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Volumn 17, Issue 14, 2008, Pages 2108-2117

Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE INHIBITOR; MUTANT PROTEIN; PHOSPHOTRANSFERASE INHIBITOR; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN INHIBITOR; RESVERATROL; SIRTINOL; SIRTUIN; SIRTUIN 2 INHIBITOR; TRANSCRIPTION FACTOR DAF 16; TRANSCRIPTION FACTOR FOXO;

EID: 46249124837     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddn109     Document Type: Article
Times cited : (57)

References (54)
  • 1
    • 0344099622 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystropby: A late-onset polyalanine disease
    • Brais, B. (2003) Oculopharyngeal muscular dystropby: A late-onset polyalanine disease. Cytogenet.Genome Res., 100, 252-260.
    • (2003) Cytogenet.Genome Res , vol.100 , pp. 252-260
    • Brais, B.1
  • 2
    • 17344371397 scopus 로고    scopus 로고
    • Brais, B., Bouchard, J.P., Xie, Y.G., Rochefort, D.L., Chretion, N., Tome, F.M., Lafreniere, R.G., Rommens, J.M., Uyama, E., Nohira, O. et al. (1998) Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. [Erratum (1998) Nat Genet, 19, 404.] Nat. Genet., 18, 164-167.
    • Brais, B., Bouchard, J.P., Xie, Y.G., Rochefort, D.L., Chretion, N., Tome, F.M., Lafreniere, R.G., Rommens, J.M., Uyama, E., Nohira, O. et al. (1998) Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. [Erratum (1998) Nat Genet, 19, 404.] Nat. Genet., 18, 164-167.
  • 3
    • 0034737319 scopus 로고    scopus 로고
    • The nuclear poly(A) binding protein; PABP2, forms an oligomeric particle covering the length of the poly(A) tail
    • Keller, R.W., Kuhn, U.,Aragon, M., Bornikova, L., Wahle, E. and Bear, D.G. (2000) The nuclear poly(A) binding protein; PABP2, forms an oligomeric particle covering the length of the poly(A) tail. J Mol Biol. 297, 569-583.
    • (2000) J Mol Biol , vol.297 , pp. 569-583
    • Keller, R.W.1    Kuhn, U.2    Aragon, M.3    Bornikova, L.4    Wahle, E.5    Bear, D.G.6
  • 4
    • 0033951076 scopus 로고    scopus 로고
    • Deciphering the cellular pathway for transport of poly(A)-binding protein II
    • Calado, A., Kutay, U., Kuhn, U., Wahle, E. and Carmo-Fonseca, M. (2000) Deciphering the cellular pathway for transport of poly(A)-binding protein II. Rna, 6, 245-256.
    • (2000) Rna , vol.6 , pp. 245-256
    • Calado, A.1    Kutay, U.2    Kuhn, U.3    Wahle, E.4    Carmo-Fonseca, M.5
  • 5
    • 0035873278 scopus 로고    scopus 로고
    • The product of an oculopharyngeal muscular dystrophy gene, poly(A)- binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression
    • Kim, Y.J., Noguchi, S., Hayashi, Y.K., Tsukahara, T., Shimizu, T. and Arahata, K. (2001) The product of an oculopharyngeal muscular dystrophy gene, poly(A)- binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Hum. Mol. Genet., 10, 1129-1139.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1129-1139
    • Kim, Y.J.1    Noguchi, S.2    Hayashi, Y.K.3    Tsukahara, T.4    Shimizu, T.5    Arahata, K.6
  • 6
    • 0033764563 scopus 로고    scopus 로고
    • Intranuclear inclusions in oculopharyngeal muscular dystrophy contain poly(A) binding protein 2
    • Becher, M.W., Kotzuk, J.A., Davis, L.E. and Bear, D.G. (2000) Intranuclear inclusions in oculopharyngeal muscular dystrophy contain poly(A) binding protein 2. Ann. Neurol., 48, 812-815.
    • (2000) Ann. Neurol , vol.48 , pp. 812-815
    • Becher, M.W.1    Kotzuk, J.A.2    Davis, L.E.3    Bear, D.G.4
  • 8
    • 0037023781 scopus 로고    scopus 로고
    • Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy
    • Bao, Y.P., Cook, L.J., O'Donovan, D., Uyama, E. and Rubinsztein, D.C. (2002) Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. J. Biol. Chem., 277, 12263-12269.
    • (2002) J. Biol. Chem , vol.277 , pp. 12263-12269
    • Bao, Y.P.1    Cook, L.J.2    O'Donovan, D.3    Uyama, E.4    Rubinsztein, D.C.5
  • 9
    • 0142185364 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome pathway and molecular chaperones oculopharyngeal muscular dystrophy
    • Abu-Baker, A., Messaed, C., Laganiere, J., Gaspar, C., Brais, B. and Rouleau, G.A. (2003) Involvement of the ubiquitin-proteasome pathway and molecular chaperones oculopharyngeal muscular dystrophy. Hum. Mol. Genet., 12, 2609-2623.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 2609-2623
    • Abu-Baker, A.1    Messaed, C.2    Laganiere, J.3    Gaspar, C.4    Brais, B.5    Rouleau, G.A.6
  • 10
    • 1942485876 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus
    • Berciano, M.T., Villagra, N.T., Ojeda, J.L., Navascues, J., Gomes, A., Lafarga, M. and Carmo-Fonseca, M. (2004) Oculopharyngeal muscular dystrophy-like nuclear inclusions are present in normal magnocellular neurosecretory neurons of the hypothalamus. Hum. Mol. Genet., 13, 829-838.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 829-838
    • Berciano, M.T.1    Villagra, N.T.2    Ojeda, J.L.3    Navascues, J.4    Gomes, A.5    Lafarga, M.6    Carmo-Fonseca, M.7
  • 11
    • 17844369724 scopus 로고    scopus 로고
    • In Vivo aggregation properties of the nuclear poly(A)-binding protein PABPN1
    • Tavanez, J.P., Calado, P., Braga, J., Lafarga, M. and Carmo-Fonseca, M. (2005) In Vivo aggregation properties of the nuclear poly(A)-binding protein PABPN1. Rna, 11, 752-762.
    • (2005) Rna , vol.11 , pp. 752-762
    • Tavanez, J.P.1    Calado, P.2    Braga, J.3    Lafarga, M.4    Carmo-Fonseca, M.5
  • 12
    • 34248995490 scopus 로고    scopus 로고
    • Messaed, C., Dion, P., Abu-Baker, A., Rochefort, D., Laganiere, J., Brais, B. and rouleau, G.A. Q007 Soluble expanded PABPN1 promotes cell death in Oculopharyngeal muscular dystrophy. Neurobiol. Dis., 26, 546-557.
    • Messaed, C., Dion, P., Abu-Baker, A., Rochefort, D., Laganiere, J., Brais, B. and rouleau, G.A. Q007) Soluble expanded PABPN1 promotes cell death in Oculopharyngeal muscular dystrophy. Neurobiol. Dis., 26, 546-557.
  • 13
    • 0034703413 scopus 로고    scopus 로고
    • Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA
    • Calado, A., Tome, F.M., Brais, B., Rouleau, G.A., Kuhn, U., Wahle, E. and Carmo-Fonseca, M. (2000) Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum. Mol. Genet., 9, 2321-2328.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2321-2328
    • Calado, A.1    Tome, F.M.2    Brais, B.3    Rouleau, G.A.4    Kuhn, U.5    Wahle, E.6    Carmo-Fonseca, M.7
  • 14
    • 20044363444 scopus 로고    scopus 로고
    • Corbeil-Girard, L.P., Klein, A.F., Sasseville, A.M., Lavoie, H., Dicaire, M.J., Saint-Denis, A., Page, M., Duranceau, A., Codere. F., Bouchard, J.P. et al. (2005) PABPN1 overexpression leads to upregulation of genes encoding nuclear proteins that are sequestered in oculopharyngeal muscular dystrophy nuclear inclusions. Neurobiol. Dis., 18, 551-567.
    • Corbeil-Girard, L.P., Klein, A.F., Sasseville, A.M., Lavoie, H., Dicaire, M.J., Saint-Denis, A., Page, M., Duranceau, A., Codere. F., Bouchard, J.P. et al. (2005) PABPN1 overexpression leads to upregulation of genes encoding nuclear proteins that are sequestered in oculopharyngeal muscular dystrophy nuclear inclusions. Neurobiol. Dis., 18, 551-567.
  • 15
    • 33846440511 scopus 로고    scopus 로고
    • Oculopharyngeal muscular dystrophy: Recent advances in the understanding of the molecular pathogenic mechanisms and treatment strategies
    • Abu-Baker, A. and Rouleau, G.A. (2007) Oculopharyngeal muscular dystrophy: Recent advances in the understanding of the molecular pathogenic mechanisms and treatment strategies. Biochim. Biophys. Acta, 1772, 173-185.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 173-185
    • Abu-Baker, A.1    Rouleau, G.A.2
  • 17
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent beta amyloid toxicity through inhibiting NF-kappa B signaling
    • Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.F., Kwon, H., Yi, S., Mucke, L. and Gan, L. (2005) SIRT1 protects against microglia-dependent beta amyloid toxicity through inhibiting NF-kappa B signaling. J. Biol. Chem., 280, 40364-40374.
    • (2005) J. Biol. Chem , vol.280 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6    Mucke, L.7    Gan, L.8
  • 18
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen, E., Bieschke, J., Perciavalle, R.M., Kelly, J.W. and Dillin, A. (2006) Opposing activities protect against age-onset proteotoxicity. Science, 313, 1604-1610.
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 20
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D.C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 23
    • 34249846128 scopus 로고    scopus 로고
    • Resveratrol stimulates AMP kinase activity in neurons
    • Dasgupta, B. and Milbrandt, J. (2007) Resveratrol stimulates AMP kinase activity in neurons. Proc. Natl. Acad. Sci. USA, 104, 7217-7222.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7217-7222
    • Dasgupta, B.1    Milbrandt, J.2
  • 24
    • 0027451263 scopus 로고
    • Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans
    • Okkema, P.G., Harrison, S.W., Plunger, V., Aryana, A. and Fire, A. (1993) Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans. Genetics, 135, 385-404.
    • (1993) Genetics , vol.135 , pp. 385-404
    • Okkema, P.G.1    Harrison, S.W.2    Plunger, V.3    Aryana, A.4    Fire, A.5
  • 25
    • 0033406058 scopus 로고    scopus 로고
    • Mutations in the dystrophin-like dys-1 gene of Caenorhabditis elegans result in reduced acetylcholinesterase activity
    • Giugia, J., Gieseler, K., Arpagaus, M. and Segalat, L. (1999) Mutations in the dystrophin-like dys-1 gene of Caenorhabditis elegans result in reduced acetylcholinesterase activity. FEBS Lett., 463, 270-272.
    • (1999) FEBS Lett , vol.463 , pp. 270-272
    • Giugia, J.1    Gieseler, K.2    Arpagaus, M.3    Segalat, L.4
  • 27
    • 0033920386 scopus 로고    scopus 로고
    • A role for SKIP in EBNA2 activation of CBF1-repressed promoters
    • Zhou, S., Fujimuro, M., Hsieh, J.J., Chen, L. and Hayward, S.D. (2000) A role for SKIP in EBNA2 activation of CBF1-repressed promoters. J. Virol., 74, 1939-1947.
    • (2000) J. Virol , vol.74 , pp. 1939-1947
    • Zhou, S.1    Fujimuro, M.2    Hsieh, J.J.3    Chen, L.4    Hayward, S.D.5
  • 29
    • 33745686137 scopus 로고    scopus 로고
    • The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells
    • Riessland, M., Brichta, L., Hahnen, E., and Wirth, B. (2006) The benzamide M344, a novel histone deacetylase inhibitor, significantly increases SMN2 RNA/protein levels in spinal muscular atrophy cells. Hum. Genet., 120, 101-110.
    • (2006) Hum. Genet , vol.120 , pp. 101-110
    • Riessland, M.1    Brichta, L.2    Hahnen, E.3    Wirth, B.4
  • 30
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo, V.D. and Kennedy, B.K. (2006) Sirtuins in aging and age-related disease. Cell, 126, 257-268.
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 31
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • Oin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J.T., et al. (2006) Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J. Biol. Chem, 281, 21745-21754.
    • (2006) J. Biol. Chem , vol.281 , pp. 21745-21754
    • Oin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6    Zhao, W.7    Thiyagarajan, M.8    MacGrogan, D.9    Rodgers, J.T.10
  • 32
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H.A. and Guarente, L. (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature, 410 227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 33
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J.F., Brignull, H.R., Weyers, J.J. and Morimoto, R.I. (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA, 99, 10417-10422.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 34
    • 10644282295 scopus 로고    scopus 로고
    • The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans
    • Apfeld, J., O'Connor, G., McDonagh, T., DiStefano, P.S. and Curtis, R. (2004) The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans. Genes Dev., 18 3004-3009.
    • (2004) Genes Dev , vol.18 , pp. 3004-3009
    • Apfeld, J.1    O'Connor, G.2    McDonagh, T.3    DiStefano, P.S.4    Curtis, R.5
  • 35
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer, E.L., Oskoui, P.R., Banko, M.R., Maniar, J.M., Gygi, M.P., Gygi, S.P. and Brunet, A. (2007) The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor. J. Biol. Chem., 282, 30107-30119.
    • (2007) J. Biol. Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6    Brunet, A.7
  • 36
    • 33847396951 scopus 로고    scopus 로고
    • Small molecule inhibitors of Stat3 signaling pathway
    • Deng, J., Grande, F. and Neamati, N. (2007) Small molecule inhibitors of Stat3 signaling pathway. Curr. Cancer Drug Targets, 7, 91-107.
    • (2007) Curr. Cancer Drug Targets , vol.7 , pp. 91-107
    • Deng, J.1    Grande, F.2    Neamati, N.3
  • 38
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer's disease amyloid-beta peptides
    • Marambaud, P., Zhao, H. and Davies, P. (2005) Resveratrol promotes clearance of Alzheimer's disease amyloid-beta peptides. J. Biol. Chem., 280, 37377-37382.
    • (2005) J. Biol. Chem , vol.280 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 39
    • 31944450272 scopus 로고    scopus 로고
    • Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate
    • Valenzano, D.R., Terzibasi, E., Genade, T., Cattaneo, A., Domenici, L. and Cellerino, A. (2006) Resveratrol prolongs lifespan and retards the onset of age-related markers in a short-lived vertebrate. Curr. Biol. 16, 296-300.
    • (2006) Curr. Biol , vol.16 , pp. 296-300
    • Valenzano, D.R.1    Terzibasi, E.2    Genade, T.3    Cattaneo, A.4    Domenici, L.5    Cellerino, A.6
  • 41
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R. and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature, 431, 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 42
    • 33847290297 scopus 로고    scopus 로고
    • Duplication of Atxn11 suppresses SCA1 neuropathology by decreasing incorporation of polyglutamine-expanded ataxin-1 into native complexes
    • Bowman, A.B., Lam, Y.C., Jafar-Nejad, P., Chen, H.K., Richman, R., Samaco, R.C., Fryer, J.D., Kahle, J.J., Orr, H.T. and Zoghbi, H.Y. (2007) Duplication of Atxn11 suppresses SCA1 neuropathology by decreasing incorporation of polyglutamine-expanded ataxin-1 into native complexes. Nat. Genet., 39, 373-379.
    • (2007) Nat. Genet , vol.39 , pp. 373-379
    • Bowman, A.B.1    Lam, Y.C.2    Jafar-Nejad, P.3    Chen, H.K.4    Richman, R.5    Samaco, R.C.6    Fryer, J.D.7    Kahle, J.J.8    Orr, H.T.9    Zoghbi, H.Y.10
  • 43
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki, T., Sasaki, Y. and Milbrandt, J. (2004) Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science, 305, 1010-1013.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 45
    • 33846916625 scopus 로고    scopus 로고
    • FOXO transcription factors
    • Carter, M.E. and Brunet, A. (2007) FOXO transcription factors. Curr. Biol., 17, R113-R114.
    • (2007) Curr. Biol , vol.17
    • Carter, M.E.1    Brunet, A.2
  • 46
    • 43949109275 scopus 로고    scopus 로고
    • Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
    • ahead of print
    • Mammucari, C., Schiaffino, S. and Sandri, M. (2008) Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle. Autophagy, 4. ahead of print.
    • (2008) Autophagy , vol.4
    • Mammucari, C.1    Schiaffino, S.2    Sandri, M.3
  • 47
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao, J., Brault, J.J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S.H. and Goldberg, A.L. (2007) FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab., 6, 472-483.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 49
    • 33846332013 scopus 로고    scopus 로고
    • Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors
    • Allen, D.L. and Unterman, T.G. (2007) Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. Am. J. Physiol. Cell Physiol., 292, C188-C199.
    • (2007) Am. J. Physiol. Cell Physiol , vol.292
    • Allen, D.L.1    Unterman, T.G.2
  • 50
    • 0021724834 scopus 로고
    • Dominant mutations affecting muscle structure in Caenorhabditis elegans that map near the actin gene cluster
    • Waterston, R.H., Hirsh, D. and Lane, T.R. (1984) Dominant mutations affecting muscle structure in Caenorhabditis elegans that map near the actin gene cluster. J. Mol. Biol., 180, 473-496.
    • (1984) J. Mol. Biol , vol.180 , pp. 473-496
    • Waterston, R.H.1    Hirsh, D.2    Lane, T.R.3
  • 51
    • 33744976074 scopus 로고    scopus 로고
    • Berdichevsky, A., Viswanathan, M., Horvitz, H.R. and Guarente, L. (2006) C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell, 125, 1165-1177.
    • Berdichevsky, A., Viswanathan, M., Horvitz, H.R. and Guarente, L. (2006) C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell, 125, 1165-1177.
  • 52
    • 33645824089 scopus 로고    scopus 로고
    • Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails
    • Hosoda, N., Lejeune, F. and Maquat, L.E. (2006) Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails. Mol. Cell. Biol., 26, 3085-3097.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3085-3097
    • Hosoda, N.1    Lejeune, F.2    Maquat, L.E.3
  • 53
    • 38449093531 scopus 로고    scopus 로고
    • Duerr, J.S. (2006) Immunohistochemistry (June 19, 2006). In The C. elegans Research Community (ed.), WormBook. WormBook. doi/ 10.1895/wormbook.1.105.1, http://www.wormbook.org.
    • Duerr, J.S. (2006) Immunohistochemistry (June 19, 2006). In The C. elegans Research Community (ed.), WormBook. WormBook. doi/ 10.1895/wormbook.1.105.1, http://www.wormbook.org.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.