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Volumn 88, Issue 4, 2014, Pages 2071-2082

De Novo prion aggregates trigger autophagy in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; AUTOPHAGY; BLOTTING, WESTERN; DNA PRIMERS; HEAT-SHOCK PROTEINS; IMMUNOHISTOCHEMISTRY; MICE; MICE, TRANSGENIC; MUSCLE CELLS; MUSCLE, SKELETAL; POLYMERASE CHAIN REACTION; PRION DISEASES;

EID: 84893472608     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02279-13     Document Type: Article
Times cited : (19)

References (73)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144. http://dx.doi.org/10.1126/science.6801762.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 0021697856 scopus 로고
    • Prions: novel infectious pathogens
    • Prusiner SB. 1984. Prions: novel infectious pathogens. Adv. Virus Res. 29:1-56. http://dx.doi.org/10.1016/S0065-3527(08)60404-2.
    • (1984) Adv. Virus Res. , vol.29 , pp. 1-56
    • Prusiner, S.B.1
  • 3
    • 78651252910 scopus 로고    scopus 로고
    • Molecular pathology of human prion disease
    • Wadsworth JD, Collinge J. 2011. Molecular pathology of human prion disease. Acta Neuropathol. 121:69-77. http://dx.doi.org/10.1007/s00401-010-0735-5.
    • (2011) Acta Neuropathol. , vol.121 , pp. 69-77
    • Wadsworth, J.D.1    Collinge, J.2
  • 4
    • 84862889276 scopus 로고    scopus 로고
    • Prion propagation, toxicity and degradation
    • Aguzzi A, Falsig J. 2012. Prion propagation, toxicity and degradation. Nat. Neurosci. 15:936-939. http://dx.doi.org/10.1038/nn.3120.
    • (2012) Nat. Neurosci. , vol.15 , pp. 936-939
    • Aguzzi, A.1    Falsig, J.2
  • 6
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan CG, Ma J. 2010. Generating a prion with bacterially expressed recombinant prion protein. Science 327:1132-1135.http://dx.doi.org/10.1126/science.1183748.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 8
    • 79551573471 scopus 로고    scopus 로고
    • Immunohistochemical study of PrPSc distribution in neural and extraneural tissues of two cats with feline spongiform encephalopathy
    • Hilbe MM, Soldati GG, Zlinszky KK, Wunderlin SS, Ehrensperger FF.2009. Immunohistochemical study of PrPSc distribution in neural and extraneural tissues of two cats with feline spongiform encephalopathy.BMC Vet. Res. 5:11. http://dx.doi.org/10.1186/1746-6148-5-11.
    • (2009) BMC Vet. Res. , vol.5 , pp. 11
    • Hilbe, M.M.1    Soldati, G.G.2    Zlinszky, K.K.3    Wunderlin, S.S.4    Ehrensperger, F.F.5
  • 9
    • 0034784808 scopus 로고    scopus 로고
    • PrPCWD in the myenteric plexus, vagosympathetic trunk and endocrine glands of deer with chronic wasting disease
    • Sigurdson CJ, Spraker TR, Miller MW, Oesch B, Hoover EA. 2001. PrPCWD in the myenteric plexus, vagosympathetic trunk and endocrine glands of deer with chronic wasting disease. J. Gen. Virol. 82:2327-2334.http://vir.sgmjournals.org/content/82/10/2327.long.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2327-2334
    • Sigurdson, C.J.1    Spraker, T.R.2    Miller, M.W.3    Oesch, B.4    Hoover, E.A.5
  • 10
    • 77955034938 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease
    • Ironside JW. 2010. Variant Creutzfeldt-Jakob disease. Haemophilia 16(Suppl. 5):175-180. http://dx.doi.org/10.1111/j.1365-2516.2010.02317.x.
    • (2010) Haemophilia , vol.16 , Issue.SUPPL. 5 , pp. 175-180
    • Ironside, J.W.1
  • 11
    • 27644504903 scopus 로고    scopus 로고
    • PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease.J
    • Herzog C, Riviere J, Lescoutra-Etchegaray N, Charbonnier A, Leblanc V, Sales N, Deslys JP, Lasmezas CI. 2005. PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease.J. Virol. 79:14339-14345. http://dx.doi.org/10.1128/JVI.79.22.14339-14345.2005.
    • (2005) Virol. , vol.79 , pp. 14339-14345
    • Herzog, C.1    Riviere, J.2    Lescoutra-Etchegaray, N.3    Charbonnier, A.4    Leblanc, V.5    Sales, N.6    Deslys, J.P.7    Lasmezas, C.I.8
  • 12
    • 0242361687 scopus 로고    scopus 로고
    • Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease
    • Glatzel M, Abela E, Maissen M, Aguzzi A. 2003. Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease. N. Engl. J. Med. 349:1812-1820. http://dx.doi.org/10.1056/NEJMoa030351.
    • (2003) N. Engl. J. Med. , vol.349 , pp. 1812-1820
    • Glatzel, M.1    Abela, E.2    Maissen, M.3    Aguzzi, A.4
  • 14
    • 0038110004 scopus 로고    scopus 로고
    • Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie
    • Thomzig A, Kratzel C, Lenz G, Kruger D, Beekes M. 2003. Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie.EMBO Rep. 4:1-4. http://dx.doi.org/10.1038/sj.embor.embor717.
    • (2003) EMBO Rep. , vol.4 , pp. 1-4
    • Thomzig, A.1    Kratzel, C.2    Lenz, G.3    Kruger, D.4    Beekes, M.5
  • 17
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway D, DeArmond SJ, Cayetano-Canlas J, Groth D, Foster D, Yang SL, Torchia M, Carlson GA, Prusiner SB. 1994. Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76:117-129. http://dx.doi.org/10.1016/0092-8674(94)90177-5.
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1    DeArmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 20
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP (121-231)
    • Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. 1996. NMR structure of the mouse prion protein domain PrP (121-231). Nature 382:180-182. http://dx.doi.org/10.1038/382180a0.
    • (1996) Nature , vol.382 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Billeter, M.4    Glockshuber, R.5    Wüthrich, K.6
  • 22
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • Hershko A, Ciechanover A. 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425-479. http://dx.doi.org/10.1146/annurev.biochem.67.1.425.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 23
    • 82755187338 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. 2012. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Biochim. Biophys. Acta 1824:3-13. http://dx.doi.org/10.1016/j.bbapap.2011.03.007.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 3-13
    • Ciechanover, A.1
  • 24
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E, Cuervo AM. 2010. Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 13:805-811. http://dx.doi.org/10.1038/nn.2575.
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 25
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation
    • Askanas V, Engel WK, Nogalska A. 2009. Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol. 19:493-506. http://dx.doi.org/10.1111/j.1750-3639.2009.00290.x.
    • (2009) Brain Pathol. , vol.19 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 26
    • 56749104288 scopus 로고    scopus 로고
    • Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains
    • Askanas V, Engel WK. 2008. Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol. 116:583-595. http://dx.doi.org/10.1007/s00401-008-0449-0.
    • (2008) Acta Neuropathol. , vol.116 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 27
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitincontaining autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, Dantuma NP, Taylor JP. 2010. VCP/p97 is essential for maturation of ubiquitincontaining autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6:217-227. http://dx.doi.org/10.4161/auto.6.2.11014.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 29
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P, Ron D. 2011. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334:1081-1086. http://dx.doi.org/10.1126/science.1209038.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 32
    • 80053212141 scopus 로고    scopus 로고
    • Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein
    • Nunziante M, Ackermann K, Dietrich K, Wolf H, Gadtke L, Gilch S, Vorberg I, Groschup M, Schatzl HM. 2011. Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein. J. Biol. Chem. 286:33942-33953. http://dx.doi.org/10.1074/jbc.M111.272617.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33942-33953
    • Nunziante, M.1    Ackermann, K.2    Dietrich, K.3    Wolf, H.4    Gadtke, L.5    Gilch, S.6    Vorberg, I.7    Groschup, M.8    Schatzl, H.M.9
  • 34
    • 0344683235 scopus 로고    scopus 로고
    • National Research Council, 8th ed. National Academies Press, Washington, DC.
    • National Research Council. 2011. Guide for the care and use of laboratory animals, 8th ed. National Academies Press, Washington, DC.
    • (2011) Guide for the care and use of laboratory animals
  • 36
    • 77952782927 scopus 로고    scopus 로고
    • Distribution pattern of muscle fiber types in the perivertebral musculature of two different sized species of mice
    • Hesse B, Fischer MS, Schilling N. 2010. Distribution pattern of muscle fiber types in the perivertebral musculature of two different sized species of mice. Anat. Rec. (Hoboken) 293:446-463. http://dx.doi.org/10.1002/ar.21090.
    • (2010) Anat. Rec. (Hoboken) , vol.293 , pp. 446-463
    • Hesse, B.1    Fischer, M.S.2    Schilling, N.3
  • 42
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332:462-464. http://dx.doi.org/10.1038/332462a0.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 43
    • 34447093377 scopus 로고    scopus 로고
    • Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
    • Weihl CC, Miller SE, Hanson PI, Pestronk A. 2007. Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice. Hum. Mol. Genet. 16:919-928. http://dx.doi.org/10.1093/hmg/ddm037.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 919-928
    • Weihl, C.C.1    Miller, S.E.2    Hanson, P.I.3    Pestronk, A.4
  • 44
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin JH, Walter P, Yen TS. 2008. Endoplasmic reticulum stress in disease pathogenesis. Annu. Rev. Pathol. 3:399-425. http://dx.doi.org/10.1146/annurev.pathmechdis.3.121806.151434.
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 48
    • 0037219399 scopus 로고    scopus 로고
    • Filamentous tau in oligodendrocytes and astrocytes of transgenic mice expressing the human tau isoform with the P301L mutation
    • Lin WL, Lewis J, Yen SH, Hutton M, Dickson DW. 2003. Filamentous tau in oligodendrocytes and astrocytes of transgenic mice expressing the human tau isoform with the P301L mutation. Am. J. Pathol. 162:213-218. http://dx.doi.org/10.1016/S0002-9440(10)63812-6.
    • (2003) Am. J. Pathol. , vol.162 , pp. 213-218
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3    Hutton, M.4    Dickson, D.W.5
  • 50
    • 84883451249 scopus 로고    scopus 로고
    • Selective autophagy: talking with the UPS
    • Park C, Cuervo AM. 2013. Selective autophagy: talking with the UPS. Cell Biochem. Biophys. 67:3-13. http://dx.doi.org/10.1007/s12013-013-9623-7.
    • (2013) Cell Biochem. Biophys. , vol.67 , pp. 3-13
    • Park, C.1    Cuervo, A.M.2
  • 51
    • 79952628267 scopus 로고    scopus 로고
    • The Beclin 1 network regulates autophagy and apoptosis
    • Kang R, Zeh HJ, Lotze MT, Tang D. 2011. The Beclin 1 network regulates autophagy and apoptosis. Cell Death Differ. 18:571-580. http://dx.doi.org/10.1038/cdd.2010.191.
    • (2011) Cell Death Differ. , vol.18 , pp. 571-580
    • Kang, R.1    Zeh, H.J.2    Lotze, M.T.3    Tang, D.4
  • 52
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy: assays and artifacts
    • Barth S, Glick D, Macleod KF. 2010. Autophagy: assays and artifacts. J. Pathol. 221:117-124. http://dx.doi.org/10.1002/path.2694.
    • (2010) J. Pathol. , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    Macleod, K.F.3
  • 54
    • 84862768394 scopus 로고    scopus 로고
    • Autophagy proteins in macroendocytic engulfment
    • Florey O, Overholtzer M. 2012. Autophagy proteins in macroendocytic engulfment. Trends Cell Biol. 22:374-380. http://dx.doi.org/10.1016/j.tcb.2012.04.005.
    • (2012) Trends Cell Biol. , vol.22 , pp. 374-380
    • Florey, O.1    Overholtzer, M.2
  • 55
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A. 2001. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20:5383-5391. http://dx.doi.org/10.1093/emboj/20.19.5383.
    • (2001) EMBO J. , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 56
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • Rane NS, Yonkovich JL, Hegde RS. 2004. Protection from cytosolic prion protein toxicity by modulation of protein translocation. EMBO J. 23:4550-4559. http://dx.doi.org/10.1038/sj.emboj.7600462.
    • (2004) EMBO J. , vol.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 57
    • 33744739867 scopus 로고    scopus 로고
    • Genetically augmenting Aβ42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice
    • Kitazawa M, Green KN, Caccamo A, LaFerla FM. 2006. Genetically augmenting Aβ42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice. Am. J. Pathol. 168:1986-1997. http://dx.doi.org/10.2353/ajpath.2006.051232.
    • (2006) Am. J. Pathol. , vol.168 , pp. 1986-1997
    • Kitazawa, M.1    Green, K.N.2    Caccamo, A.3    LaFerla, F.M.4
  • 59
    • 80053247082 scopus 로고    scopus 로고
    • Novel demonstration of conformationally modified tau in sporadic inclusion-body myositis muscle fibers
    • Nogalska A, D'Agostino C, Engel WK, Askanas V. 2011. Novel demonstration of conformationally modified tau in sporadic inclusion-body myositis muscle fibers. Neurosci. Lett. 503:229-233. http://dx.doi.org/10.1016/j.neulet.2011.08.042.
    • (2011) Neurosci. Lett. , vol.503 , pp. 229-233
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3    Askanas, V.4
  • 62
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. 2003. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 22:5435-5445. http://dx.doi.org/10.1093/emboj/cdg537.
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 64
    • 78649937640 scopus 로고    scopus 로고
    • Transcriptional analysis implicates endoplasmic reticulum stress in bovine spongiform encephalopathy
    • Tang Y, Xiang W, Terry L, Kretzschmar HA, Windl O. 2010. Transcriptional analysis implicates endoplasmic reticulum stress in bovine spongiform encephalopathy. PLoS One 5:e14207. http://dx.doi.org/10.1371/journal.pone.0014207.
    • (2010) PLoS One , vol.5
    • Tang, Y.1    Xiang, W.2    Terry, L.3    Kretzschmar, H.A.4    Windl, O.5
  • 66
    • 34250351315 scopus 로고    scopus 로고
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication
    • Hetz C, Castilla J, Soto C. 2007. Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J. Biol. Chem. 282:12725-12733. http://dx.doi.org/10.1074/jbc.M611909200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12725-12733
    • Hetz, C.1    Castilla, J.2    Soto, C.3
  • 67
    • 68349097450 scopus 로고    scopus 로고
    • p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • Nogalska A, Terracciano C, D'Agostino C, King Engel W, Askanas V. 2009. p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol.118:407-413. http://dx.doi.org/10.1007/s00401-009-0564-6.
    • (2009) Acta Neuropathol. , vol.118 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3    King Engel, W.4    Askanas, V.5
  • 68
    • 77953894192 scopus 로고    scopus 로고
    • Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy
    • Ju JS, Weihl CC. 2010. Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy. Hum. Mol. Genet. 19:R38-R45. http://dx.doi.org/10.1093/hmg/ddq157.
    • (2010) Hum. Mol. Genet. , vol.19
    • Ju, J.S.1    Weihl, C.C.2
  • 70
    • 84869475871 scopus 로고    scopus 로고
    • Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases
    • Xu Y, Tian C, Wang SB, Xie WL, Guo Y, Zhang J, Shi Q, Chen C, Dong XP. 2012. Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases. Autophagy 8:1604-1620. http://dx.doi.org/10.4161/auto.21482.
    • (2012) Autophagy , vol.8 , pp. 1604-1620
    • Xu, Y.1    Tian, C.2    Wang, S.B.3    Xie, W.L.4    Guo, Y.5    Zhang, J.6    Shi, Q.7    Chen, C.8    Dong, X.P.9
  • 71
    • 84865749298 scopus 로고    scopus 로고
    • Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Straussler-Scheinker disease
    • Cortes CJ, Qin K, Cook J, Solanki A, Mastrianni JA. 2012. Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Straussler-Scheinker disease. J. Neurosci. 32:12396-12405. http://dx.doi.org/10.1523/JNEUROSCI.6189-11.2012.
    • (2012) J. Neurosci. , vol.32 , pp. 12396-12405
    • Cortes, C.J.1    Qin, K.2    Cook, J.3    Solanki, A.4    Mastrianni, J.A.5
  • 72
    • 65249103439 scopus 로고    scopus 로고
    • Autophagy induction by trehalose counteracts cellular prion infection
    • Aguib Y, Heiseke A, Gilch S, Riemer C, Baier M, Schatzl HM, Ertmer A. 2009. Autophagy induction by trehalose counteracts cellular prion infection. Autophagy 5:361-369. http://dx.doi.org/10.4161/auto.5.3.7662.
    • (2009) Autophagy , vol.5 , pp. 361-369
    • Aguib, Y.1    Heiseke, A.2    Gilch, S.3    Riemer, C.4    Baier, M.5    Schatzl, H.M.6    Ertmer, A.7
  • 73
    • 61849102412 scopus 로고    scopus 로고
    • Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy
    • Heiseke A, Aguib Y, Riemer C, Baier M, Schatzl HM. 2009. Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy. J. Neurochem. 109:25-34. http://dx.doi.org/10.1111/j.1471-4159.2009.05906.x.
    • (2009) J. Neurochem. , vol.109 , pp. 25-34
    • Heiseke, A.1    Aguib, Y.2    Riemer, C.3    Baier, M.4    Schatzl, H.M.5


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