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Volumn 21, Issue 8, 2003, Pages 897-902

A transgenic mouse model of the ubiquitin/proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; NEUROLOGY; PATHOLOGY; PROTEINS;

EID: 0043208904     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt851     Document Type: Article
Times cited : (203)

References (47)
  • 1
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M.Y. & Goldberg, A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001).
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 2
    • 0035895604 scopus 로고    scopus 로고
    • Regulation of the G 1 to S transition by the ubiquitin pathway
    • DeSalle, L.M. & Pagano, M. Regulation of the G1 to S transition by the ubiquitin pathway. FEBS Lett. 490, 179-189 (2001).
    • (2001) FEBS Lett. , vol.490 , pp. 179-189
    • DeSalle, L.M.1    Pagano, M.2
  • 3
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin, M. & Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663 (2000).
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380 (1998).
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 6
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M. & Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001).
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 7
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA 1
    • Cummings, C.J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154 (1998).
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1
  • 8
    • 0034730172 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
    • Lam, Y.A. et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 97, 9902-9906 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9902-9906
    • Lam, Y.A.1
  • 9
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten, K. et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157, 417-427 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1
  • 11
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R.W. & Lomas, D.A. Conformational disease. Lancet 350, 134-138 (1997).
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 12
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski, P.J. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 35, 9-12 (2002).
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 13
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto, C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498, 204-207 (2001).
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 14
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef, L.G., Lindsten, K., Masucci, M.G. & Dantuma, N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11, 2689-2700 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 15
    • 0033396283 scopus 로고    scopus 로고
    • Intranuclear inclusions and the ubiquitin-proteasome pathway: Digestion of a red herring?
    • Floyd, J.A. & Hamilton, B.A. Intranuclear inclusions and the ubiquitin-proteasome pathway: digestion of a red herring? Neuron 24, 765-766 (1999).
    • (1999) Neuron , vol.24 , pp. 765-766
    • Floyd, J.A.1    Hamilton, B.A.2
  • 16
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. & Greenberg, M.E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66 (1998).
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 17
    • 18444386197 scopus 로고    scopus 로고
    • A long CAG repeat in the mouse Scal locus replicates SCA 1 features and reveals the impact of protein solubility on selective neurodegeneration
    • Watase, K. et al. A long CAG repeat in the mouse Scal locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron 34, 905-919 (2002).
    • (2002) Neuron , vol.34 , pp. 905-919
    • Watase, K.1
  • 18
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • Ryan, K.M., Phillips, A.C. & Vousden, K.H. Regulation and function of the p53 tumor suppressor protein. Curr. Opin. Cell. Biol. 13, 332-337 (2001).
    • (2001) Curr. Opin. Cell. Biol. , vol.13 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 19
    • 0034092911 scopus 로고    scopus 로고
    • Regulation of the cdk Inhibitor p27 and its deregulation in cancer
    • Slingerland, J. & Pagano, M. Regulation of the cdk Inhibitor p27 and its deregulation in cancer. J. Cell Physiol. 183, 10-17 (2000).
    • (2000) J. Cell Physiol. , vol.183 , pp. 10-17
    • Slingerland, J.1    Pagano, M.2
  • 20
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96, 10403-10408 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1
  • 21
    • 0033564512 scopus 로고    scopus 로고
    • Eponemycin exerts its antitumor effect through the inhibition of proteasome function
    • Meng, L., Kwok, B.H., Sin, N. & Crews, C.M. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 59, 2798-2801 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 2798-2801
    • Meng, L.1    Kwok, B.H.2    Sin, N.3    Crews, C.M.4
  • 22
    • 0036023407 scopus 로고    scopus 로고
    • A phase I trial of the novel proteasome inhibitor PS 341 in advanced solid tumor malignancies. Clin
    • Aghajanian, C. et al. A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin. Cancer Res. 8, 2505-2511 (2002).
    • (2002) Cancer Res. , vol.8 , pp. 2505-2511
    • Aghajanian, C.1
  • 23
    • 0037093067 scopus 로고    scopus 로고
    • Antitumorigenic effects of HIV protease inhibitor ritonavir: Inhibition of Kaposi sarcoma
    • Pati, S. et al. Antitumorigenic effects of HIV protease inhibitor ritonavir: inhibition of Kaposi sarcoma. Blood 99, 3771-3779 (2002).
    • (2002) Blood , vol.99 , pp. 3771-3779
    • Pati, S.1
  • 24
    • 0036131462 scopus 로고    scopus 로고
    • HIV protease inhibitors are potent anti-angiogenic molecules and promote regression of Kaposi sarcoma
    • Sgadari, C. et al. HIV protease inhibitors are potent anti-angiogenic molecules and promote regression of Kaposi sarcoma. Nat. Med. 8, 225-232 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 225-232
    • Sgadari, C.1
  • 25
    • 0035975264 scopus 로고    scopus 로고
    • Protection against experimental autoimmune encephalomyelitis by a proteasome modulator
    • Hosseini, H. et al. Protection against experimental autoimmune encephalomyelitis by a proteasome modulator. J. Neurobiol. 118, 233-244 (2001).
    • (2001) J. Neurobiol. , vol.118 , pp. 233-244
    • Hosseini, H.1
  • 26
    • 0036198493 scopus 로고    scopus 로고
    • Proteasome inhibition reduces superantigen-mediated T cell activation and the severity of psoriasis in a SCID-hu model
    • Zollner, T.M. et al. Proteasome inhibition reduces superantigen-mediated T cell activation and the severity of psoriasis in a SCID-hu model. J. Clin. Invest. 109, 671-679 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 671-679
    • Zollner, T.M.1
  • 27
    • 0034902852 scopus 로고    scopus 로고
    • A proteasome inhibitor effectively prevents mouse heart allograft rejection
    • Luo, H. et al. A proteasome inhibitor effectively prevents mouse heart allograft rejection. Transplantation 72, 196-202 (2001).
    • (2001) Transplantation , vol.72 , pp. 196-202
    • Luo, H.1
  • 28
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K.L. & Goldberg, A.L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779 (1999).
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 29
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Huntington's disease
    • Rubinsztein, D.C. Lessons from animal models of Huntington's disease. Trends Genet. 18, 202-209 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 30
    • 0036303818 scopus 로고    scopus 로고
    • Genetically engineered mouse models of neurode generative diseases
    • Wong, P.C., Cai, H., Borchelt, D.R. & Price, D.L. Genetically engineered mouse models of neurodegenerative diseases. Nat. Neurosci. 5, 633-639 (2002).
    • (2002) Nat. Neurosci. , vol.5 , pp. 633-639
    • Wong, P.C.1    Cai, H.2    Borchelt, D.R.3    Price, D.L.4
  • 31
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M. & Masucci, M.G. Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 18, 538-543 (2000).
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 32
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C., Ota, I.M. & Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 34
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J. et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135 (1995).
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1
  • 35
    • 0030671540 scopus 로고    scopus 로고
    • Active site-directed inhibitors of Rhodococcus 20 S proteasome. Kinetics and mechanism
    • McCormack, T. et al. Active site-directed inhibitors of Rhodococcus 20 S proteasome. Kinetics and mechanism. J. Biol. Chem. 272, 26103-26109 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26103-26109
    • McCormack, T.1
  • 36
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HSIV by a new class of inhibitors
    • Bogyo, M. et al. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HSIV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94, 6629-6634 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1
  • 37
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev, A.F. & Goldberg, A.L. Proteasome inhibitors: from research tools to drug candidates. Chem. Biol. 8, 739-758 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 38
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • Myung, J., Kim, K.B., Lindsten, K., Dantuma, N.P. & Crews, C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7, 411-420 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 39
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of β-amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen, F.W. et al. Frameshift mutants of β-amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279, 242-247 (1998).
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1
  • 40
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • Perutz, M.F. & Windle, A.H. Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature 412, 143-144 (2001).
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 41
    • 0032475877 scopus 로고    scopus 로고
    • Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial?
    • Sisodia, S.S. Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? Cell 95, 1-4 (1998).
    • (1998) Cell , vol.95 , pp. 1-4
    • Sisodia, S.S.1
  • 42
    • 0141650794 scopus 로고    scopus 로고
    • Monitoring the ubiquitin/proteasome system in conformational diseases
    • in the press
    • Lindsten, K. & Dantuma, N.P. Monitoring the ubiquitin/proteasome system in conformational diseases. Ageing Res. Rev. in the press.
    • Ageing Res. Rev.
    • Lindsten, K.1    Dantuma, N.P.2
  • 43
    • 0035680611 scopus 로고    scopus 로고
    • Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin
    • French, B.A. et al. Aggresome formation in liver cells in response to different toxic mechanisms: role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol. 71, 241-246 (2001).
    • (2001) Exp. Mol. Pathol. , vol.71 , pp. 241-246
    • French, B.A.1
  • 45
    • 0034039137 scopus 로고    scopus 로고
    • Proteasome activation as a critical event of thymocyte apoptosis
    • Dallaporta, B. et al. Proteasome activation as a critical event of thymocyte apoptosis. Cell Death Differ. 7, 368-373 (2000).
    • (2000) Cell Death Differ. , vol.7 , pp. 368-373
    • Dallaporta, B.1
  • 46
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang, Y., Fang, S., Jensen, J.P., Weissman, A.M. & Ashwell, J.D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874-877 (2000).
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 47
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L. et al. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272, 263-267 (1996).
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1


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