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Volumn 11, Issue 2, 1997, Pages 213-226

The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; COMPLEMENTARY DNA; HYBRID PROTEIN; LIGASE; PLANT DNA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 0031080458     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.11020213.x     Document Type: Article
Times cited : (79)

References (61)
  • 1
    • 0025685244 scopus 로고
    • Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations, and necrotic lesions in a higher plant
    • Bachmair, A., Becker, F., Masterson, V. and Schell, J. (1990) Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations, and necrotic lesions in a higher plant. EMBO J. 9, 4543-4549.
    • (1990) EMBO J. , vol.9 , pp. 4543-4549
    • Bachmair, A.1    Becker, F.2    Masterson, V.3    Schell, J.4
  • 2
    • 0027675474 scopus 로고
    • Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin-conjugating enzyme (E2) from Arabidopsis thaliana
    • Battling, D., Rehling, P. and Weiler, E.W. (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
    • Battling, D.1    Rehling, P.2    Weiler, E.W.3
  • 3
    • 0000810989 scopus 로고
    • Altered response to viral infection by tobacco plants perturbed in ubiquitin system
    • Becken F., Buschfeld, E., Schell, J. and Bachmair, A. (1993) Altered response to viral infection by tobacco plants perturbed in ubiquitin system. Plant J. 3, 875-881.
    • (1993) Plant J. , vol.3 , pp. 875-881
    • Becken, F.1    Buschfeld, E.2    Schell, J.3    Bachmair, A.4
  • 4
    • 0024060207 scopus 로고
    • Characterization of a polyubiquitin gene in Arabidopsis thaliana
    • Burke, T.J., Callis, J.A. and Vierstra, R.D. (1988) Characterization of a polyubiquitin gene in Arabidopsis thaliana. Mol. Gen. Genet. 213, 435-443.
    • (1988) Mol. Gen. Genet. , vol.213 , pp. 435-443
    • Burke, T.J.1    Callis, J.A.2    Vierstra, R.D.3
  • 5
    • 0028836104 scopus 로고
    • Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia
    • Callis, J., Carpenter, T., Sun, C.-W. and Vierstra, R.D. (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
  • 6
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT α2 repressor
    • Chen, P., Johnson, P., Sommer, T., Jentsch, S. and Hochstrasser, M. (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT α2 repressor. Cell, 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 7
    • 0026728663 scopus 로고
    • Phytochrome requires the 6-kDa N-terminal domain for full biological activity
    • Cherry, J.R., Hundred, D. and Vierstra, R.D. (1992) Phytochrome requires the 6-kDa N-terminal domain for full biological activity. Proc. Natl Acad. Sci. USA, 89, 5039-5043.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5039-5043
    • Cherry, J.R.1    Hundred, D.2    Vierstra, R.D.3
  • 8
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary, R.R., Dermody, J.J., Jha, K. K. and Ozer, H.L (1994) Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell. Biol. 14, 1997-2003.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1997-2003
    • Chowdary, R.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 9
    • 0026816010 scopus 로고
    • Maize polyubiquitin genes, structure, thermal perturbation of expression, transcript splicing, and promoter activity following transfer to protoplasts by electroporation
    • Christensen, A.M., Sharrock, R.A. and Quail, P.H. (1992) Maize polyubiquitin genes, structure, thermal perturbation of expression, transcript splicing, and promoter activity following transfer to protoplasts by electroporation. Plant Mol. Biol. 18, 675-689.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 675-689
    • Christensen, A.M.1    Sharrock, R.A.2    Quail, P.H.3
  • 10
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell, 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 11
    • 0020478687 scopus 로고
    • 'Covalent affinity' purification of ubiquitin-activating enzyme
    • Ciechanover, A., Elias, S., Heller, H. and Herskho, A. (1982) 'Covalent affinity' purification of ubiquitin-activating enzyme. J. Biol. Chem. 257, 2537-2542.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2537-2542
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Herskho, A.4
  • 12
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover, A., Finley, E. and Varshavsky, A. (1984) Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell, 37, 57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, E.2    Varshavsky, A.3
  • 13
    • 0028967412 scopus 로고
    • Phosphorylation of ubiquitin-activating enzyme in cultured cells
    • Cook, J.C. and Chock, P.B. (1995) Phosphorylation of ubiquitin-activating enzyme in cultured cells. Proc. Natl Acad. Sci. USA, 91, 3454-3457.
    • (1995) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3454-3457
    • Cook, J.C.1    Chock, P.B.2
  • 14
    • 0027975055 scopus 로고
    • Changes in protein ubiquitination and the expression of ubiquitin-encoding transcripts in daylily petals during floral development and senescence
    • Courtney, S.E., Rider, C.C. and Stead, A.D. (1994) Changes in protein ubiquitination and the expression of ubiquitin-encoding transcripts in daylily petals during floral development and senescence. Physiol. Plant. 91, 196-204.
    • (1994) Physiol. Plant. , vol.91 , pp. 196-204
    • Courtney, S.E.1    Rider, C.C.2    Stead, A.D.3
  • 15
    • 0000111203 scopus 로고
    • Semi-quantitative PCR for the analysis of gene expression
    • McPherson, M.J., Quirke, P Taylor, G.R., eds. Oxford: IRL Press
    • Dallman, M.J. and Porter, A.C.G. (1991) Semi-quantitative PCR for the analysis of gene expression. In PCR, A Practical Approach (McPherson, M.J., Quirke, P. and Taylor, G.R., eds). Oxford: IRL Press, pp. 215-224.
    • (1991) PCR, A Practical Approach , pp. 215-224
    • Dallman, M.J.1    Porter, A.C.G.2
  • 16
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. and Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 18
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzymes from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. and Varshavsky, A. (1984) Thermolability of ubiquitin-activating enzymes from the mammalian cell cycle mutant ts85. Cell, 37, 43-55.
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 19
    • 0027021315 scopus 로고
    • Ubiquitin genes are differentially regulated in protoplast-derived cultures of Nicotiana sylvestris and in response to various stresses
    • Genschik, P., Parmentier, Y., Durr, A., Marbach, J., Criqui, M.C., Jamet, E. and Fleck, J. (1992) Ubiquitin genes are differentially regulated in protoplast-derived cultures of Nicotiana sylvestris and in response to various stresses. Plant Mol. Biol. 20, 897-910.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 897-910
    • Genschik, P.1    Parmentier, Y.2    Durr, A.3    Marbach, J.4    Criqui, M.C.5    Jamet, E.6    Fleck, J.7
  • 20
    • 0028519157 scopus 로고
    • Molecular characterization of β-type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an α-type proteasome subunit early in the cell cycle
    • Genschik, P., Jamet, E., Phillips, G., Parmentier, Y., Gigot, C. and Fleck, J. (1994) Molecular characterization of β-type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an α-type proteasome subunit early in the cell cycle. Plant J. 6, 537-546.
    • (1994) Plant J. , vol.6 , pp. 537-546
    • Genschik, P.1    Jamet, E.2    Phillips, G.3    Parmentier, Y.4    Gigot, C.5    Fleck, J.6
  • 21
    • 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, P.-A., Carpenter, T.B., van Nocker, S., Sullivan, M.L. and Vierstra, R.D. (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
  • 22
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzner, M., Murray, A.W. and Kirschner, M.W. (1991) Cyclin is degraded by the ubiquitin pathway. Nature, 349, 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzner, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 23
    • 0025960565 scopus 로고
    • Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1
    • Handley, P.M., Mueckler, M., Siegel, N.R. and Ciechanover, A. (1991) Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. Proc. Natl Acad. Sci. USA, 88, 258-262.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 258-262
    • Handley, P.M.1    Mueckler, M.2    Siegel, N.R.3    Ciechanover, A.4
  • 24
    • 0028577266 scopus 로고
    • Human ubiquitin-activating enzyme. E1: Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs
    • Handley-Gearhart, P.M., Stephen, A.G., Trausch-Azar, J.S., Ciechanover, A. and Schwarz, A.L. (1994) Human ubiquitin-activating enzyme. E1: indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs. J. Biol. Chem. 269, 33171-33178.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33171-33178
    • Handley-Gearhart, P.M.1    Stephen, A.G.2    Trausch-Azar, J.S.3    Ciechanover, A.4    Schwarz, A.L.5
  • 25
    • 0000334676 scopus 로고
    • Analysis of the ubiquitin-dependent proteolytic pathway in wheat germ: Isolation and characterization of the ubiquitin-activating enzyme (E1)
    • Hatfield, P.M. and Vierstra, R.D. (1989) Analysis of the ubiquitin-dependent proteolytic pathway in wheat germ: isolation and characterization of the ubiquitin-activating enzyme (E1). Biochemistry, 28, 735-742.
    • (1989) Biochemistry , vol.28 , pp. 735-742
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 26
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme (E1) from wheat: Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield, P.M. and Vierstra, R.D. (1992) Multiple forms of ubiquitin-activating enzyme (E1) from wheat: identification of an essential cysteine by in vitro mutagenesis. J. Biol. Chem. 267, 14799-14803.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 27
    • 0024995885 scopus 로고
    • Cloning of ubiquitin-activating enzyme from wheat and expression of a functional protein in Escherichia coli
    • Hatfield, P.M. Callis, J.A. and Vierstra, R.D. (1990) Cloning of ubiquitin-activating enzyme from wheat and expression of a functional protein in Escherichia coli. J. Biol. Chem. 265, 15813-15817.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15813-15817
    • Hatfield, P.M.1    Callis, J.A.2    Vierstra, R.D.3
  • 28
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. and Riezman, H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell, 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 29
    • 0024978147 scopus 로고
    • Ubiquitin-phytochrome conjugates: Pool dynamics during in vivo phytochrome degradation
    • Jabben, M., Shanklin, J. and Vierstra, R.D. (1989) Ubiquitin-phytochrome conjugates: pool dynamics during in vivo phytochrome degradation. J. Biol. Chem. 264, 4998-5005.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4998-5005
    • Jabben, M.1    Shanklin, J.2    Vierstra, R.D.3
  • 30
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R.A., Kavanagh, T.A. and Bevan, M.W. (1987) GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6, 3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 31
    • 0025831142 scopus 로고
    • A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1
    • Kay, G.F., Ashworth, A., Penny, G.D., Dunlop, M., Swift, S., Brockdorff, N. and Rastan, S. (1991) A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1. Nature, 354, 486-489.
    • (1991) Nature , vol.354 , pp. 486-489
    • Kay, G.F.1    Ashworth, A.2    Penny, G.D.3    Dunlop, M.4    Swift, S.5    Brockdorff, N.6    Rastan, S.7
  • 32
    • 0026084955 scopus 로고
    • Human ubiquitin-activating enzyme (E1): Compensation for heat-labile mouse E1 and its gene localization on the X chromosome
    • Kudo, M., Sugasawa, K., Hori, T.-A., Enomoto, T., Hanaoka, F. and Ui, M. (1991) Human ubiquitin-activating enzyme (E1): compensation for heat-labile mouse E1 and its gene localization on the X chromosome. Exp. Cell Res. 192, 110-117.
    • (1991) Exp. Cell Res. , vol.192 , pp. 110-117
    • Kudo, M.1    Sugasawa, K.2    Hori, T.-A.3    Enomoto, T.4    Hanaoka, F.5    Ui, M.6
  • 33
    • 0023775756 scopus 로고
    • A Chinese hamster cell cycle mutant arrested at 63 phase has a temperature-sensitive ubiquitin-activating enzyme, E1
    • Kulka, R.G., Raboy, B., Schuster, R., Parag, H.A., Diamond, G., Ciechanover, A. and Marcus, M. (1988) A Chinese hamster cell cycle mutant arrested at 63 phase has a temperature-sensitive ubiquitin-activating enzyme, E1. J. Biol. Chem. 263, 15726-15731.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15726-15731
    • Kulka, R.G.1    Raboy, B.2    Schuster, R.3    Parag, H.A.4    Diamond, G.5    Ciechanover, A.6    Marcus, M.7
  • 34
    • 0028817813 scopus 로고
    • The gap junction protein connexin-43 is degraded via the ubiquitin proteasome pathway
    • Laing, J.G. and Beyer, E.C. (1995) The gap junction protein connexin-43 is degraded via the ubiquitin proteasome pathway. J. Biol. Chem. 270, 26399-26403.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26399-26403
    • Laing, J.G.1    Beyer, E.C.2
  • 35
    • 0027165626 scopus 로고
    • Arabidopsis auxin resistant gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1
    • Leyser, H.M.O., Lincoln, C.A., Timpte, C., Lammer, D., Turner, J. and Estelle, M. (1993) Arabidopsis auxin resistant gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1. Nature, 364, 161-164.
    • (1993) Nature , vol.364 , pp. 161-164
    • Leyser, H.M.O.1    Lincoln, C.A.2    Timpte, C.3    Lammer, D.4    Turner, J.5    Estelle, M.6
  • 36
    • 0025967290 scopus 로고
    • UBA1: An essential yeast gene encoding ubiquitin-activating enzyme E1
    • McGrath, J.P., Jentsch, S. and Varshavsky, A. (1991) UBA1: an essential yeast gene encoding ubiquitin-activating enzyme E1. EMBO J. 10, 227-236.
    • (1991) EMBO J. , vol.10 , pp. 227-236
    • McGrath, J.P.1    Jentsch, S.2    Varshavsky, A.3
  • 39
    • 0025790212 scopus 로고
    • Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1
    • Mitchell, M.J., Woods, D.R., Tucker, P.K., Opp, J.S. and Bishop, C.E. (1991) Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1. Nature. 354, 483-486.
    • (1991) Nature , vol.354 , pp. 483-486
    • Mitchell, M.J.1    Woods, D.R.2    Tucker, P.K.3    Opp, J.S.4    Bishop, C.E.5
  • 40
    • 0029047641 scopus 로고
    • Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase cdc2
    • Nagai, Y., Kaneda, S., Nomura, K., Yasuda, H. and Seno, T. (1995) Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase cdc2. J. Cell Sci. 108, 2145-2152.
    • (1995) J. Cell Sci. , vol.108 , pp. 2145-2152
    • Nagai, Y.1    Kaneda, S.2    Nomura, K.3    Yasuda, H.4    Seno, T.5
  • 41
    • 17544365083 scopus 로고    scopus 로고
    • The Arabidopsis thaliana UBC7/13/14 genes encode a family of multiubiquitin chain-forming E2 enzymes
    • van Nocker, S., Walker, J. and Vierstra, R.D. (1996) The Arabidopsis thaliana UBC7/13/14 genes 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.2    Vierstra, R.D.3
  • 42
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V.J., Rando, O.J., Goldberg, A.L. and Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell, 78, 77-785.
    • (1994) Cell , vol.78 , pp. 77-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 43
    • 0029360720 scopus 로고
    • Seeing double: Appreciating genetic redundancy
    • Pickett, F.B. and Meeks-Wagner, D.R. (1995) Seeing double: appreciating genetic redundancy. Plant Cell, 7, 1347-1356.
    • (1995) Plant Cell , vol.7 , pp. 1347-1356
    • Pickett, F.B.1    Meeks-Wagner, D.R.2
  • 44
    • 0000405306 scopus 로고
    • The structure and expression of maize genes encoding the major heat shock protein, hsp70
    • Rochester D.L., Winter, J.A. and Shah, D.M. (1986) The structure and expression of maize genes encoding the major heat shock protein, hsp70. EMBO J. 5, 451-458.
    • (1986) EMBO J. , vol.5 , pp. 451-458
    • Rochester, D.L.1    Winter, J.A.2    Shah, D.M.3
  • 45
    • 0001810352 scopus 로고
    • Extraction of DNA from plant tissues
    • Rogers, S.O. and Bendich, A.J. (1988) Extraction of DNA from plant tissues. Plant Mol. Biol. 6, 1-10.
    • (1988) Plant Mol. Biol. , vol.6 , pp. 1-10
    • Rogers, S.O.1    Bendich, A.J.2
  • 46
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in ubiquitination of p53
    • Scheffner, M., Huibregtse, J.M., Vierstra, R.D. and Howley, P.M. (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in ubiquitination of p53. Cell, 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 47
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M., Nuber, U. and Huibregtse, J.M. (1995) Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature, 363, 81-83.
    • (1995) Nature , vol.363 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 49
    • 0030055236 scopus 로고    scopus 로고
    • Localization of ubiquitin to differentiating vascular tissue
    • Stephenson, P., Collins, B.A., Reid, P.D. and Rubinstein, B. (1996) Localization of ubiquitin to differentiating vascular tissue. Am. J. Bot. 83, 140-147.
    • (1996) Am. J. Bot. , vol.83 , pp. 140-147
    • Stephenson, P.1    Collins, B.A.2    Reid, P.D.3    Rubinstein, B.4
  • 50
    • 0006418264 scopus 로고
    • HPLC resolution of ubiquitin pathway enzymes from wheat germ
    • Sullivan, M.L., Callis, J.A. and Vierstra, R.D. (1990) HPLC resolution of ubiquitin pathway enzymes from wheat germ. Plant Physiol. 94, 710-716.
    • (1990) Plant Physiol. , vol.94 , pp. 710-716
    • Sullivan, M.L.1    Callis, J.A.2    Vierstra, R.D.3
  • 51
    • 0028370795 scopus 로고
    • Wheat ubiquitin-conjugating enzymes, TaUBC1 and TaUBC4, are encoded by small multigene families in Arabidopsis thaliana
    • Sullivan, M.L., Carpenter, T.B. and Vierstra, R.D. (1994) Wheat ubiquitin-conjugating enzymes, TaUBC1 and TaUBC4, are encoded by small multigene families in Arabidopsis thaliana. Plant Mol. Biol. 24, 651-661.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 651-661
    • Sullivan, M.L.1    Carpenter, T.B.2    Vierstra, R.D.3
  • 52
    • 0028428501 scopus 로고
    • Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis
    • Thoma, S., Hecht, U., Kippers, A., Botella, J., De Vries, S. and Somerville, C. (1994) Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis. Plant Physiol. 105, 35-45.
    • (1994) Plant Physiol. , vol.105 , pp. 35-45
    • Thoma, S.1    Hecht, U.2    Kippers, A.3    Botella, J.4    De Vries, S.5    Somerville, C.6
  • 53
    • 0030175281 scopus 로고    scopus 로고
    • Members of two gene families encoding the ubiquitin-activating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed
    • Thoma, S., Sullivan, M.L. and Vierstra, R.D. (1996) Members of two gene families encoding the ubiquitin-activating enzymes, AtUBC1-3 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
  • 54
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain
    • Treier, M., Staszewski, L.M. and Bohmann, D. (1994) Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain. Cell, 78, 787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 57
    • 0001906410 scopus 로고
    • Phytochrome degradation
    • Kendrick, R.E Kronenberg, G.H.M., eds. Dordrecht, Netherlands: Martinus Nijhoff Publishers
    • Vierstra, R.D. (1994) Phytochrome degradation. In Photomorphogenesis in Plants, 2nd edn (Kendrick, R.E. and Kronenberg, G.H.M., eds). Dordrecht, Netherlands: Martinus Nijhoff Publishers, pp. 141-162.
    • (1994) Photomorphogenesis in Plants, 2nd Edn , pp. 141-162
    • Vierstra, R.D.1
  • 58
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S. and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 59
    • 0028519141 scopus 로고
    • Floral expression of a gene encoding an E2-related ubiquitin-conjugating protein from Arabidopsis thaliana
    • Watts, F.Z., Butt, N., Layfield, P., Machuka, J., Burke, J.F. and Moore, A.L (1994) Floral expression of a gene encoding an E2-related ubiquitin-conjugating protein from Arabidopsis thaliana. Plant Mol. Bid 26, 445-451.
    • (1994) Plant Mol. Bid , vol.26 , pp. 445-451
    • Watts, F.Z.1    Butt, N.2    Layfield, P.3    Machuka, J.4    Burke, J.F.5    Moore, A.L.6
  • 61
    • 0025371984 scopus 로고
    • The protein encoded by the Arabidopsis homeotic gene agamous resembles transcription factors
    • Yanofsky, M.F., Ma, H., Bowman, J.L., Drews, G.N., Feldman, K.A. and Meyerowitz, E.M. (1990) The protein encoded by the Arabidopsis homeotic gene agamous resembles transcription factors. Nature, 346, 35-39.
    • (1990) Nature , vol.346 , pp. 35-39
    • Yanofsky, M.F.1    Ma, H.2    Bowman, J.L.3    Drews, G.N.4    Feldman, K.A.5    Meyerowitz, E.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.