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Volumn 23, Issue 24, 2003, Pages 9251-9261

Ubiquitin Depletion as a Key Mediator of Toxicity by Translational Inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ANISOMYCIN; CYCLOHEXIMIDE; HYGROMYCIN B; UBIQUITIN;

EID: 0344629427     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.24.9251-9261.2003     Document Type: Article
Times cited : (179)

References (52)
  • 1
    • 0021040518 scopus 로고
    • Effect of protein synthesis inhibitors on the fidelity of translation in eukaryotic systems
    • Abraham, A. K., and A. Pihl. 1983. Effect of protein synthesis inhibitors on the fidelity of translation in eukaryotic systems. Biochim. Biophys. Acta 741:197-203.
    • (1983) Biochim. Biophys. Acta , vol.741 , pp. 197-203
    • Abraham, A.K.1    Pihl, A.2
  • 3
    • 0031961688 scopus 로고    scopus 로고
    • Regulation of translational initiation during cellular responses to stress
    • Brostrom, C. O., and M. A. Brostrom. 1998. Regulation of translational initiation during cellular responses to stress. Prog. Nucleic Acid Res. Mol. Biol. 58:79-125.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.58 , pp. 79-125
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 4
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans
    • Burbea, M., L. Dreier, J. S. Dittman, M. E. Grunwald, and J. Kaplan. 2002. Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans. Neuron 35:107-120.
    • (2002) Neuron , vol.35 , pp. 107-120
    • Burbea, M.1    Dreier, L.2    Dittman, J.S.3    Grunwald, M.E.4    Kaplan, J.5
  • 5
    • 0029023915 scopus 로고
    • Consequences of overexpression of ubiquitin in yeast: Elevated tolerances of osmostress, ethanol and canavanine, yet reduced tolerances of cadmium, arsenite and paromomycin
    • Chen, Y., and P. W. Piper. 1995. Consequences of overexpression of ubiquitin in yeast: elevated tolerances of osmostress, ethanol and canavanine, yet reduced tolerances of cadmium, arsenite and paromomycin. Biochim. Biophys. Acta 1268:59-64.
    • (1995) Biochim. Biophys. Acta , vol.1268 , pp. 59-64
    • Chen, Y.1    Piper, P.W.2
  • 6
    • 0031655755 scopus 로고    scopus 로고
    • Yeast gene YRR1, which is required for resistance to 4-nitroquinoline N-oxide, mediates transcriptional activation of the multidrug resistance transporter gene SNQ2
    • Cui, Z., T. Shiraki, D. Hirata, and T. Miyakawa. 1998. Yeast gene YRR1, which is required for resistance to 4-nitroquinoline N-oxide, mediates transcriptional activation of the multidrug resistance transporter gene SNQ2. Mol. Microbiol. 29:1307-1315.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1307-1315
    • Cui, Z.1    Shiraki, T.2    Hirata, D.3    Miyakawa, T.4
  • 7
    • 0023654338 scopus 로고
    • Chemical synthesis and expression of a cassette adapted ubiquitin gene
    • Ecker, D. J., M. I. Khan, J. Marsh, T. R. Butt, and S. T. Cooke. 1987. Chemical synthesis and expression of a cassette adapted ubiquitin gene. J. Biol. Chem. 262:3524-3527.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3524-3527
    • Ecker, D.J.1    Khan, M.I.2    Marsh, J.3    Butt, T.R.4    Cooke, S.T.5
  • 8
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. 2003. Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 6:231-242.
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 9
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., B. Bartel, and A. Varshavsky. 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
  • 10
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley, D., E. Ozkaynak, and A. Varshavsky. 1987. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48:1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozkaynak, E.2    Varshavsky, A.3
  • 11
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J.-M., and R. Haguenauer-Tsapis. 1997. Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16:5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.-M.1    Haguenauer-Tsapis, R.2
  • 12
    • 1842405431 scopus 로고    scopus 로고
    • Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation
    • Gerlinger, U. M., R. Guckel, M. Hoffmann, D. H. Wolf, and W. Hilt. 1997. Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation. Mol. Biol. Cell 8:2487-2489.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2487-2489
    • Gerlinger, U.M.1    Guckel, R.2    Hoffmann, M.3    Wolf, D.H.4    Hilt, W.5
  • 13
    • 0023115331 scopus 로고
    • The dynamics of ubiquitin pools within cultured human lung fibroblasts
    • Haas, A. L., and P. M. Bright. 1987. The dynamics of ubiquitin pools within cultured human lung fibroblasts. J. Biol. Chem. 262:345-351.
    • (1987) J. Biol. Chem. , vol.262 , pp. 345-351
    • Haas, A.L.1    Bright, P.M.2
  • 15
    • 0026637019 scopus 로고
    • Ubiquitin metabolism in HeLa cells starved of amino acids
    • Hiroi, Y., and M. Rechsteiner. 1992. Ubiquitin metabolism in HeLa cells starved of amino acids. J. Biol. Chem. 307:156-161.
    • (1992) J. Biol. Chem. , vol.307 , pp. 156-161
    • Hiroi, Y.1    Rechsteiner, M.2
  • 16
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch, S. 1992. The ubiquitin-conjugation system. Annu. Rev. Genet. 26: 179-207.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 17
    • 0027181247 scopus 로고
    • Immunohistochemical localization of ubiquitin in gerbil hippocampus with induced tolerance to ischemia
    • Kato, H., T. Chen, X. H. Liu, N. Nakata, and K. Kogure. 1993. Immunohistochemical localization of ubiquitin in gerbil hippocampus with induced tolerance to ischemia. Brain Res. 619:339-343.
    • (1993) Brain Res. , vol.619 , pp. 339-343
    • Kato, H.1    Chen, T.2    Liu, X.H.3    Nakata, N.4    Kogure, K.5
  • 18
    • 0036938488 scopus 로고    scopus 로고
    • PDR2 gain-of-function mutations eliminate the need for Pdr1 and require the UBP6 product for resistance to translational inhibitors
    • Keeven, J., D. Ko, J. Shallom, B. Uccelini, and J. Golin. 2002. PDR2 gain-of-function mutations eliminate the need for Pdr1 and require the UBP6 product for resistance to translational inhibitors. Curr. Genet. 41:11-19.
    • (2002) Curr. Genet. , vol.41 , pp. 11-19
    • Keeven, J.1    Ko, D.2    Shallom, J.3    Uccelini, B.4    Golin, J.5
  • 19
    • 0030904329 scopus 로고    scopus 로고
    • Movement of the 3′-end of tRNA through the peptidyl transferase center and its inhibition by antibiotics
    • Kirillov, S., B. T. Porse, B. Vester, P. Wooley, and R. A. Garrett. 1997. Movement of the 3′-end of tRNA through the peptidyl transferase center and its inhibition by antibiotics. FEBS Lett. 406:223-233.
    • (1997) FEBS Lett. , vol.406 , pp. 223-233
    • Kirillov, S.1    Porse, B.T.2    Vester, B.3    Wooley, P.4    Garrett, R.A.5
  • 21
    • 0024024371 scopus 로고
    • Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae
    • McCusker, J. H., and J. E. Haber. 1988. Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae. Genetics 119: 303-315.
    • (1988) Genetics , vol.119 , pp. 303-315
    • McCusker, J.H.1    Haber, J.E.2
  • 22
    • 0024024729 scopus 로고
    • Crl mutants of Saccharomyces cerevisiae resemble both mutants affecting general control of amino acid biosynthesis and omnipotent translational suppressor mutants
    • McCusker, J. H., and J. E. Haber. 1988b. Crl mutants of Saccharomyces cerevisiae resemble both mutants affecting general control of amino acid biosynthesis and omnipotent translational suppressor mutants. Genetics 119: 317-327.
    • (1988) Genetics , vol.119 , pp. 317-327
    • McCusker, J.H.1    Haber, J.E.2
  • 23
    • 0342871691 scopus 로고    scopus 로고
    • Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, and the cellular stress response
    • Mimnaugh, E. G., H. Y. Chen, J. R. Davie, J. E. Celis, and L. Neckers. 1997. Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: effects on replication, transcription, and the cellular stress response. Biochemistry 36: 14418-14429.
    • (1997) Biochemistry , vol.36 , pp. 14418-14429
    • Mimnaugh, E.G.1    Chen, H.Y.2    Davie, J.R.3    Celis, J.E.4    Neckers, L.5
  • 24
    • 0036942162 scopus 로고    scopus 로고
    • Alterations of ubiquitin immunoreactivity in the hippocampal formation after perforant pathway lesion
    • Mizukami, K., M. Ishikawa, M. Iwakiri, S. Hidaka, N. Kato, and T. Asada. 2002. Alterations of ubiquitin immunoreactivity in the hippocampal formation after perforant pathway lesion. Acta Neuropathol. 103:453-457.
    • (2002) Acta Neuropathol. , vol.103 , pp. 453-457
    • Mizukami, K.1    Ishikawa, M.2    Iwakiri, M.3    Hidaka, S.4    Kato, N.5    Asada, T.6
  • 25
    • 0024015468 scopus 로고
    • Ubiquitin gene expression in Dictystelium is induced by heat and cold shock, cadmium, and inhibitors of protein synthesis
    • Müller-Taubenberger, A., J. Hagmann, A. Noegel, and G. Gerisch. 1988. Ubiquitin gene expression in Dictystelium is induced by heat and cold shock, cadmium, and inhibitors of protein synthesis. J. Cell Sci. 90:51-58.
    • (1988) J. Cell Sci. , vol.90 , pp. 51-58
    • Müller-Taubenberger, A.1    Hagmann, J.2    Noegel, A.3    Gerisch, G.4
  • 26
    • 0037179795 scopus 로고    scopus 로고
    • New roles for ubiquitin in the assembly and function of neuronal circuits
    • Murphey, R. K., and T. A. Godenschwege. 2002. New roles for ubiquitin in the assembly and function of neuronal circuits. Neuron 36:5-8.
    • (2002) Neuron , vol.36 , pp. 5-8
    • Murphey, R.K.1    Godenschwege, T.A.2
  • 28
    • 0033974801 scopus 로고    scopus 로고
    • Molecular characterization of ubiquitin genes from Aspergillus nidulans: mRNA expression on different stress and growth conditions
    • Noventa-Jordao, M. A., A. M. do Nacimento, M. H. S. Goldman, H. F. Terenzi, and G. H. Goldman. 2000. Molecular characterization of ubiquitin genes from Aspergillus nidulans: mRNA expression on different stress and growth conditions. Biochim. Biophys. Acta 1490:237-244.
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 237-244
    • Noventa-Jordao, M.A.1    Do Nacimento, A.M.2    Goldman, M.H.S.3    Terenzi, H.F.4    Goldman, G.H.5
  • 29
    • 0015216932 scopus 로고
    • The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes
    • Obrig, T. G., W. J. Culp, W. L. McKeehan, and B. Hardesty. 1971. The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes. J. Biol. Chem. 246:174-181.
    • (1971) J. Biol. Chem. , vol.246 , pp. 174-181
    • Obrig, T.G.1    Culp, W.J.2    McKeehan, W.L.3    Hardesty, B.4
  • 31
    • 0021679940 scopus 로고
    • The yeast ubiquitin gene: Head-to-tail repeats encoding a polyubiquitin precursor protein
    • Özkaynak, E., D. Finley, and A. Varshavsky. 1984. The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein. Nature 312: 663-666.
    • (1984) Nature , vol.312 , pp. 663-666
    • Özkaynak, E.1    Finley, D.2    Varshavsky, A.3
  • 32
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik, A., V. Chau, and J. W. Wills. 2000. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. USA 97:13069-13074.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 33
    • 0024227435 scopus 로고
    • Membrane potential defect in hygromycin B-resistant pma1 mutants of Saccharomyces cerevisiae
    • Perlin, D. S., C. L. Brown, and J. E. Haber. 1988. Membrane potential defect in hygromycin B-resistant pma1 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 34:18118-18122.
    • (1988) J. Biol. Chem. , vol.34 , pp. 18118-18122
    • Perlin, D.S.1    Brown, C.L.2    Haber, J.E.3
  • 34
    • 0014207856 scopus 로고
    • Cycloheximide resistance in yeast: A property of the 60S ribosomal subunit
    • Rao, S. S., and A. P. Grollman. 1967. Cycloheximide resistance in yeast: a property of the 60S ribosomal subunit. Biochem. Biophys. Res. Commun. 29:696-704.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 696-704
    • Rao, S.S.1    Grollman, A.P.2
  • 35
    • 0023192490 scopus 로고
    • A specific endpoint assay for ubiquitin
    • Rose, I. A., and J. V. B. Warms. 1987. A specific endpoint assay for ubiquitin. Proc. Natl. Acad. Sci. USA 84:1477-1481.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1477-1481
    • Rose, I.A.1    Warms, J.V.B.2
  • 37
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin, D. M., M. H. Glickman, C. N. Larsen, S. Dhruvakumar, and D. Finley. 1998. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17:4909-4919.
    • (1998) EMBO J. , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 38
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly-synthesized proteins by proteasomes
    • Schubert, U., L. C. Anton, J. Gibbs, C. C. Norbury, J. W. Yewdell, and J. R. Bennink. 2000. Rapid degradation of a large fraction of newly-synthesized proteins by proteasomes. Nature 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 39
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert, W., and S. Jentsch. 1990. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9:543-550.
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 40
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y., and A. L. Goldberg. 2001. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 41
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., S. Sadis, A. L. Haas, and D. Finley. 1995. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15:1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 42
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence, J., R. R. Gall, G. Dittmar, F. Sherman, and D. Finley. 2000. Cell cycle regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102:67-76.
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gall, R.R.2    Dittmar, G.3    Sherman, F.4    Finley, D.5
  • 43
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • Swaminathan, S., A. Y. Amerik, and M. Hochstrasser. 1999. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10:2583-2594.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 44
    • 0033949431 scopus 로고    scopus 로고
    • p53 accumulation due to down-regulation of ubiquitin: Relevance for neuronal apoptosis
    • Tan, Z., W. Tu, W. Liu, M. Baudry, and S. S. Scheiber. 2000. p53 accumulation due to down-regulation of ubiquitin: relevance for neuronal apoptosis. Cell Death Differ. 7:675-681.
    • (2000) Cell Death Differ. , vol.7 , pp. 675-681
    • Tan, Z.1    Tu, W.2    Liu, W.3    Baudry, M.4    Scheiber, S.S.5
  • 45
    • 0035854477 scopus 로고    scopus 로고
    • Downregulation of free ubiquitin: A novel mechanism of p53 stabilization and neuronal cell death
    • Tan, Z., W. Tu, and S. S. Scheiber. 2001. Downregulation of free ubiquitin: a novel mechanism of p53 stabilization and neuronal cell death. Mol. Brain Res. 91:179-188.
    • (2001) Mol. Brain Res. , vol.91 , pp. 179-188
    • Tan, Z.1    Tu, W.2    Scheiber, S.S.3
  • 46
    • 0023959560 scopus 로고
    • Dual regulation of the polyubiquitin gene by cyclic AMP and heat shock in yeast
    • Tanaka, K., K. Matsumoto, and A. Toh-e. 1988. Dual regulation of the polyubiquitin gene by cyclic AMP and heat shock in yeast. EMBO J. 7:495-502.
    • (1988) EMBO J. , vol.7 , pp. 495-502
    • Tanaka, K.1    Matsumoto, K.2    Toh-E, A.3
  • 47
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma, R., S. Chen, R. Feldman, D. Schieltz, J. Yates, J. Dohmen, and R. J. Deshaies. 2000. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11:3425-3439.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 48
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., R. Oania, W. H. McDonald, J. R. Yates III, E. V. Koonin, and R. J. Deshaies. 2002. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298:611-615.
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Oania, R.2    McDonald, W.H.3    Yates III, J.R.4    Koonin, E.V.5    Deshaies, R.J.6
  • 49
    • 0343227056 scopus 로고
    • Effect of cycloheximide on ribosomal aggregates engaged in protein synthesis in vitro
    • Wettstein, F. O., H. Noll, and S. Penman. 1964. Effect of cycloheximide on ribosomal aggregates engaged in protein synthesis in vitro. Biochim. Biophys. Acta 87:525-527.
    • (1964) Biochim. Biophys. Acta , vol.87 , pp. 525-527
    • Wettstein, F.O.1    Noll, H.2    Penman, S.3
  • 50
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. 2000. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell Dev. Biol. 11:141-148.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 52
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and R. E. Cohen. 2002. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419:403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2


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