistance genes and recent gene duplications. BMC Biol 3:20
    • (2005) BMC Biol , vol.3 , pp. 20
  • 56
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 57
    • 1942437673 scopus 로고    scopus 로고
    • The immunophilin-interacting protein AtFIP37 from Arabidopsis is essential for plant development and is involved in trichome endoreduplication
    • Vespa L, Vachon G, Berger F, Perazza D, Faure JD, Herzog M (2004) The immunophilin-interacting protein AtFIP37 from Arabidopsis is essential for plant development and is involved in trichome endoreduplication. Plant Physiol 134:1283-1292
    • (2004) Plant Physiol , vol.134 , pp. 1283-1292
    • Vespa, L.1    Vachon, G.2    Berger, F.3    Perazza, D.4    Faure, J.D.5    Herzog, M.6
  • 59
    • 0029901423 scopus 로고    scopus 로고
    • Identification of the structural and functional human homolog of the yeast conjugating enzyme UBC9
    • Yasugi T, Howley PM (1996) Identification of the structural and functional human homolog of the yeast conjugating enzyme UBC9. Nucleic Acids Res 24:2005-2010
    • (1996) Nucleic Acids Res , vol.24 , pp. 2005-2010
    • Yasugi, T.1    Howley, P.M.2
  • 60
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • Zhou W, Ryan JJ, Zhou H (2004) Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J Biol Chem 279:32262-32268
    • (2004) J Biol Chem , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 61
    • 34250150964 scopus 로고
    • Study on nuclear and cytoplasmic genome expression in wheat by two-dimensional gel electrophoresis
    • Zivy M, Thiellement H, deVienne D, Hofmann JP (1983) Study on nuclear and cytoplasmic genome expression in wheat by two-dimensional gel electrophoresis. Theor Appl Genet 66:1-7
    • (1983) Theor Appl Genet , vol.66 , pp. 1-7
    • Zivy, M.1    Thiellement, H.2    Devienne, D.3    Hofmann, J.P.4


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