메뉴 건너뛰기




Volumn 72, Issue 21, 2015, Pages 4027-4047

Regulation of protein homeostasis in neurodegenerative diseases: The role of coding and non-coding genes

Author keywords

Aggresome; Alzheimer's disease; C. elegans; Chaperone; Genetic modifiers; Huntington's disease; iPOD; JunQ; miRNA; Neurodegeneration; Non coding RNA; Parkinson's disease; Protein aggregation; Protein homeostasis; Protein quality control; Proteostasis; Proteotoxicity; tRNA

Indexed keywords

ALPHA SYNUCLEIN; BETA SECRETASE; MICRORNA; POLYGLUTAMINE; SMALL NUCLEAR RNA; SURVIVAL MOTOR NEURON PROTEIN; TRANSFER RNA; UNTRANSLATED RNA; PROTEIN;

EID: 84944175522     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1985-0     Document Type: Review
Times cited : (28)

References (265)
  • 1
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • 10.1021/bi961799n 1:CAS:528:DyaK28XmtVOls7s%3D 8901511
    • Weinreb PH, Zhen W, Poon AW et al (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35:13709-13715. doi: 10.1021/bi961799n
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3
  • 2
    • 57049095821 scopus 로고    scopus 로고
    • Function and structure of inherently disordered proteins
    • 10.1016/j.sbi.2008.10.002 1:CAS:528:DC%2BD1cXhsVOisr%2FK 18952168
    • Dunker AK, Silman I, Uversky VN, Sussman JL (2008) Function and structure of inherently disordered proteins. Curr Opin Struct Biol 18:756-764. doi: 10.1016/j.sbi.2008.10.002
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 756-764
    • Dunker, A.K.1    Silman, I.2    Uversky, V.N.3    Sussman, J.L.4
  • 3
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • 10.1529/biophysj.106.094045 1796814 1:CAS:528:DC%2BD2sXit1amtbs%3D 17158572
    • Radivojac P, Iakoucheva LM, Oldfield CJ et al (2007) Intrinsic disorder and functional proteomics. Biophys J 92:1439-1456. doi: 10.1529/biophysj.106.094045
    • (2007) Biophys J , vol.92 , pp. 1439-1456
    • Radivojac, P.1    Iakoucheva, L.M.2    Oldfield, C.J.3
  • 4
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
    • 10.1016/S0022-2836(02)00969-5 1:CAS:528:DC%2BD38XnslGrtLw%3D 12381310
    • Iakoucheva LM, Brown CJ, Lawson JD et al (2002) Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins. J Mol Biol 323:573-584. doi: 10.1016/S0022-2836(02)00969-5
    • (2002) J Mol Biol , vol.323 , pp. 573-584
    • Iakoucheva, L.M.1    Brown, C.J.2    Lawson, J.D.3
  • 5
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • 10.1002/jmr.747 1:CAS:528:DC%2BD2MXhtVCgt73F 16094605
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18:343-384. doi: 10.1002/jmr.747
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 6
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • 10.1111/j.1742-4658.2005.04948.x 1:CAS:528:DC%2BD2MXhtFGqtbjO 16218947
    • Dunker AK, Cortese MS, Romero P et al (2005) Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272:5129-5148. doi: 10.1111/j.1742-4658.2005.04948.x
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3
  • 7
    • 1942421714 scopus 로고    scopus 로고
    • Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed
    • 1:CAS:528:DC%2BD2cXjsFyrurY%3D 15084258
    • Agashe VR, Guha S, Chang H-C et al (2004) Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell 117:199-209
    • (2004) Cell , vol.117 , pp. 199-209
    • Agashe, V.R.1    Guha, S.2    Chang, H.-C.3
  • 8
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • 10.1038/10754 1:CAS:528:DyaK1MXksVenu7Y%3D 10404229
    • Frydman J, Erdjument-Bromage H, Tempst P, Hartl FU (1999) Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat Struct Biol 6:697-705. doi: 10.1038/10754
    • (1999) Nat Struct Biol , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4
  • 9
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • 398335 1:CAS:528:DyaK2MXlvFynsbk%3D 7774586
    • Freeman BC, Myers MP, Schumacher R, Morimoto RI (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 14:2281-2292
    • (1995) EMBO J , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 10
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • 10.1038/41024 1:CAS:528:DyaK2sXkvVCjtro%3D 9237751
    • Netzer WJ, Hartl FU (1997) Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388:343-349. doi: 10.1038/41024
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 11
    • 0028360710 scopus 로고
    • ATP-dependent chaperoning activity of reticulocyte lysate
    • 1:CAS:528:DyaK2cXkt12gsbc%3D 8144534
    • Schumacher RJ, Hurst R, Sullivan WP et al (1994) ATP-dependent chaperoning activity of reticulocyte lysate. J Biol Chem 269:9493-9499
    • (1994) J Biol Chem , vol.269 , pp. 9493-9499
    • Schumacher, R.J.1    Hurst, R.2    Sullivan, W.P.3
  • 12
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • 10.1146/annurev.biochem.70.1.603 1:CAS:528:DC%2BD3MXlsVehtLo%3D 11395418
    • Frydman J (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70:603-647. doi: 10.1146/annurev.biochem.70.1.603
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 13
    • 0032573163 scopus 로고    scopus 로고
    • Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
    • 23633 1:CAS:528:DyaK1cXntFWktrY%3D 9789005
    • Kim S, Schilke B, Craig EA, Horwich AL (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci 95:12860-12865
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 12860-12865
    • Kim, S.1    Schilke, B.2    Craig, E.A.3    Horwich, A.L.4
  • 14
    • 0028079904 scopus 로고
    • The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase
    • 1:CAS:528:DyaK2cXmvFKrtr0%3D 8001582
    • Crombie T, Boyle JP, Coggins JR, Brown AJ (1994) The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Eur J Biochem 226:657-664
    • (1994) Eur J Biochem , vol.226 , pp. 657-664
    • Crombie, T.1    Boyle, J.P.2    Coggins, J.R.3    Brown, A.J.4
  • 15
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • 10.1038/nature10317 1:CAS:528:DC%2BC3MXpt1aqsb8%3D 21776078
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475:324-332. doi: 10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 16
    • 84878948560 scopus 로고    scopus 로고
    • Molecular Chaperone Functions in Protein Folding and Proteostasis
    • 10.1146/annurev-biochem-060208-092442 1:CAS:528:DC%2BC3sXhtFOqsrzF 23746257
    • Kim YE, Hipp MS, Bracher A et al (2013) Molecular Chaperone Functions in Protein Folding and Proteostasis. Annu Rev Biochem 82:323-355. doi: 10.1146/annurev-biochem-060208-092442
    • (2013) Annu Rev Biochem , vol.82 , pp. 323-355
    • Kim, Y.E.1    Hipp, M.S.2    Bracher, A.3
  • 17
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • 10.1038/nrm2993 1:CAS:528:DC%2BC3cXht1yjsL3K
    • Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nature Publishing Group 11:777-788. doi: 10.1038/nrm2993
    • (2010) Nature Publishing Group , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 19
    • 84857131348 scopus 로고    scopus 로고
    • HSF transcription factor family, heat shock response, and protein intrinsic disorder
    • 1:CAS:528:DC%2BC38XkvFamtLo%3D 22044151
    • Westerheide SD, Raynes R, Powell C et al (2012) HSF transcription factor family, heat shock response, and protein intrinsic disorder. Curr Protein Pept Sci 13:86-103
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 86-103
    • Westerheide, S.D.1    Raynes, R.2    Powell, C.3
  • 20
    • 84863313893 scopus 로고    scopus 로고
    • Cellular strategies of protein quality control
    • 10.1101/cshperspect.a004374 3140689 21746797
    • Chen B, Retzlaff M, Roos T, Frydman J (2011) Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol 3:a004374-a004375. doi: 10.1101/cshperspect.a004374
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. a004374-a004375
    • Chen, B.1    Retzlaff, M.2    Roos, T.3    Frydman, J.4
  • 21
    • 84863651655 scopus 로고    scopus 로고
    • Aging as an event of proteostasis collapse
    • 10.1101/cshperspect.a004440 3101847 21441594
    • Taylor RC, Dillin A (2011) Aging as an event of proteostasis collapse. Cold Spring Harb Perspect Biol 3:a004440-a004441. doi: 10.1101/cshperspect.a004440
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. a004440-a004441
    • Taylor, R.C.1    Dillin, A.2
  • 22
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • 10.1101/gad.1657108 2732416 1:CAS:528:DC%2BD1cXnsVOlurY%3D 18519635
    • Morimoto RI (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 22:1427-1438. doi: 10.1101/gad.1657108
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 23
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan. 1-11.
    • Åkerfelt M, Morimoto RI, Sistonen L (2010) Heat shock factors: integrators of cell stress, development and lifespan. 1-11. doi: 10.1038/nrm2938
    • (2010)
    • Åkerfelt M, M.1
  • 24
    • 25844466597 scopus 로고    scopus 로고
    • Heat Shock Response Modulators as Therapeutic Tools for Diseases of Protein Conformation
    • 10.1074/jbc.R500010200 1:CAS:528:DC%2BD2MXhtVens7nJ 16076838
    • Westerheide SD, Morimoto RI (2005) Heat Shock Response Modulators as Therapeutic Tools for Diseases of Protein Conformation. J Biol Chem 280:33097-33100. doi: 10.1074/jbc.R500010200
    • (2005) J Biol Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 25
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Stress in Disease Pathogenesis
    • 10.1146/annurev.pathmechdis.3.121806.151434 1:CAS:528:DC%2BD1cXjsFersLg%3D
    • Lin JH, Walter P, Yen TSB (2008) Endoplasmic Reticulum Stress in Disease Pathogenesis. Annu Rev Pathol Mech Dis 3:399-425. doi: 10.1146/annurev.pathmechdis.3.121806.151434
    • (2008) Annu Rev Pathol Mech Dis , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.B.3
  • 26
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • 10.1038/nrm2199 1:CAS:528:DC%2BD2sXmvVaktLY%3D 17565364
    • Ron D, Walter P (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8:519-529. doi: 10.1038/nrm2199
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 28
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • 10.1038/415092a 1:CAS:528:DC%2BD38Xkt1yhtQ%3D%3D 11780124
    • Calfon M, Zeng H, Urano F et al (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415:92-96. doi: 10.1038/415092a
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3
  • 29
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • 1:CAS:528:DC%2BD38XjtlKlsg%3D%3D 11779464
    • Yoshida H, Matsui T, Yamamoto A et al (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107:881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3
  • 30
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • 1:CAS:528:DyaK28XmvVOktrc%3D 8898193
    • Cox JS, Walter P (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87:391-404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 31
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • 1:CAS:528:DyaK3sXksValu7g%3D 8513503
    • Cox JS, Shamu CE, Walter P (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73:1197-1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 32
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2 +/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • 1:CAS:528:DyaK3sXms1ektL0%3D 8358794
    • Mori K, Ma W, Gething MJ, Sambrook J (1993) A transmembrane protein with a cdc2 +/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74:743-756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 33
    • 3142658576 scopus 로고    scopus 로고
    • XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation
    • 10.1016/j.immuni.2004.06.010 1:CAS:528:DC%2BD2cXmtlKjt74%3D 15345222
    • Shaffer AL, Shapiro-Shelef M, Iwakoshi NN et al (2004) XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21:81-93. doi: 10.1016/j.immuni.2004.06.010
    • (2004) Immunity , vol.21 , pp. 81-93
    • Shaffer, A.L.1    Shapiro-Shelef, M.2    Iwakoshi, N.N.3
  • 34
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • 10.1042/BJ20020391 1222788 1:CAS:528:DC%2BD38XnvFGltb0%3D 12014989
    • Okada T, Yoshida H, Akazawa R et al (2002) Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J 366:585-594. doi: 10.1042/BJ20020391
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3
  • 35
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • 1:CAS:528:DC%2BD3cXjtFSrtL4%3D 10847680
    • Travers KJ, Patil CK, Wodicka L et al (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3
  • 36
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • 1:CAS:528:DC%2BD3MXlvFahtQ%3D%3D 11163209
    • Ye J, Rawson RB, Komuro R et al (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6:1355-1364
    • (2000) Mol Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3
  • 37
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • 25679 1:CAS:528:DyaK1MXntlyrsLs%3D 10564271
    • Haze K, Yoshida H, Yanagi H et al (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10:3787-3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3
  • 38
    • 34548189283 scopus 로고    scopus 로고
    • ATF6α optimizes long-term endoplasmic reticulum function to protect cells from chronic stress
    • 10.1016/j.devcel.2007.07.005 1:CAS:528:DC%2BD2sXhtVels73M 17765679
    • Wu J, Rutkowski DT, Dubois M et al (2007) ATF6α optimizes long-term endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 13:351-364. doi: 10.1016/j.devcel.2007.07.005
    • (2007) Dev Cell , vol.13 , pp. 351-364
    • Wu, J.1    Rutkowski, D.T.2    Dubois, M.3
  • 39
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • 86199 1:CAS:528:DC%2BD3cXmsVams7w%3D 10958673
    • Yoshida H, Okada T, Haze K et al (2000) ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 20:6755-6767
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3
  • 40
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • 1:CAS:528:DC%2BD3MXkvVaqurk%3D 11430820
    • Scheuner D, Song B, McEwen E et al (2001) Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 7:1165-1176
    • (2001) Mol Cell , vol.7 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3
  • 41
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • 1:CAS:528:DC%2BD3cXosV2mtrs%3D 11106749
    • Harding HP, Novoa I, Zhang Y et al (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6:1099-1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3
  • 42
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • 10.1038/16729 1:CAS:528:DyaK1MXpvVGrtA%3D%3D 9930704
    • Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397:271-274. doi: 10.1038/16729
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 43
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • 10.1016/j.cell.2012.11.012 3521611 1:CAS:528:DC%2BC38XhvVaisr3L 23217703
    • Brodsky JL (2012) Cleaning up: ER-associated degradation to the rescue. Cell 151:1163-1167. doi: 10.1016/j.cell.2012.11.012
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 44
    • 84857612880 scopus 로고    scopus 로고
    • Protein folding and quality control in the ER
    • 10.1101/cshperspect.a007526 3220362 21875985
    • Araki K, Nagata K (2011) Protein folding and quality control in the ER. Cold Spring Harb Perspect Biol 3:a007526-a007527. doi: 10.1101/cshperspect.a007526
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. a007526-a007527
    • Araki, K.1    Nagata, K.2
  • 45
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • 10.1038/nrm2546 2654601 1:CAS:528:DC%2BD1cXhsVWhurjI 19002207
    • Vembar SS, Brodsky JL (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9:944-957. doi: 10.1038/nrm2546
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 46
    • 77952583297 scopus 로고    scopus 로고
    • Protein quality control in the ER: The recognition of misfolded proteins
    • 10.1016/j.semcdb.2010.03.006 20347046
    • Määttänen P, Gehring K, Bergeron JJM, Thomas DY (2010) Protein quality control in the ER: the recognition of misfolded proteins. Semin Cell Dev Biol 21:500-511. doi: 10.1016/j.semcdb.2010.03.006
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 500-511
    • Määttänen, P.1    Gehring, K.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 47
    • 77957293977 scopus 로고    scopus 로고
    • Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation
    • 10.1111/j.1463-1326.2010.01273.x 3071497 1:CAS:528:DC%2BC3cXhsVGgs7vF 21029298
    • Goeckeler JL, Brodsky JL (2010) Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation. Diabetes Obes Metab 12:32-38. doi: 10.1111/j.1463-1326.2010.01273.x
    • (2010) Diabetes Obes Metab , vol.12 , pp. 32-38
    • Goeckeler, J.L.1    Brodsky, J.L.2
  • 48
    • 48249155627 scopus 로고    scopus 로고
    • ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C
    • 10.1091/mbc.E07-07-0674 2397301 1:CAS:528:DC%2BD1cXntV2rtLg%3D 18400946
    • Dong M, Bridges JP, Apsley K et al (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol Biol Cell 19:2620-2630. doi: 10.1091/mbc.E07-07-0674
    • (2008) Mol Biol Cell , vol.19 , pp. 2620-2630
    • Dong, M.1    Bridges, J.P.2    Apsley, K.3
  • 49
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • 2174341 1:CAS:528:DC%2BD3MXktVags78%3D 11381090
    • Nishikawa SI, Fewell SW, Kato Y et al (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153:1061-1070
    • (2001) J Cell Biol , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3
  • 50
    • 0028927425 scopus 로고
    • In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER
    • 398186 1:CAS:528:DyaK2MXlsFSgu7k%3D 7720700
    • Schmitz A, Maintz M, Kehle T, Herzog V (1995) In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER. EMBO J 14:1091-1098
    • (1995) EMBO J , vol.14 , pp. 1091-1098
    • Schmitz, A.1    Maintz, M.2    Kehle, T.3    Herzog, V.4
  • 51
    • 0028928021 scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
    • 42600 1:CAS:528:DyaK2MXktFWrsLs%3D 7878056
    • Knittler MR, Dirks S, Haas IG (1995) Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci 92:1764-1768
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 52
    • 77952580752 scopus 로고    scopus 로고
    • Life and death of a BiP substrate
    • 10.1016/j.semcdb.2009.12.008 2883687 1:CAS:528:DC%2BC3cXmsleks70%3D 20026282
    • Otero JH, Lizák B, Hendershot LM (2010) Life and death of a BiP substrate. Semin Cell Dev Biol 21:472-478. doi: 10.1016/j.semcdb.2009.12.008
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 472-478
    • Otero, J.H.1    Lizák, B.2    Hendershot, L.M.3
  • 53
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • 1:STN:280:DyaK2c%2FmtF2ruw%3D%3D 7902213
    • Blond-Elguindi S, Cwirla SE, Dower WJ et al (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75:717-728
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3
  • 54
    • 55549141494 scopus 로고    scopus 로고
    • Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
    • 10.1038/emboj.2008.199 2580781 1:CAS:528:DC%2BD1cXhtlaltL7I 18923430
    • Petrova K, Oyadomari S, Hendershot LM, Ron D (2008) Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J 27:2862-2872. doi: 10.1038/emboj.2008.199
    • (2008) EMBO J , vol.27 , pp. 2862-2872
    • Petrova, K.1    Oyadomari, S.2    Hendershot, L.M.3    Ron, D.4
  • 55
    • 55549139747 scopus 로고    scopus 로고
    • Regulated release of ERdj3 from unfolded proteins by BiP
    • 10.1038/emboj.2008.207 2580786 1:CAS:528:DC%2BD1cXhtlaltL7L 18923428
    • Jin Y, Awad W, Petrova K, Hendershot LM (2008) Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J 27:2873-2882. doi: 10.1038/emboj.2008.207
    • (2008) EMBO J , vol.27 , pp. 2873-2882
    • Jin, Y.1    Awad, W.2    Petrova, K.3    Hendershot, L.M.4
  • 56
    • 33748776034 scopus 로고    scopus 로고
    • The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse
    • 10.1016/j.febslet.2006.08.055 1:CAS:528:DC%2BD28XpvFGntL4%3D 16962589
    • Weitzmann A, Volkmer J, Zimmermann R (2006) The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse. FEBS Lett 580:5237-5240. doi: 10.1016/j.febslet.2006.08.055
    • (2006) FEBS Lett , vol.580 , pp. 5237-5240
    • Weitzmann, A.1    Volkmer, J.2    Zimmermann, R.3
  • 57
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a Mammalian BiP-associated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP
    • 10.1074/jbc.M208377200 1:CAS:528:DC%2BD38XptFSqs78%3D 12356756
    • Chung KT, Shen Y, Hendershot LM (2002) BAP, a Mammalian BiP-associated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP. J Biol Chem 277:47557-47563. doi: 10.1074/jbc.M208377200
    • (2002) J Biol Chem , vol.277 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 58
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • 51342 1:CAS:528:DyaK3MXhvVWitLo%3D 1826368
    • Liberek K, Marszalek J, Ang D et al (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci 88:2874-2878
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3
  • 59
    • 58549098933 scopus 로고    scopus 로고
    • ERdj3, a Luminal ER DnaJ Homologue, Binds Directly to Unfolded Proteins in the Mammalian ER: Identification of Critical Residues
    • 10.1021/bi8015923 2709649 1:CAS:528:DC%2BD1cXhsFSqsLbN 19090675
    • Jin Y, Zhuang M, Hendershot LM (2009) ERdj3, a Luminal ER DnaJ Homologue, Binds Directly to Unfolded Proteins in the Mammalian ER: identification of Critical Residues. Biochemistry 48:41-49. doi: 10.1021/bi8015923
    • (2009) Biochemistry , vol.48 , pp. 41-49
    • Jin, Y.1    Zhuang, M.2    Hendershot, L.M.3
  • 60
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • 10.1146/annurev.biochem.78.081507.101607 3431160 1:CAS:528:DC%2BD1MXos1Ghurw%3D 19489727
    • Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78:477-513. doi: 10.1146/annurev.biochem.78.081507.101607
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 61
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • 10.1146/annurev.biochem.67.1.425 1:CAS:528:DyaK1cXlsFOmsLc%3D 9759494
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425-479. doi: 10.1146/annurev.biochem.67.1.425
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 62
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • 10.1146/annurev.genet.30.1.405 1:CAS:528:DyaK2sXht1yk 8982460
    • Hochstrasser M (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30:405-439. doi: 10.1146/annurev.genet.30.1.405
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 63
    • 4143061786 scopus 로고    scopus 로고
    • Binding of Polyubiquitin Chains to Ubiquitin-associated (UBA) Domains of HHR23A
    • 10.1016/j.jmb.2004.06.057 1:CAS:528:DC%2BD2cXmsVCrtbo%3D 15321727
    • Raasi S, Orlov I, Fleming KG, Pickart CM (2004) Binding of Polyubiquitin Chains to Ubiquitin-associated (UBA) Domains of HHR23A. J Mol Biol 341:1367-1379. doi: 10.1016/j.jmb.2004.06.057
    • (2004) J Mol Biol , vol.341 , pp. 1367-1379
    • Raasi, S.1    Orlov, I.2    Fleming, K.G.3    Pickart, C.M.4
  • 64
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • 10.1093/emboj/19.1.94 1171781 1:CAS:528:DC%2BD3cXht1ylt7w%3D 10619848
    • Thrower JS, Hoffman L, Rechsteiner M, Pickart CM (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J 19:94-102. doi: 10.1093/emboj/19.1.94
    • (2000) EMBO J , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 65
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • 10.1038/nature01071 1:CAS:528:DC%2BD38XntlGgsbY%3D 12353037
    • Yao T, Cohen RE (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419:403-407. doi: 10.1038/nature01071
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 66
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • 10.1126/science.1075898 1:CAS:528:DC%2BD38XotVWisL0%3D 12183636
    • Verma R, Aravind L, Oania R et al (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298:611-615. doi: 10.1126/science.1075898
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3
  • 67
    • 34248350363 scopus 로고    scopus 로고
    • MPN +, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • 129983 12370088
    • Maytal-Kivity V, Reis N, Hofmann K, Glickman MH (2002) MPN +, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem 3:28
    • (2002) BMC Biochem , vol.3 , pp. 28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 68
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • 10.1074/jbc.274.6.3363 1:CAS:528:DyaK1MXhtVemsrk%3D 9920878
    • Kisselev AF, Akopian TN, Woo KM, Goldberg AL (1999) The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J Biol Chem 274:3363-3371. doi: 10.1074/jbc.274.6.3363
    • (1999) J Biol Chem , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 69
    • 84866244791 scopus 로고    scopus 로고
    • Autophagy in Protein and Organelle Turnover
    • 10.1101/sqb.2011.76.011023
    • Mizushima N (2012) Autophagy in Protein and Organelle Turnover. Cold Spring Harb Symp Quant Biol 76:397-402. doi: 10.1101/sqb.2011.76.011023
    • (2012) Cold Spring Harb Symp Quant Biol , vol.76 , pp. 397-402
    • Mizushima, N.1
  • 71
    • 74949090299 scopus 로고    scopus 로고
    • An overview of the molecular mechanism of autophagy
    • Springer Berlin Heidelberg, Berlin, Heidelberg
    • Yang Z, Klionsky DJ (2009) An overview of the molecular mechanism of autophagy. Current topics in microbiology and immunology. Springer, Berlin Heidelberg, Berlin, Heidelberg, pp 1-32
    • (2009) Current Topics in Microbiology and Immunology , pp. 1-32
    • Yang, Z.1    Klionsky, D.J.2
  • 73
    • 79952585579 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: The proteasome and autophagy
    • 10.1101/cshperspect.a006734 2982176 1:CAS:528:DC%2BC3MXhsFKqtL8%3D 21068151
    • Wong E, Cuervo AM (2010) Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2:a006734-a006735. doi: 10.1101/cshperspect.a006734
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. a006734-a006735
    • Wong, E.1    Cuervo, A.M.2
  • 74
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • 10.4161/auto.5.8.10274
    • Ylä-Anttila P, Vihinen H, Jokitalo E, Eskelinen E-L (2014) 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 5:1180-1185. doi: 10.4161/auto.5.8.10274
    • (2014) Autophagy , vol.5 , pp. 1180-1185
    • Ylä-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.-L.4
  • 75
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • 10.1038/ncb1991 1:CAS:528:DC%2BD1MXhsV2gsLnE 19898463
    • Hayashi-Nishino M, Fujita N, Noda T et al (2009) A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol 11:1433-1437. doi: 10.1038/ncb1991
    • (2009) Nat Cell Biol , vol.11 , pp. 1433-1437
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3
  • 76
    • 77957265786 scopus 로고    scopus 로고
    • MiR-106b aberrantly expressed in a double transgenic mouse model for Alzheimer's disease targets TGF-β type II receptor
    • 10.1016/j.brainres.2010.08.023 1:CAS:528:DC%2BC3cXht1Wht7%2FN 20709030
    • Wang H, Liu J, Zong Y et al (2010) miR-106b aberrantly expressed in a double transgenic mouse model for Alzheimer's disease targets TGF-β type II receptor. Brain Res 1357:166-174. doi: 10.1016/j.brainres.2010.08.023
    • (2010) Brain Res , vol.1357 , pp. 166-174
    • Wang, H.1    Liu, J.2    Zong, Y.3
  • 77
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • 10.1038/ncb2078 2923063 1:CAS:528:DC%2BC3cXpsFWnsL4%3D 20639872
    • Ravikumar B, Moreau K, Jahreiss L et al (2010) Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat Cell Biol 12:747-757. doi: 10.1038/ncb2078
    • (2010) Nat Cell Biol , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3
  • 78
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • 10.1083/jcb.200803137 2518708 1:CAS:528:DC%2BD1cXhtV2rurzK 18725538
    • Axe EL, Walker SA, Manifava M et al (2008) Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 182:685-701. doi: 10.1083/jcb.200803137
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3
  • 79
    • 84894030921 scopus 로고    scopus 로고
    • Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy
    • 10.1083/jcb.201307050 3926955 1:CAS:528:DC%2BC2cXivFejsr4%3D 24535825
    • Nazarko TY, Ozeki K, Till A et al (2014) Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy. J Cell Biol 204:541-557. doi: 10.1083/jcb.201307050
    • (2014) J Cell Biol , vol.204 , pp. 541-557
    • Nazarko, T.Y.1    Ozeki, K.2    Till, A.3
  • 80
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • 10.1038/emboj.2012.151 3395097 1:CAS:528:DC%2BC38Xns1Whsbg%3D 22643220
    • Motley AM, Nuttall JM, Hettema EH (2012) Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J 31:2852-2868. doi: 10.1038/emboj.2012.151
    • (2012) EMBO J , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 81
    • 79251558467 scopus 로고    scopus 로고
    • Atg35, a micropexophagy-specific protein that regulates micropexophagic apparatus formation in Pichia pastoris
    • 10.4161/auto.7.4.14369 3127218 1:CAS:528:DC%2BC3MXlvVWntbs%3D 21169734
    • Nazarko VY, Nazarko TY, Farre J-C et al (2011) Atg35, a micropexophagy-specific protein that regulates micropexophagic apparatus formation in Pichia pastoris. Autophagy 7:375-385. doi: 10.4161/auto.7.4.14369
    • (2011) Autophagy , vol.7 , pp. 375-385
    • Nazarko, V.Y.1    Nazarko, T.Y.2    Farre, J.-C.3
  • 82
    • 77956924900 scopus 로고    scopus 로고
    • Selective transport of alpha-mannosidase by autophagic pathways: Identification of a novel receptor, Atg34p
    • 10.1074/jbc.M110.143511 2943286 1:CAS:528:DC%2BC3cXhtFKksL%2FP 20639194
    • Suzuki K, Kondo C, Morimoto M, Ohsumi Y (2010) Selective transport of alpha-mannosidase by autophagic pathways: identification of a novel receptor, Atg34p. J Biol Chem 285:30019-30025. doi: 10.1074/jbc.M110.143511
    • (2010) J Biol Chem , vol.285 , pp. 30019-30025
    • Suzuki, K.1    Kondo, C.2    Morimoto, M.3    Ohsumi, Y.4
  • 83
    • 73949122199 scopus 로고    scopus 로고
    • A genomic screen for yeast mutants defective in selective mitochondria autophagy
    • 10.1091/mbc.E09-03-0225 2777103 1:CAS:528:DC%2BD1MXhsFSkurbE 19793921
    • Kanki T, Wang K, Baba M et al (2009) A genomic screen for yeast mutants defective in selective mitochondria autophagy. Mol Biol Cell 20:4730-4738. doi: 10.1091/mbc.E09-03-0225
    • (2009) Mol Biol Cell , vol.20 , pp. 4730-4738
    • Kanki, T.1    Wang, K.2    Baba, M.3
  • 84
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • 10.1016/j.devcel.2009.06.014 2746076 1:CAS:528:DC%2BD1MXpsV2msbY%3D 19619495
    • Kanki T, Wang K, Cao Y et al (2009) Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell 17:98-109. doi: 10.1016/j.devcel.2009.06.014
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3
  • 85
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • 10.1016/j.devcel.2007.12.011 3763908 1:CAS:528:DC%2BD1cXjsFyltL8%3D 18331717
    • Farre J-C, Manjithaya R, Mathewson RD, Subramani S (2008) PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev Cell 14:365-376. doi: 10.1016/j.devcel.2007.12.011
    • (2008) Dev Cell , vol.14 , pp. 365-376
    • Farre, J.-C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 86
    • 33644587420 scopus 로고    scopus 로고
    • Atg28, a novel coiled-coil protein involved in autophagic degradation of peroxisomes in the methylotrophic yeast Pichia pastoris
    • 10.4161/auto.2226 1:CAS:528:DC%2BD28XkvFGjt78%3D 16874081
    • Stasyk OV, Stasyk OG, Mathewson RD et al (2006) Atg28, a novel coiled-coil protein involved in autophagic degradation of peroxisomes in the methylotrophic yeast Pichia pastoris. Autophagy 2:30-38. doi: 10.4161/auto.2226
    • (2006) Autophagy , vol.2 , pp. 30-38
    • Stasyk, O.V.1    Stasyk, O.G.2    Mathewson, R.D.3
  • 87
    • 33947378818 scopus 로고    scopus 로고
    • Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae
    • 10.1016/j.bbrc.2007.02.150 1:CAS:528:DC%2BD2sXjsVGisbk%3D 17362880
    • Kabeya Y, Kawamata T, Suzuki K, Ohsumi Y (2007) Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae. Biochemical and Biophysical Research Communications 356:405-410. doi: 10.1016/j.bbrc.2007.02.150
    • (2007) Biochemical and Biophysical Research Communications , vol.356 , pp. 405-410
    • Kabeya, Y.1    Kawamata, T.2    Suzuki, K.3    Ohsumi, Y.4
  • 88
    • 27844461994 scopus 로고    scopus 로고
    • Characterization of a novel autophagy-specific gene, ATG29
    • 10.1016/j.bbrc.2005.10.163 1:CAS:528:DC%2BD2MXht1Ggu7%2FN 16289106
    • Kawamata T, Kamada Y, Suzuki K et al (2005) Characterization of a novel autophagy-specific gene, ATG29. Biochem Biophys Res Commun 338:1884-1889. doi: 10.1016/j.bbrc.2005.10.163
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1884-1889
    • Kawamata, T.1    Kamada, Y.2    Suzuki, K.3
  • 89
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • 1:CAS:528:DC%2BD3sXotlSqu7o%3D 14536056
    • Klionsky DJ, Cregg JM, Dunn WA et al (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell 5:539-545
    • (2003) Dev Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1    Cregg, J.M.2    Dunn, W.A.3
  • 90
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macroautophagy
    • 10.1038/ncb0910-814 3616322 1:CAS:528:DC%2BC3cXhtFSju7zE 20811353
    • Yang Z, Klionsky DJ (2010) Eaten alive: a history of macroautophagy. Nat Cell Biol 12:814-822. doi: 10.1038/ncb0910-814
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 91
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • 10.1038/ncb1007-1102 1:CAS:528:DC%2BD2sXhtFSntbzJ 17909521
    • Xie Z, Klionsky DJ (2007) Autophagosome formation: core machinery and adaptations. Nat Cell Biol 9:1102-1109. doi: 10.1038/ncb1007-1102
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 92
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum
    • 10.4161/auto.7.7.14733
    • Mijaljica D, Prescott M, Devenish RJ (2014) Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 7:673-682. doi: 10.4161/auto.7.7.14733
    • (2014) Autophagy , vol.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 93
    • 79960330523 scopus 로고    scopus 로고
    • A photoconvertible fluorescent reporter to track chaperone-mediated autophagy
    • 10.1038/ncomms1393 3529934 21750540
    • Koga H, Martinez-Vicente M, Macian F et al (2011) A photoconvertible fluorescent reporter to track chaperone-mediated autophagy. Nat Commun 2:386. doi: 10.1038/ncomms1393
    • (2011) Nat Commun , vol.2 , pp. 386
    • Koga, H.1    Martinez-Vicente, M.2    Macian, F.3
  • 94
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • 1:CAS:528:DyaK28Xks1Wmu7o%3D 8662539
    • Cuervo AM, Dice JF (1996) A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273:501-503
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 95
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • 1:CAS:528:DyaK3cXivFei 2799391
    • Chiang HL, Terlecky SR, Plant CP, Dice JF (1989) A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246:382-385
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 96
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • 1:CAS:528:DyaL1cXkt1Slt78%3D 3360807
    • Chiang HL, Dice JF (1988) Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J Biol Chem 263:6797-6805
    • (1988) J Biol Chem , vol.263 , pp. 6797-6805
    • Chiang, H.L.1    Dice, J.F.2
  • 97
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • 2139836 1:CAS:528:DyaK2sXjtlenu7c%3D 9151685
    • Agarraberes FA, Terlecky SR, Dice JF (1997) An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 137:825-834
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 98
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • 10.1074/jbc.M001394200 1:CAS:528:DC%2BD3cXmsVWqt7c%3D 10862611
    • Salvador N, Aguado C, Horst M, Knecht E (2000) Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 275:27447-27456. doi: 10.1074/jbc.M001394200
    • (2000) J Biol Chem , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 99
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • 10.1038/nature04724 1:CAS:528:DC%2BD28XlvVGlsbc%3D 16625204
    • Hara T, Nakamura K, Matsui M et al (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441:885-889. doi: 10.1038/nature04724
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 101
    • 0038493550 scopus 로고    scopus 로고
    • Characterization of chronic low-level proteasome inhibition on neural homeostasis
    • 10.1046/j.1471-4159.2003.01885.x
    • Ding Q, Dimayuga E, Martin S et al (2004) Characterization of chronic low-level proteasome inhibition on neural homeostasis. J Neurochem 86:489-497. doi: 10.1046/j.1471-4159.2003.01885.x
    • (2004) J Neurochem , vol.86 , pp. 489-497
    • Ding, Q.1    Dimayuga, E.2    Martin, S.3
  • 102
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • 10.1038/nature05853 1:CAS:528:DC%2BD2sXms1WjsL8%3D 17568747
    • Pandey UB, Nie Z, Batlevi Y et al (2007) HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447:859-863. doi: 10.1038/nature05853
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3
  • 103
    • 33645829816 scopus 로고    scopus 로고
    • Consequences of the selective blockage of chaperone-mediated autophagy
    • 10.1073/pnas.0507436103 1458654 1:CAS:528:DC%2BD28XktFaitro%3D 16585521
    • Massey AC, Kaushik S, Sovak G et al (2006) Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci 103:5805-5810. doi: 10.1073/pnas.0507436103
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 5805-5810
    • Massey, A.C.1    Kaushik, S.2    Sovak, G.3
  • 104
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • 10.1038/ncb2838 4121856 1:CAS:528:DC%2BC3sXhsVeqsLrN 24036477
    • Escusa-Toret S, Vonk WIM, Frydman J (2013) Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat Cell Biol 15:1231-1243. doi: 10.1038/ncb2838
    • (2013) Nat Cell Biol , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.M.2    Frydman, J.3
  • 105
    • 84865277422 scopus 로고    scopus 로고
    • Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    • 10.1091/mbc.E12-03-0194 3418301 1:CAS:528:DC%2BC38Xht1arur7O 22718905
    • Malinovska L, Kroschwald S, Munder MC et al (2012) Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell 23:3041-3056. doi: 10.1091/mbc.E12-03-0194
    • (2012) Mol Biol Cell , vol.23 , pp. 3041-3056
    • Malinovska, L.1    Kroschwald, S.2    Munder, M.C.3
  • 106
    • 84861743338 scopus 로고    scopus 로고
    • Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress
    • 10.1074/jbc.M112.350934 3366003 1:CAS:528:DC%2BC38XnvVSqtb4%3D 22518844
    • Liu X-D, Ko S, Xu Y et al (2012) Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress. J Biol Chem 287:19687-19698. doi: 10.1074/jbc.M112.350934
    • (2012) J Biol Chem , vol.287 , pp. 19687-19698
    • Liu, X.-D.1    Ko, S.2    Xu, Y.3
  • 107
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • 10.1083/jcb.201106037 3257523 1:CAS:528:DC%2BC3MXhsFSlur3P 22065637
    • Specht S, Miller SBM, Mogk A, Bukau B (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 195:617-629. doi: 10.1083/jcb.201106037
    • (2011) J Cell Biol , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.M.2    Mogk, A.3    Bukau, B.4
  • 108
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • 10.1038/nature07195 2746971 1:CAS:528:DC%2BD1cXhtVGgtr7P 18756251
    • Kaganovich D, Kopito R, Frydman J (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454:1088-1095. doi: 10.1038/nature07195
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 109
    • 33745824614 scopus 로고    scopus 로고
    • ALIS are stress-induced protein storage compartments for substrates of the proteasome and autophagy
    • 1:CAS:528:DC%2BD28XnsVWjsbw%3D 16874109
    • Szeto J, Kaniuk NA, Canadien V et al (2006) ALIS are stress-induced protein storage compartments for substrates of the proteasome and autophagy. Autophagy 2:189-199
    • (2006) Autophagy , vol.2 , pp. 189-199
    • Szeto, J.1    Kaniuk, N.A.2    Canadien, V.3
  • 110
    • 84892865694 scopus 로고    scopus 로고
    • Sorting out the trash: The spatial nature of eukaryotic protein quality control
    • 10.1016/j.ceb.2013.12.006 4204729 1:CAS:528:DC%2BC2cXitlersrs%3D 24463332
    • Sontag EM, Vonk WI, Frydman J (2014) Sorting out the trash: the spatial nature of eukaryotic protein quality control. Curr Opin Cell Biol 26:139-146. doi: 10.1016/j.ceb.2013.12.006
    • (2014) Curr Opin Cell Biol , vol.26 , pp. 139-146
    • Sontag, E.M.1    Vonk, W.I.2    Frydman, J.3
  • 111
    • 55249120532 scopus 로고    scopus 로고
    • Protein quality control: On IPODs and other JUNQ
    • 10.1016/j.cub.2008.09.036 1:CAS:528:DC%2BD1cXhtlGmtrbJ 19000801
    • Bagola K, Sommer T (2008) Protein quality control: on IPODs and other JUNQ. Curr Biol 18:R1019-R1021. doi: 10.1016/j.cub.2008.09.036
    • (2008) Curr Biol , vol.18 , pp. R1019-R1021
    • Bagola, K.1    Sommer, T.2
  • 112
    • 84901856381 scopus 로고    scopus 로고
    • Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin
    • 10.1073/pnas.1324035111 4050583 1:CAS:528:DC%2BC2cXotlyrs70%3D 24843142
    • Ogrodnik M, Salmonowicz H, Brown R et al (2014) Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin. Proc Natl Acad Sci 111:8049-8054. doi: 10.1073/pnas.1324035111
    • (2014) Proc Natl Acad Sci , vol.111 , pp. 8049-8054
    • Ogrodnik, M.1    Salmonowicz, H.2    Brown, R.3
  • 113
    • 84866883258 scopus 로고    scopus 로고
    • Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity
    • 10.1073/pnas.1205829109 3465386 1:CAS:528:DC%2BC38XhsFGisrfM 22967507
    • Weisberg SJ, Lyakhovetsky R, Werdiger A-C et al (2012) Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity. Proc Natl Acad Sci USA 109:15811-15816. doi: 10.1073/pnas.1205829109
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 15811-15816
    • Weisberg, S.J.1    Lyakhovetsky, R.2    Werdiger, A.-C.3
  • 114
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • 2175217 1:CAS:528:DyaK1MXisFCrtA%3D%3D 9864362
    • Johnston JA, Ward CL, Kopito RR (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143:1883-1898
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 115
    • 0036733778 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin mediates the assembly of aggresomes
    • 10.1002/cm.10057 1:CAS:528:DC%2BD38Xnslenurk%3D 12211113
    • Johnston JA, Illing ME, Kopito RR (2002) Cytoplasmic dynein/dynactin mediates the assembly of aggresomes. Cell Motil Cytoskeleton 53:26-38. doi: 10.1002/cm.10057
    • (2002) Cell Motil Cytoskeleton , vol.53 , pp. 26-38
    • Johnston, J.A.1    Illing, M.E.2    Kopito, R.R.3
  • 116
    • 14044263586 scopus 로고    scopus 로고
    • Cutting edge: Microbial products elicit formation of dendritic cell aggresome-like induced structures in macrophages
    • 10.4049/jimmunol.174.5.2471 1:CAS:528:DC%2BD2MXhsFerurw%3D 15728449
    • Canadien V, Tan T, Zilber R et al (2005) Cutting edge: microbial products elicit formation of dendritic cell aggresome-like induced structures in macrophages. J Immunol 174:2471-2475. doi: 10.4049/jimmunol.174.5.2471
    • (2005) J Immunol , vol.174 , pp. 2471-2475
    • Canadien, V.1    Tan, T.2    Zilber, R.3
  • 117
    • 79251494142 scopus 로고    scopus 로고
    • Spatial protein quality control and the evolution of lineage-specific ageing
    • 10.1098/rstb.2010.0282
    • Nyström T (2010) Spatial protein quality control and the evolution of lineage-specific ageing. Philos Trans Royal Soc B Bio Sci 366:71-75. doi: 10.1098/rstb.2010.0282
    • (2010) Philos Trans Royal Soc B Bio Sci , vol.366 , pp. 71-75
    • Nyström, T.1
  • 118
    • 77955714515 scopus 로고    scopus 로고
    • Protein folding and aggregation in bacteria
    • 10.1007/s00018-010-0344-4 1:CAS:528:DC%2BC3cXpsVGisbo%3D 20358253
    • Sabate R, de Groot NS, Ventura S (2010) Protein folding and aggregation in bacteria. Cell Mol Life Sci 67:2695-2715. doi: 10.1007/s00018-010-0344-4
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2695-2715
    • Sabate, R.1    De Groot, N.S.2    Ventura, S.3
  • 119
    • 84885223714 scopus 로고    scopus 로고
    • Fission Yeast Does Not Age under Favorable Conditions, but Does so after Stress
    • 10.1016/j.cub.2013.07.084 1:CAS:528:DC%2BC3sXhsVClsrfP 24035542
    • Coelho M, Dereli A, Haese A et al (2013) Fission Yeast Does Not Age under Favorable Conditions, but Does So after Stress. Curr Biol 23:1844-1852. doi: 10.1016/j.cub.2013.07.084
    • (2013) Curr Biol , vol.23 , pp. 1844-1852
    • Coelho, M.1    Dereli, A.2    Haese, A.3
  • 120
    • 74549184412 scopus 로고    scopus 로고
    • The Polarisome Is Required for Segregation and Retrograde Transport of Protein Aggregates
    • 10.1016/j.cell.2009.12.031 1:CAS:528:DC%2BC3cXkvVWitLk%3D 20141839
    • Liu B, Larsson L, Caballero A et al (2010) The Polarisome Is Required for Segregation and Retrograde Transport of Protein Aggregates. Cell 140:257-267. doi: 10.1016/j.cell.2009.12.031
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3
  • 121
    • 69549118308 scopus 로고    scopus 로고
    • E. Coli Transports Aggregated Proteins to the Poles by a Specific and Energy-Dependent Process
    • 10.1016/j.jmb.2009.07.009 1:CAS:528:DC%2BD1MXhtV2ku73I 19596340
    • Rokney A, Shagan M, Kessel M et al (2009) E. coli Transports Aggregated Proteins to the Poles by a Specific and Energy-Dependent Process. J Mol Biol 392:589-601. doi: 10.1016/j.jmb.2009.07.009
    • (2009) J Mol Biol , vol.392 , pp. 589-601
    • Rokney, A.1    Shagan, M.2    Kessel, M.3
  • 122
    • 57749089780 scopus 로고    scopus 로고
    • Selective benefits of damage partitioning in unicellular systems and its effects on aging
    • 10.1073/pnas.0804550105 2596250 1:CAS:528:DC%2BD1cXhsV2rtL%2FP 19020097
    • Erjavec N, Cvijovic M, Klipp E, Nyström T (2008) Selective benefits of damage partitioning in unicellular systems and its effects on aging. Proc Natl Acad Sci USA 105:18764-18769. doi: 10.1073/pnas.0804550105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18764-18769
    • Erjavec, N.1    Cvijovic, M.2    Klipp, E.3    Nyström, T.4
  • 123
    • 42949100420 scopus 로고    scopus 로고
    • Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation
    • 10.1073/pnas.0708931105 2268587 1:CAS:528:DC%2BD1cXjtVSitLk%3D 18287048
    • Lindner AB, Madden R, Demarez A et al (2008) Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation. Proc Natl Acad Sci USA 105:3076-3081. doi: 10.1073/pnas.0708931105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3076-3081
    • Lindner, A.B.1    Madden, R.2    Demarez, A.3
  • 124
    • 84868149498 scopus 로고    scopus 로고
    • Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast
    • 10.1016/j.celrep.2012.08.024 1:CAS:528:DC%2BC38XhslCls73M 23022486
    • Spokoini R, Moldavski O, Nahmias Y et al (2012) Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep 2:738-747. doi: 10.1016/j.celrep.2012.08.024
    • (2012) Cell Rep , vol.2 , pp. 738-747
    • Spokoini, R.1    Moldavski, O.2    Nahmias, Y.3
  • 125
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • 10.1038/nrm3810 1:CAS:528:DC%2BC2cXosV2lurk%3D
    • Knowles TPJ, Vendruscolo M, Dobson CM (2014) The amyloid state and its association with protein misfolding diseases. Nature Publishing Group 15:384-396. doi: 10.1038/nrm3810
    • (2014) Nature Publishing Group , vol.15 , pp. 384-396
    • Knowles, T.P.J.1    Vendruscolo, M.2    Dobson, C.M.3
  • 126
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • 10.1038/nrn1007 1:CAS:528:DC%2BD3sXptlY%3D 12511861
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4:49-60. doi: 10.1038/nrn1007
    • (2003) Nat Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 127
    • 84891529441 scopus 로고    scopus 로고
    • Enhancing protein disaggregation restores proteasome activity in aged cells
    • 1:CAS:528:DC%2BC2cXntVWru7c%3D
    • Andersson V, Hanzén S, Liu B et al (2013) Enhancing protein disaggregation restores proteasome activity in aged cells. Aging (Albany NY) 5:802-812
    • (2013) Aging (Albany NY) , vol.5 , pp. 802-812
    • Andersson, V.1    Hanzén, S.2    Liu, B.3
  • 128
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in drosophila muscles regulates organism-wide proteostasis during aging
    • 10.1016/j.cell.2010.10.007 3066043 1:CAS:528:DC%2BC3cXhsVygsLfJ 21111239
    • Demontis F, Perrimon N (2010) FOXO/4E-BP signaling in drosophila muscles regulates organism-wide proteostasis during aging. Cell 143:813-825. doi: 10.1016/j.cell.2010.10.007
    • (2010) Cell , vol.143 , pp. 813-825
    • Demontis, F.1    Perrimon, N.2
  • 129
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • 10.1073/pnas.0902882106 2736453 1:CAS:528:DC%2BD1MXhtFGntr%2FL 19706382
    • Ben-Zvi A, Miller EA, Morimoto RI (2009) Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc Natl Acad Sci 106:14914-14919. doi: 10.1073/pnas.0902882106
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 130
    • 34548479261 scopus 로고    scopus 로고
    • Aging perturbs 26S proteasome assembly in Drosophila melanogaster
    • 10.1096/fj.06-6751com 3435146 1:CAS:528:DC%2BD2sXhtVehurfK 17413001
    • Vernace VA, Arnaud L, Schmidt-Glenewinkel T, Figueiredo-Pereira ME (2007) Aging perturbs 26S proteasome assembly in Drosophila melanogaster. FASEB J 21:2672-2682. doi: 10.1096/fj.06-6751com
    • (2007) FASEB J , vol.21 , pp. 2672-2682
    • Vernace, V.A.1    Arnaud, L.2    Schmidt-Glenewinkel, T.3    Figueiredo-Pereira, M.E.4
  • 131
    • 16344363800 scopus 로고    scopus 로고
    • Altered proteasome structure, function, and oxidation in aged muscle
    • (2005) Altered proteasome structure, function, and oxidation in aged muscle. 19:644-646. doi: 10.1096/fj.04-2578fje
    • (2005) , vol.19 , pp. 644-646
  • 132
    • 0034613294 scopus 로고    scopus 로고
    • Age-related Decline in Chaperone-mediated Autophagy
    • 10.1074/jbc.M002102200 1:CAS:528:DC%2BD3cXntlCitLY%3D 10806201
    • Cuervo AM, Dice JF (2000) Age-related Decline in Chaperone-mediated Autophagy. J Biol Chem 275:31505-31513. doi: 10.1074/jbc.M002102200
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 133
    • 0032860808 scopus 로고    scopus 로고
    • The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities
    • 1:STN:280:DyaK1MvisVymtA%3D%3D
    • Vittorini S, Paradiso C, Donati A et al (1999) The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities. J Gerontol Series A Bio Sci Med Sci 54:B318-B323
    • (1999) J Gerontol Series A Bio Sci Med Sci , vol.54 , pp. B318-B323
    • Vittorini, S.1    Paradiso, C.2    Donati, A.3
  • 134
    • 80053371954 scopus 로고    scopus 로고
    • Firefly luciferase mutants as sensors of proteome stress
    • 10.1038/nmeth.1697 1:CAS:528:DC%2BC3MXhtFWkurfK 21892152
    • Gupta R, Kasturi P, Bracher A et al (2011) Firefly luciferase mutants as sensors of proteome stress. Nat Methods 8:879-884. doi: 10.1038/nmeth.1697
    • (2011) Nat Methods , vol.8 , pp. 879-884
    • Gupta, R.1    Kasturi, P.2    Bracher, A.3
  • 135
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • 10.1016/j.cell.2010.11.050 1:CAS:528:DC%2BC3MXksFGisA%3D%3D 21215370
    • Olzscha H, Schermann SM, Woerner AC et al (2011) Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144:67-78. doi: 10.1016/j.cell.2010.11.050
    • (2011) Cell , vol.144 , pp. 67-78
    • Olzscha, H.1    Schermann, S.M.2    Woerner, A.C.3
  • 136
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • 10.1126/science.1124514 1:CAS:528:DC%2BD28XitVyjsb4%3D 16469881
    • Gidalevitz T, Ben-Zvi A, Ho KH et al (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311:1471-1474. doi: 10.1126/science.1124514
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3
  • 137
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
    • 10.1126/science.292.5521.1552 1:CAS:528:DC%2BD3MXktVyqs74%3D 11375494
    • Bence NF (2001) Impairment of the Ubiquitin-Proteasome System by Protein Aggregation. Science 292:1552-1555. doi: 10.1126/science.292.5521.1552
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1
  • 138
    • 84928963751 scopus 로고    scopus 로고
    • Widespread Proteome Remodeling and Aggregation in Aging C. Elegans
    • 10.1016/j.cell.2015.03.032 1:CAS:528:DC%2BC2MXotVKltbY%3D 25957690
    • Walther DM, Kasturi P, Zheng M et al (2015) Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell 161:919-932. doi: 10.1016/j.cell.2015.03.032
    • (2015) Cell , vol.161 , pp. 919-932
    • Walther, D.M.1    Kasturi, P.2    Zheng, M.3
  • 139
    • 84855823950 scopus 로고    scopus 로고
    • Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan
    • 10.1111/j.1474-9726.2011.00765.x 3437485 1:CAS:528:DC%2BC38XitVensbY%3D 22103665
    • Reis-Rodrigues P, Czerwieniec G, Peters TW et al (2012) Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan. Aging Cell 11:120-127. doi: 10.1111/j.1474-9726.2011.00765.x
    • (2012) Aging Cell , vol.11 , pp. 120-127
    • Reis-Rodrigues, P.1    Czerwieniec, G.2    Peters, T.W.3
  • 140
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C. Elegans
    • 10.1371/journal.pbio.1000450 2919420 20711477
    • David DC, Ollikainen N, Trinidad JC et al (2010) Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol 8:e1000450. doi: 10.1371/journal.pbio.1000450
    • (2010) PLoS Biol , vol.8 , pp. e1000450
    • David, D.C.1    Ollikainen, N.2    Trinidad, J.C.3
  • 141
    • 84878873344 scopus 로고    scopus 로고
    • Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid
    • 10.1007/s00401-013-1089-6 3593646 23378033
    • Bigio EH, Wu JY, Deng H-X et al (2013) Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid. Acta Neuropathol 125:463-465. doi: 10.1007/s00401-013-1089-6
    • (2013) Acta Neuropathol , vol.125 , pp. 463-465
    • Bigio, E.H.1    Wu, J.Y.2    Deng, H.-X.3
  • 142
    • 80052942395 scopus 로고    scopus 로고
    • A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies
    • 10.1093/brain/awr160 3170529 21752791
    • Lashley T, Rohrer JD, Bandopadhyay R et al (2011) A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies. Brain 134:2548-2564. doi: 10.1093/brain/awr160
    • (2011) Brain , vol.134 , pp. 2548-2564
    • Lashley, T.1    Rohrer, J.D.2    Bandopadhyay, R.3
  • 143
    • 84887903154 scopus 로고    scopus 로고
    • Modelling FUSopathies: Focus on protein aggregation
    • 10.1042/BST20130212 1:CAS:528:DC%2BC3sXhvVSmtbzL 24256263
    • Shelkovnikova TA (2013) Modelling FUSopathies: focus on protein aggregation. Biochem Soc Trans 41:1613-1617. doi: 10.1042/BST20130212
    • (2013) Biochem Soc Trans , vol.41 , pp. 1613-1617
    • Shelkovnikova, T.A.1
  • 144
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • 10.1038/nrm2101 1:CAS:528:DC%2BD2sXotFKmtw%3D%3D 17245412
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8:101-112. doi: 10.1038/nrm2101
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 146
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • 10.1146/annurev.biochem.75.101304.123901 1:CAS:528:DC%2BD28XosVKhs70%3D 16756495
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. doi: 10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 147
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • 10.1096/fj.03-1072fje
    • De Felice FG (2004) Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. FASEB J. doi: 10.1096/fj.03-1072fje
    • (2004) FASEB J
    • De Felice, F.G.1
  • 148
    • 0141746349 scopus 로고    scopus 로고
    • The role of protein stability, solubility, and net charge in amyloid fibril formation
    • 10.1110/ps.03152903 2366926 1:CAS:528:DC%2BD3sXnslKlsb8%3D 14500896
    • Schmittschmitt JP, Scholtz JM (2003) The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Sci 12:2374-2378. doi: 10.1110/ps.03152903
    • (2003) Protein Sci , vol.12 , pp. 2374-2378
    • Schmittschmitt, J.P.1    Scholtz, J.M.2
  • 149
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • 10.1038/35065514 11242064
    • Fändrich M, Fletcher MA, Dobson CM (2001) Amyloid fibrils from muscle myoglobin. Nature 410:165-166. doi: 10.1038/35065514
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 150
    • 0034612254 scopus 로고    scopus 로고
    • The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state
    • 18622 10841549
    • Ferrão-Gonzales AD, Souto SO, Silva JL, Foguel D (2000) The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc Natl Acad Sci 97:6445-6450
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6445-6450
    • Ferrão-Gonzales, A.D.1    Souto, S.O.2    Silva, J.L.3    Foguel, D.4
  • 151
    • 0034254241 scopus 로고    scopus 로고
    • Partially Unfolded States of β 2-Microglobulin and Amyloid Formation in Vitro
    • 10.1021/bi000276j 1:CAS:528:DC%2BD3cXksVagtLc%3D 10913285
    • McParland VJ, Kad NM, Kalverda AP et al (2000) Partially Unfolded States of β 2-Microglobulin and Amyloid Formation in Vitro. Biochemistry 39:8735-8746. doi: 10.1021/bi000276j
    • (2000) Biochemistry , vol.39 , pp. 8735-8746
    • McParland, V.J.1    Kad, N.M.2    Kalverda, A.P.3
  • 152
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • 22338 1:CAS:528:DyaK1MXjslCitb4%3D 10097081
    • Chiti F, Webster P, Taddei N et al (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci 96:3590-3594
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3
  • 153
    • 13144259646 scopus 로고    scopus 로고
    • Amyloid fibril formation by an SH3 domain
    • 22470 1:CAS:528:DyaK1cXis1OhtLw%3D 9539718
    • Guijarro JI, Sunde M, Jones JA et al (1998) Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci 95:4224-4228
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 4224-4228
    • Guijarro, J.I.1    Sunde, M.2    Jones, J.A.3
  • 154
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • 10.1006/jmbi.1998.1863 1:CAS:528:DyaK1cXkslCksr8%3D 9654449
    • Litvinovich SV, Brew SA, Aota S et al (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J Mol Biol 280:245-258. doi: 10.1006/jmbi.1998.1863
    • (1998) J Mol Biol , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3
  • 155
    • 77649265357 scopus 로고    scopus 로고
    • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
    • 10.1038/nmeth.1432 1:CAS:528:DC%2BC3cXhvFGmsbw%3D 20154676
    • Maurer-Stroh S, Debulpaep M, Kuemmerer N et al (2010) Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat Methods 7:237-242. doi: 10.1038/nmeth.1432
    • (2010) Nat Methods , vol.7 , pp. 237-242
    • Maurer-Stroh, S.1    Debulpaep, M.2    Kuemmerer, N.3
  • 156
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • 10.1038/nbt1012 1:CAS:528:DC%2BD2cXotFGqtb8%3D 15361882
    • Fernandez-Escamilla A-M, Rousseau F, Schymkowitz J, Serrano L (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22:1302-1306. doi: 10.1038/nbt1012
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 157
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • 10.1038/416535a 1:CAS:528:DC%2BD38XivVOntL8%3D 11932745
    • Walsh DM, Klyubin I, Fadeeva JV et al (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416:535-539. doi: 10.1038/416535a
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 158
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta 1-42 are potent central nervous system neurotoxins
    • 27787 1:STN:280:DyaK1c3mtlektQ%3D%3D 9600986
    • Lambert MP, Barlow AK, Chromy BA et al (1998) Diffusible, nonfibrillar ligands derived from Abeta 1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci 95:6448-6453
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 159
    • 0029671451 scopus 로고    scopus 로고
    • Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains
    • 1:CAS:528:DyaK28XhtlSmsL8%3D 8626743
    • Kuo YM, Emmerling MR, Vigo-Pelfrey C et al (1996) Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J Biol Chem 271:4077-4081
    • (1996) J Biol Chem , vol.271 , pp. 4077-4081
    • Kuo, Y.M.1    Emmerling, M.R.2    Vigo-Pelfrey, C.3
  • 160
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • 10.1074/jbc.274.36.25945 1:CAS:528:DyaK1MXmtVWht70%3D 10464339
    • Walsh DM, Hartley DM, Kusumoto Y et al (1999) Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 274:25945-25952. doi: 10.1074/jbc.274.36.25945
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3
  • 161
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • 1:CAS:528:DyaK2sXlslOku74%3D 9268388
    • Walsh DM, Lomakin A, Benedek GB et al (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 272:22364-22372
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3
  • 162
    • 81355160169 scopus 로고    scopus 로고
    • Identifying polyglutamine protein species in situ that best predict neurodegeneration
    • 10.1038/nchembio.694 3271120 1:CAS:528:DC%2BC3MXhtlyisrfE 22037470
    • Miller J, Arrasate M, Brooks E et al (2011) Identifying polyglutamine protein species in situ that best predict neurodegeneration. Nat Chem Biol 7:925-934. doi: 10.1038/nchembio.694
    • (2011) Nat Chem Biol , vol.7 , pp. 925-934
    • Miller, J.1    Arrasate, M.2    Brooks, E.3
  • 164
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • 10.1038/nature02998 1:CAS:528:DC%2BD2cXotl2ktrc%3D 15483602
    • Arrasate M, Mitra S, Schweitzer ES et al (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805-810. doi: 10.1038/nature02998
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3
  • 165
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 10.1126/science.1079469 1:CAS:528:DC%2BD3sXivFyms7k%3D 12702875
    • Kayed R, Head E, Thompson JL et al (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489. doi: 10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 166
    • 84907938241 scopus 로고    scopus 로고
    • Antibodies and protein misfolding: From structural research tools to therapeutic strategies
    • 10.1016/j.bbapap.2014.08.016 25194824
    • De Genst E, Messer A, Dobson CM (2014) Antibodies and protein misfolding: from structural research tools to therapeutic strategies. BBA - Proteins and Proteomics 1844:1907-1919. doi: 10.1016/j.bbapap.2014.08.016
    • (2014) BBA - Proteins and Proteomics , vol.1844 , pp. 1907-1919
    • De Genst, E.1    Messer, A.2    Dobson, C.M.3
  • 167
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • 10.1038/nn.3028 1:CAS:528:DC%2BC38XhtlOltrc%3D 22286176
    • Benilova I, Karran E, De Strooper B (2012) The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 15:349-357. doi: 10.1038/nn.3028
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 168
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • 10.1017/S0033583506004422 1:CAS:528:DC%2BD28XhtFKku7nM 16978447
    • Lashuel HA, Lansbury PT (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39:167-201. doi: 10.1017/S0033583506004422
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 169
    • 84858046578 scopus 로고    scopus 로고
    • Neuropathological alterations in Alzheimer disease
    • 10.1101/cshperspect.a006189 3234452 22229116
    • Serrano-Pozo A, Frosch MP, Masliah E, Hyman BT (2011) Neuropathological alterations in Alzheimer disease. Cold Spring Harb Perspect Med 1:a006189. doi: 10.1101/cshperspect.a006189
    • (2011) Cold Spring Harb Perspect Med , vol.1 , pp. a006189
    • Serrano-Pozo, A.1    Frosch, M.P.2    Masliah, E.3    Hyman, B.T.4
  • 170
    • 77953667076 scopus 로고    scopus 로고
    • Neurodegenerative diseases: Lessons from genome-wide screens in small model organisms
    • 10.1002/emmm.200900051 3378155 20049741
    • van Ham TJ, Breitling R, Swertz MA, Nollen EAA (2009) Neurodegenerative diseases: lessons from genome-wide screens in small model organisms. EMBO Mol Med 1:360-370. doi: 10.1002/emmm.200900051
    • (2009) EMBO Mol Med , vol.1 , pp. 360-370
    • Van Ham, T.J.1    Breitling, R.2    Swertz, M.A.3    Nollen, E.A.A.4
  • 171
    • 41549104948 scopus 로고    scopus 로고
    • Yeast as a model for studying human neurodegenerative disorders
    • 10.1002/biot.200700217 1:CAS:528:DC%2BD1cXkt1Cls7k%3D 18228539
    • Miller-Fleming L, Giorgini F, Outeiro TF (2008) Yeast as a model for studying human neurodegenerative disorders. Biotechnol J 3:325-338. doi: 10.1002/biot.200700217
    • (2008) Biotechnol J , vol.3 , pp. 325-338
    • Miller-Fleming, L.1    Giorgini, F.2    Outeiro, T.F.3
  • 172
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy bodies
    • 10.1038/42166 1:CAS:528:DyaK2sXlslWru7o%3D 9278044
    • Spillantini MG, Schmidt ML, Lee VM et al (1997) Alpha-synuclein in Lewy bodies. Nature 388:839-840. doi: 10.1038/42166
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1    Schmidt, M.L.2    Lee, V.M.3
  • 173
    • 84989160282 scopus 로고    scopus 로고
    • Alpha-synuclein biology in Lewy body diseases
    • 10.1186/s13195-014-0073-2 4288216 25580161
    • Kim WS, Kågedal K, Halliday GM (2014) Alpha-synuclein biology in Lewy body diseases. Alzheimers Res Ther 6:73. doi: 10.1186/s13195-014-0073-2
    • (2014) Alzheimers Res Ther , vol.6 , pp. 73
    • Kim, W.S.1    Kågedal, K.2    Halliday, G.M.3
  • 174
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • 10.1126/science.1090439 1780172 1:CAS:528:DC%2BD3sXpsVWns74%3D 14657500
    • Outeiro TF, Lindquist S (2003) Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302:1772-1775. doi: 10.1126/science.1090439
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 175
    • 46549089111 scopus 로고    scopus 로고
    • Protein folding diseases and neurodegeneration: Lessons learned from yeast
    • 10.1016/j.bbamcr.2008.01.020 1:CAS:528:DC%2BD1cXnt1Ojtbo%3D 18298958
    • Winderickx J, Delay C, De Vos A et al (2008) Protein folding diseases and neurodegeneration: lessons learned from yeast. Biochim Biophys Acta 1783:1381-1395. doi: 10.1016/j.bbamcr.2008.01.020
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1381-1395
    • Winderickx, J.1    Delay, C.2    De Vos, A.3
  • 176
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • 10.1126/science.1129462 1983366 1:CAS:528:DC%2BD28XmvFyqtr8%3D 16794039
    • Cooper AA, Gitler AD, Cashikar A et al (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313:324-328. doi: 10.1126/science.1129462
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3
  • 177
    • 61349147706 scopus 로고    scopus 로고
    • Alpha-Synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity
    • 10.1038/ng.300 2683786 1:CAS:528:DC%2BD1MXht1ehsbk%3D 19182805
    • Gitler AD, Chesi A, Geddie ML et al (2009) Alpha-Synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41:308-315. doi: 10.1038/ng.300
    • (2009) Nat Genet , vol.41 , pp. 308-315
    • Gitler, A.D.1    Chesi, A.2    Geddie, M.L.3
  • 178
    • 84858785513 scopus 로고    scopus 로고
    • The role of the Parkinson's disease gene PARK9 in essential cellular pathways and the manganese homeostasis network in yeast
    • 10.1371/journal.pone.0034178 3311584 1:CAS:528:DC%2BC38XltF2kt7Y%3D 22457822
    • Chesi A, Kilaru A, Fang X et al (2012) The role of the Parkinson's disease gene PARK9 in essential cellular pathways and the manganese homeostasis network in yeast. PLoS One 7:e34178. doi: 10.1371/journal.pone.0034178
    • (2012) PLoS One , vol.7 , pp. e34178
    • Chesi, A.1    Kilaru, A.2    Fang, X.3
  • 179
    • 52949083619 scopus 로고    scopus 로고
    • A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in alpha-synuclein transgenic C. Elegans
    • 10.1093/hmg/ddn198 1:CAS:528:DC%2BD1cXhtFCisLzN 18617532
    • Kuwahara T, Koyama A, Koyama S et al (2008) A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in alpha-synuclein transgenic C. elegans. Hum Mol Genet 17:2997-3009. doi: 10.1093/hmg/ddn198
    • (2008) Hum Mol Genet , vol.17 , pp. 2997-3009
    • Kuwahara, T.1    Koyama, A.2    Koyama, S.3
  • 180
    • 41949097891 scopus 로고    scopus 로고
    • C. Elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging
    • 10.1371/journal.pgen.1000027 2265412 18369446
    • van Ham TJ, Thijssen KL, Breitling R et al (2008) C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. PLoS Genet 4:e1000027. doi: 10.1371/journal.pgen.1000027
    • (2008) PLoS Genet , vol.4 , pp. e1000027
    • Van Ham, T.J.1    Thijssen, K.L.2    Breitling, R.3
  • 181
    • 38649084391 scopus 로고    scopus 로고
    • Hypothesis-based RNAi screening identifies neuroprotective genes in a Parkinson's disease model
    • 10.1073/pnas.0711018105 2206604 1:CAS:528:DC%2BD1cXpvFelsw%3D%3D 18182484
    • Hamamichi S, Rivas RN, Knight AL et al (2008) Hypothesis-based RNAi screening identifies neuroprotective genes in a Parkinson's disease model. Proc Natl Acad Sci USA 105:728-733. doi: 10.1073/pnas.0711018105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 728-733
    • Hamamichi, S.1    Rivas, R.N.2    Knight, A.L.3
  • 182
    • 84866297918 scopus 로고    scopus 로고
    • Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation
    • 10.1073/pnas.1203083109 3443121 22927396
    • van der Goot AT, Zhu W, Vazquez-Manrique RP et al (2012) Delaying aging and the aging-associated decline in protein homeostasis by inhibition of tryptophan degradation. Proc Natl Acad Sci USA 109:14912-14917. doi: 10.1073/pnas.1203083109
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 14912-14917
    • Van Der Goot, A.T.1    Zhu, W.2    Vazquez-Manrique, R.P.3
  • 183
    • 35448938087 scopus 로고    scopus 로고
    • Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration
    • 10.1073/pnas.0701311104 1964831 1:CAS:528:DC%2BD2sXhtVGnt7bK 17726112
    • Komatsu M, Wang QJ, Holstein GR et al (2007) Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration. Proc Natl Acad Sci 104:14489-14494. doi: 10.1073/pnas.0701311104
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 14489-14494
    • Komatsu, M.1    Wang, Q.J.2    Holstein, G.R.3
  • 184
    • 79952747862 scopus 로고    scopus 로고
    • Alzheimer's disease
    • 10.1016/S0140-6736(10)61349-9 21371747
    • Ballard C, Gauthier S, Corbett A et al (2011) Alzheimer's disease. Lancet 377:1019-1031. doi: 10.1016/S0140-6736(10)61349-9
    • (2011) Lancet , vol.377 , pp. 1019-1031
    • Ballard, C.1    Gauthier, S.2    Corbett, A.3
  • 185
    • 68949150683 scopus 로고    scopus 로고
    • Amyloid-beta, tau, and dementia
    • 10.3233/JAD-2009-1090 1:CAS:528:DC%2BD1MXptVChsbY%3D 19542626
    • Takashima A (2009) Amyloid-beta, tau, and dementia. J Alzheimers Dis 17:729-736. doi: 10.3233/JAD-2009-1090
    • (2009) J Alzheimers Dis , vol.17 , pp. 729-736
    • Takashima, A.1
  • 186
    • 84870796993 scopus 로고    scopus 로고
    • Genetic insights in Alzheimer's disease
    • 10.1016/S1474-4422(12)70259-4 1:CAS:528:DC%2BC38XhvVCksL%2FI 23237904
    • Bettens K, Sleegers K, Van Broeckhoven C (2013) Genetic insights in Alzheimer's disease. Lancet Neurol 12:92-104. doi: 10.1016/S1474-4422(12)70259-4
    • (2013) Lancet Neurol , vol.12 , pp. 92-104
    • Bettens, K.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 187
    • 62449083712 scopus 로고    scopus 로고
    • Association of FOXO3A variation with human longevity confirmed in German centenarians
    • 10.1073/pnas.0809594106 2650329 1:CAS:528:DC%2BD1MXislahsbs%3D 19196970
    • Flachsbart F, Caliebe A, Kleindorp R et al (2009) Association of FOXO3A variation with human longevity confirmed in German centenarians. Proc Natl Acad Sci USA 106:2700-2705. doi: 10.1073/pnas.0809594106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2700-2705
    • Flachsbart, F.1    Caliebe, A.2    Kleindorp, R.3
  • 188
    • 42149141146 scopus 로고    scopus 로고
    • Functionally significant insulin-like growth factor I receptor mutations in centenarians
    • 10.1073/pnas.0705467105 2265137 1:CAS:528:DC%2BD1cXjtlKktL4%3D 18316725
    • Suh Y, Atzmon G, Cho M-O et al (2008) Functionally significant insulin-like growth factor I receptor mutations in centenarians. Proc Natl Acad Sci 105:3438-3442. doi: 10.1073/pnas.0705467105
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 3438-3442
    • Suh, Y.1    Atzmon, G.2    Cho, M.-O.3
  • 189
    • 52949122885 scopus 로고    scopus 로고
    • FOXO3A genotype is strongly associated with human longevity
    • 10.1073/pnas.0801030105 2544566 1:CAS:528:DC%2BD1cXhtFKiurfK 18765803
    • Willcox BJ, Donlon TA, He Q et al (2008) FOXO3A genotype is strongly associated with human longevity. Proc Natl Acad Sci USA 105:13987-13992. doi: 10.1073/pnas.0801030105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13987-13992
    • Willcox, B.J.1    Donlon, T.A.2    He, Q.3
  • 190
    • 0037942739 scopus 로고    scopus 로고
    • Extended longevity in mice lacking the insulin receptor in adipose tissue
    • 10.1126/science.1078223 12543978
    • Blüher M, Kahn BB, Kahn CR (2003) Extended longevity in mice lacking the insulin receptor in adipose tissue. Science 299:572-574. doi: 10.1126/science.1078223
    • (2003) Science , vol.299 , pp. 572-574
    • Blüher, M.1    Kahn, B.B.2    Kahn, C.R.3
  • 191
    • 0347664057 scopus 로고    scopus 로고
    • IGF-1 receptor regulates lifespan and resistance to oxidative stress in mice
    • 10.1038/nature01298 1:CAS:528:DC%2BD3sXhs1KhtA%3D%3D 12483226
    • Holzenberger M, Dupont J, Ducos B et al (2003) IGF-1 receptor regulates lifespan and resistance to oxidative stress in mice. Nature 421:182-187. doi: 10.1038/nature01298
    • (2003) Nature , vol.421 , pp. 182-187
    • Holzenberger, M.1    Dupont, J.2    Ducos, B.3
  • 192
    • 0035815445 scopus 로고    scopus 로고
    • A mutant drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function
    • 10.1126/science.1057987 1:CAS:528:DC%2BD3MXis1Grt74%3D 11292875
    • Tatar M (2001) A mutant drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science 292:107-110. doi: 10.1126/science.1057987
    • (2001) Science , vol.292 , pp. 107-110
    • Tatar, M.1
  • 193
    • 0027771804 scopus 로고
    • A C. Elegans mutant that lives twice as long as wild type
    • 10.1038/366461a0 1:STN:280:DyaK2c%2FmslensQ%3D%3D 8247153
    • Kenyon C, Chang J, Gensch E et al (1993) A C. elegans mutant that lives twice as long as wild type. Nature 366:461-464. doi: 10.1038/366461a0
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3
  • 194
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • 40986 1:CAS:528:DyaK2MXosVWluro%3D 7568134
    • Link CD (1995) Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc Natl Acad Sci 92:9368-9372
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 195
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • 10.1126/science.1124646 1:CAS:528:DC%2BD28XpsVOktbk%3D 16902091
    • Cohen E, Bieschke J, Perciavalle RM et al (2006) Opposing activities protect against age-onset proteotoxicity. Science 313:1604-1610. doi: 10.1126/science.1124646
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3
  • 196
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • 10.1126/science.1083701 1:CAS:528:DC%2BD3sXjslGqtr0%3D 12750521
    • Hsu A-L, Murphy CT, Kenyon C (2003) Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 300:1142-1145. doi: 10.1126/science.1083701
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.-L.1    Murphy, C.T.2    Kenyon, C.3
  • 197
    • 71449108913 scopus 로고    scopus 로고
    • Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
    • 10.1016/j.cell.2009.11.014 3017511 1:CAS:528:DC%2BC3cXhslartrk%3D 20005808
    • Cohen E, Paulsson JF, Blinder P et al (2009) Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 139:1157-1169. doi: 10.1016/j.cell.2009.11.014
    • (2009) Cell , vol.139 , pp. 1157-1169
    • Cohen, E.1    Paulsson, J.F.2    Blinder, P.3
  • 198
    • 82755197062 scopus 로고    scopus 로고
    • Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast
    • 10.1126/science.1213210 3281757 1:CAS:528:DC%2BC3MXhsFCms7nE 22033521
    • Treusch S, Hamamichi S, Goodman JL et al (2011) Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science 334:1241-1245. doi: 10.1126/science.1213210
    • (2011) Science , vol.334 , pp. 1241-1245
    • Treusch, S.1    Hamamichi, S.2    Goodman, J.L.3
  • 199
    • 79851507672 scopus 로고    scopus 로고
    • Functional screening of Alzheimer pathology genome-wide association signals in Drosophila
    • 10.1016/j.ajhg.2011.01.006 3035702 1:CAS:528:DC%2BC3MXhvFKgtb0%3D 21295279
    • Shulman JM, Chipendo P, Chibnik LB et al (2011) Functional screening of Alzheimer pathology genome-wide association signals in Drosophila. Am J Hum Genet 88:232-238. doi: 10.1016/j.ajhg.2011.01.006
    • (2011) Am J Hum Genet , vol.88 , pp. 232-238
    • Shulman, J.M.1    Chipendo, P.2    Chibnik, L.B.3
  • 200
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • 10.1073/pnas.152161099 124929 12122205
    • Morley JF, Brignull HR, Weyers JJ, Morimoto RI (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci 99:10417-10422. doi: 10.1073/pnas.152161099
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 201
    • 84855258498 scopus 로고    scopus 로고
    • A genetic screening strategy identifies novel regulators of the proteostasis network
    • 10.1371/journal.pgen.1002438 3248563 1:CAS:528:DC%2BC38Xms1Omsg%3D%3D 22242008
    • Silva MC, Fox S, Beam M et al (2011) A genetic screening strategy identifies novel regulators of the proteostasis network. PLoS Genet 7:e1002438. doi: 10.1371/journal.pgen.1002438
    • (2011) PLoS Genet , vol.7 , pp. e1002438
    • Silva, M.C.1    Fox, S.2    Beam, M.3
  • 202
    • 2342652188 scopus 로고    scopus 로고
    • Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation
    • 10.1073/pnas.0307697101 404057 1:CAS:528:DC%2BD2cXjvVyit7s%3D 15084750
    • Nollen EAA, Garcia SM, van Haaften G et al (2004) Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation. Proc Natl Acad Sci 101:6403-6408. doi: 10.1073/pnas.0307697101
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 6403-6408
    • Nollen, E.A.A.1    Garcia, S.M.2    Van Haaften, G.3
  • 203
    • 77955647865 scopus 로고    scopus 로고
    • Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity
    • 10.1016/j.cell.2010.07.020 20723760
    • van Ham TJ, Holmberg MA, van der Goot AT et al (2010) Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity. Cell 142:601-612. doi: 10.1016/j.cell.2010.07.020
    • (2010) Cell , vol.142 , pp. 601-612
    • Van Ham, T.J.1    Holmberg, M.A.2    Van Der Goot, A.T.3
  • 204
    • 84865722715 scopus 로고    scopus 로고
    • SERF protein is a direct modifier of amyloid fiber assembly
    • 10.1016/j.celrep.2012.06.012 3807654 1:CAS:528:DC%2BC38XhtlCjsrzM 22854022
    • Falsone SF, Meyer NH, Schrank E et al (2012) SERF protein is a direct modifier of amyloid fiber assembly. Cell Rep 2:358-371. doi: 10.1016/j.celrep.2012.06.012
    • (2012) Cell Rep , vol.2 , pp. 358-371
    • Falsone, S.F.1    Meyer, N.H.2    Schrank, E.3
  • 205
    • 84857989952 scopus 로고    scopus 로고
    • Large-scale functional RNAi screen in C. Elegans identifies genes that regulate the dysfunction of mutant polyglutamine neurons
    • 10.1186/1471-2164-13-91 1:CAS:528:DC%2BC38Xot12rtr4%3D
    • Lejeune F-X, Mesrob L, Parmentier F et al (2012) Large-scale functional RNAi screen in C. elegans identifies genes that regulate the dysfunction of mutant polyglutamine neurons. BMC Genom 13:91. doi: 10.1186/1471-2164-13-91
    • (2012) BMC Genom , vol.13 , pp. 91
    • Lejeune, F.-X.1    Mesrob, L.2    Parmentier, F.3
  • 206
    • 33748561495 scopus 로고    scopus 로고
    • Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    • 10.1016/j.molcel.2006.08.017 1:CAS:528:DC%2BD28XhtVKgu7zP 16973440
    • Behrends C, Langer CA, Boteva R et al (2006) Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23:887-897. doi: 10.1016/j.molcel.2006.08.017
    • (2006) Mol Cell , vol.23 , pp. 887-897
    • Behrends, C.1    Langer, C.A.2    Boteva, R.3
  • 207
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • 10.1038/ncb1477 2829982 1:CAS:528:DC%2BD28XhtVWqsLbE 16980959
    • Tam S, Geller R, Spiess C, Frydman J (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8:1155-1162. doi: 10.1038/ncb1477
    • (2006) Nat Cell Biol , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 208
    • 18144406846 scopus 로고    scopus 로고
    • A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease
    • 10.1038/ng1542 1449881 1:CAS:528:DC%2BD2MXjsF2ksrs%3D 15806102
    • Giorgini F, Guidetti P, Nguyen Q et al (2005) A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet 37:526-531. doi: 10.1038/ng1542
    • (2005) Nat Genet , vol.37 , pp. 526-531
    • Giorgini, F.1    Guidetti, P.2    Nguyen, Q.3
  • 209
    • 79958044624 scopus 로고    scopus 로고
    • The kynurenine pathway modulates neurodegeneration in a Drosophila model of Huntington's disease
    • 10.1016/j.cub.2011.04.028 3929356 1:CAS:528:DC%2BC3MXntFKmtr8%3D 21636279
    • Campesan S, Green EW, Breda C et al (2011) The kynurenine pathway modulates neurodegeneration in a Drosophila model of Huntington's disease. Curr Biol 21:961-966. doi: 10.1016/j.cub.2011.04.028
    • (2011) Curr Biol , vol.21 , pp. 961-966
    • Campesan, S.1    Green, E.W.2    Breda, C.3
  • 210
    • 79958021894 scopus 로고    scopus 로고
    • Kynurenine 3-monooxygenase inhibition in blood ameliorates neurodegeneration
    • 10.1016/j.cell.2011.05.020 3118409 1:CAS:528:DC%2BC3MXnsVOkt74%3D 21640374
    • Zwilling D, Huang S-Y, Sathyasaikumar KV et al (2011) Kynurenine 3-monooxygenase inhibition in blood ameliorates neurodegeneration. Cell 145:863-874. doi: 10.1016/j.cell.2011.05.020
    • (2011) Cell , vol.145 , pp. 863-874
    • Zwilling, D.1    Huang, S.-Y.2    Sathyasaikumar, K.V.3
  • 211
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • 10.1038/35057062 1:CAS:528:DC%2BD3MXhsFCjtLc%3D 11237011
    • Lander ES, Linton LM, Birren B et al (2001) Initial sequencing and analysis of the human genome. Nature 409:860-921. doi: 10.1038/35057062
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1    Linton, L.M.2    Birren, B.3
  • 212
    • 37648999313 scopus 로고    scopus 로고
    • Distinguishing protein-coding and noncoding genes in the human genome
    • 10.1073/pnas.0709013104 2148306 1:CAS:528:DC%2BD1cXisVOiuw%3D%3D 18040051
    • Clamp M, Fry B, Kamal M et al (2007) Distinguishing protein-coding and noncoding genes in the human genome. Proc Natl Acad Sci USA 104:19428-19433. doi: 10.1073/pnas.0709013104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19428-19433
    • Clamp, M.1    Fry, B.2    Kamal, M.3
  • 213
    • 1542563409 scopus 로고    scopus 로고
    • Initial sequencing and comparative analysis of the mouse genome
    • Mouse Genome Sequencing Consortium, Waterston RH, Lindblad-Toh K, et al 10.1038/nature01262
    • Mouse Genome Sequencing Consortium, Waterston RH, Lindblad-Toh K et al (2002) Initial sequencing and comparative analysis of the mouse genome. Nature 420:520-562. doi: 10.1038/nature01262
    • (2002) Nature , vol.420 , pp. 520-562
  • 214
    • 84865790047 scopus 로고    scopus 로고
    • An integrated encyclopedia of DNA elements in the human genome
    • ENCODE Project Consortium 10.1038/nature11247
    • ENCODE Project Consortium (2012) An integrated encyclopedia of DNA elements in the human genome. Nature 489:57-74. doi: 10.1038/nature11247
    • (2012) Nature , vol.489 , pp. 57-74
  • 215
    • 34250160256 scopus 로고    scopus 로고
    • RNA Maps Reveal New RNA Classes and a Possible Function for Pervasive Transcription
    • 10.1126/science.1138341 1:CAS:528:DC%2BD2sXmtFSjtrw%3D 17510325
    • Kapranov P, Cheng J, Dike S et al (2007) RNA Maps Reveal New RNA Classes and a Possible Function for Pervasive Transcription. Science 316:1484-1488. doi: 10.1126/science.1138341
    • (2007) Science , vol.316 , pp. 1484-1488
    • Kapranov, P.1    Cheng, J.2    Dike, S.3
  • 216
    • 24644519490 scopus 로고    scopus 로고
    • The transcriptional landscape of the mammalian genome
    • 10.1126/science.1112014 1:CAS:528:DC%2BD2MXpsFWju7o%3D 16141072
    • Carninci P, Kasukawa T, Katayama S et al (2005) The transcriptional landscape of the mammalian genome. Science 309:1559-1563. doi: 10.1126/science.1112014
    • (2005) Science , vol.309 , pp. 1559-1563
    • Carninci, P.1    Kasukawa, T.2    Katayama, S.3
  • 217
    • 84897128298 scopus 로고    scopus 로고
    • The Noncoding RNA Revolution - Trashing Old Rules to Forge New Ones
    • 10.1016/j.cell.2014.03.008 1:CAS:528:DC%2BC2cXmtVCktLo%3D 24679528
    • Cech TR, Steitz JA (2014) The Noncoding RNA Revolution - Trashing Old Rules to Forge New Ones. Cell 157:77-94. doi: 10.1016/j.cell.2014.03.008
    • (2014) Cell , vol.157 , pp. 77-94
    • Cech, T.R.1    Steitz, J.A.2
  • 218
    • 78650292831 scopus 로고    scopus 로고
    • The majority of total nuclear-encoded non-ribosomal RNA in a human cell is "dark matter" un-annotated RNA
    • 10.1186/1741-7007-8-149 3022773 1:CAS:528:DC%2BC3MXisFWquw%3D%3D 21176148
    • Kapranov P, Laurent GS, Raz T et al (2010) The majority of total nuclear-encoded non-ribosomal RNA in a human cell is "dark matter" un-annotated RNA. BMC Biol 8:149. doi: 10.1186/1741-7007-8-149
    • (2010) BMC Biol , vol.8 , pp. 149
    • Kapranov, P.1    Laurent, G.S.2    Raz, T.3
  • 219
    • 84885808774 scopus 로고    scopus 로고
    • RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention
    • 10.1016/j.neuron.2013.10.015 4098943 1:CAS:528:DC%2BC3sXhs1CrurfK 24139042
    • Donnelly CJ, Zhang P-W, Pham JT et al (2013) RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention. Neuron 80:415-428. doi: 10.1016/j.neuron.2013.10.015
    • (2013) Neuron , vol.80 , pp. 415-428
    • Donnelly, C.J.1    Zhang, P.-W.2    Pham, J.T.3
  • 220
    • 0034282958 scopus 로고    scopus 로고
    • Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy
    • 10.1093/emboj/19.17.4439 302046 1:CAS:528:DC%2BD3cXmslGktbk%3D 10970838
    • Miller JW, Urbinati CR, Teng-Umnuay P et al (2000) Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy. EMBO J 19:4439-4448. doi: 10.1093/emboj/19.17.4439
    • (2000) EMBO J , vol.19 , pp. 4439-4448
    • Miller, J.W.1    Urbinati, C.R.2    Teng-Umnuay, P.3
  • 221
    • 77955902024 scopus 로고    scopus 로고
    • The widespread regulation of microRNA biogenesis, function and decay
    • 10.1038/nrg2843 1:CAS:528:DC%2BC3cXhtVCnurzF 20661255
    • Krol J, Loedige I, Filipowicz W (2010) The widespread regulation of microRNA biogenesis, function and decay. Nat Rev Genet 11:597-610. doi: 10.1038/nrg2843
    • (2010) Nat Rev Genet , vol.11 , pp. 597-610
    • Krol, J.1    Loedige, I.2    Filipowicz, W.3
  • 222
    • 40449124713 scopus 로고    scopus 로고
    • MicroRNA expression in the adult mouse central nervous system
    • 10.1261/rna.783108 2248253 1:CAS:528:DC%2BD1cXivFaqs7g%3D 18230762
    • Bak M, Silahtaroglu A, Moller M et al (2008) MicroRNA expression in the adult mouse central nervous system. RNA 14:432-444. doi: 10.1261/rna.783108
    • (2008) RNA , vol.14 , pp. 432-444
    • Bak, M.1    Silahtaroglu, A.2    Moller, M.3
  • 223
    • 38649114329 scopus 로고    scopus 로고
    • Specific expression of long noncoding RNAs in the mouse brain
    • 10.1073/pnas.0706729105 2206602 1:CAS:528:DC%2BD1cXpvFeitg%3D%3D 18184812
    • Mercer TR, Dinger ME, Sunkin SM et al (2008) Specific expression of long noncoding RNAs in the mouse brain. Proc Natl Acad Sci USA 105:716-721. doi: 10.1073/pnas.0706729105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 716-721
    • Mercer, T.R.1    Dinger, M.E.2    Sunkin, S.M.3
  • 224
    • 38349114827 scopus 로고    scopus 로고
    • MicroRNAs show a wide diversity of expression profiles in the developing and mature central nervous system
    • 10.1186/gb-2007-8-8-r173 2375003 17711588
    • Kapsimali M, Kloosterman WP, de Bruijn E et al (2007) MicroRNAs show a wide diversity of expression profiles in the developing and mature central nervous system. Genome Biol 8:R173. doi: 10.1186/gb-2007-8-8-r173
    • (2007) Genome Biol , vol.8 , pp. R173
    • Kapsimali, M.1    Kloosterman, W.P.2    De Bruijn, E.3
  • 225
    • 34147157651 scopus 로고    scopus 로고
    • The microRNA miR-124 antagonizes the anti-neural REST/SCP1 pathway during embryonic CNS development
    • 10.1101/gad.1519107 1838526 1:CAS:528:DC%2BD2sXktFGgs78%3D 17403776
    • Visvanathan J, Lee S, Lee B et al (2007) The microRNA miR-124 antagonizes the anti-neural REST/SCP1 pathway during embryonic CNS development. Genes Dev 21:744-749. doi: 10.1101/gad.1519107
    • (2007) Genes Dev , vol.21 , pp. 744-749
    • Visvanathan, J.1    Lee, S.2    Lee, B.3
  • 226
    • 18444415448 scopus 로고    scopus 로고
    • Regulation of miRNA expression during neural cell specification
    • 10.1111/j.1460-9568.2005.03978.x 15845075
    • Smirnova L, Gräfe A, Seiler A et al (2005) Regulation of miRNA expression during neural cell specification. Eur J Neurosci 21:1469-1477. doi: 10.1111/j.1460-9568.2005.03978.x
    • (2005) Eur J Neurosci , vol.21 , pp. 1469-1477
    • Smirnova, L.1    Gräfe, A.2    Seiler, A.3
  • 227
    • 5344273958 scopus 로고    scopus 로고
    • Microarray analysis of microRNA expression in the developing mammalian brain
    • 10.1186/gb-2004-5-9-r68 522875 15345052
    • Miska EA, Alvarez-Saavedra E, Townsend M et al (2004) Microarray analysis of microRNA expression in the developing mammalian brain. Genome Biol 5:R68-R69. doi: 10.1186/gb-2004-5-9-r68
    • (2004) Genome Biol , vol.5 , pp. R68-R69
    • Miska, E.A.1    Alvarez-Saavedra, E.2    Townsend, M.3
  • 228
    • 1942494040 scopus 로고    scopus 로고
    • Expression profiling of mammalian microRNAs uncovers a subset of brain-expressed microRNAs with possible roles in murine and human neuronal differentiation
    • 10.1186/gb-2004-5-3-r13 395763 15003116
    • Sempere LF, Freemantle S, Pitha-Rowe I et al (2004) Expression profiling of mammalian microRNAs uncovers a subset of brain-expressed microRNAs with possible roles in murine and human neuronal differentiation. Genome Biol 5:R13-R14. doi: 10.1186/gb-2004-5-3-r13
    • (2004) Genome Biol , vol.5 , pp. R13-R14
    • Sempere, L.F.1    Freemantle, S.2    Pitha-Rowe, I.3
  • 229
    • 0141631876 scopus 로고    scopus 로고
    • A microRNA array reveals extensive regulation of microRNAs during brain development
    • 10.1261/rna.5980303 1370491 1:CAS:528:DC%2BD3sXnslGgsr4%3D 13130141
    • Krichevsky AM, King KS, Donahue CP et al (2003) A microRNA array reveals extensive regulation of microRNAs during brain development. RNA 9:1274-1281. doi: 10.1261/rna.5980303
    • (2003) RNA , vol.9 , pp. 1274-1281
    • Krichevsky, A.M.1    King, K.S.2    Donahue, C.P.3
  • 231
    • 84869884750 scopus 로고    scopus 로고
    • Neurodegeneration as an RNA disorder
    • 10.1016/j.pneurobio.2012.09.006 1:CAS:528:DC%2BC38XhslGjsLvJ 23063563
    • Johnson R, Noble W, Tartaglia GG, Buckley NJ (2012) Neurodegeneration as an RNA disorder. Prog Neurobiol 99:293-315. doi: 10.1016/j.pneurobio.2012.09.006
    • (2012) Prog Neurobiol , vol.99 , pp. 293-315
    • Johnson, R.1    Noble, W.2    Tartaglia, G.G.3    Buckley, N.J.4
  • 232
    • 84855991876 scopus 로고    scopus 로고
    • Non-coding RNAs with essential roles in neurodegenerative disorders
    • 10.1016/S1474-4422(11)70286-1 1:CAS:528:DC%2BC38Xht1Wrsrw%3D 22265214
    • Salta E, De Strooper B (2012) Non-coding RNAs with essential roles in neurodegenerative disorders. Lancet Neurol 11:189-200. doi: 10.1016/S1474-4422(11)70286-1
    • (2012) Lancet Neurol , vol.11 , pp. 189-200
    • Salta, E.1    De Strooper, B.2
  • 233
    • 78650692019 scopus 로고    scopus 로고
    • In vivo regulation of amyloid precursor protein neuronal splicing by microRNAs
    • 10.1111/j.1471-4159.2010.07097.x 1:CAS:528:DC%2BC3MXhtFGqtbo%3D 21062284
    • Smith P, Hashimi Al A, Girard J et al (2011) In vivo regulation of amyloid precursor protein neuronal splicing by microRNAs. J Neurochem 116:240-247. doi: 10.1111/j.1471-4159.2010.07097.x
    • (2011) J Neurochem , vol.116 , pp. 240-247
    • Smith, P.1    Hashimi Al, A.2    Girard, J.3
  • 234
    • 70349558133 scopus 로고    scopus 로고
    • MiR-34a, a microRNA up-regulated in a double transgenic mouse model of Alzheimer's disease, inhibits bcl2 translation
    • 10.1016/j.brainresbull.2009.08.006 1:CAS:528:DC%2BD1MXht1WqtbfE 19683563
    • Wang X, Liu P, Zhu H et al (2009) miR-34a, a microRNA up-regulated in a double transgenic mouse model of Alzheimer's disease, inhibits bcl2 translation. Brain Res Bull 80:268-273. doi: 10.1016/j.brainresbull.2009.08.006
    • (2009) Brain Res Bull , vol.80 , pp. 268-273
    • Wang, X.1    Liu, P.2    Zhu, H.3
  • 235
    • 44049108170 scopus 로고    scopus 로고
    • Loss of microRNA cluster miR-29a/b-1 in sporadic Alzheimer's disease correlates with increased BACE1/beta-secretase expression
    • 10.1073/pnas.0710263105 2359789 18434550
    • Hébert SS, Horré K, Nicolaï L et al (2008) Loss of microRNA cluster miR-29a/b-1 in sporadic Alzheimer's disease correlates with increased BACE1/beta-secretase expression. Proc Natl Acad Sci USA 105:6415-6420. doi: 10.1073/pnas.0710263105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6415-6420
    • Hébert, S.S.1    Horré, K.2    Nicolaï, L.3
  • 236
    • 38749095507 scopus 로고    scopus 로고
    • The expression of microRNA miR-107 decreases early in Alzheimer's disease and may accelerate disease progression through regulation of beta-site amyloid precursor protein-cleaving enzyme 1
    • 10.1523/JNEUROSCI.5065-07.2008 2837363 18234899
    • Wang W-X, Rajeev BW, Stromberg AJ et al (2008) The expression of microRNA miR-107 decreases early in Alzheimer's disease and may accelerate disease progression through regulation of beta-site amyloid precursor protein-cleaving enzyme 1. J Neurosci 28:1213-1223. doi: 10.1523/JNEUROSCI.5065-07.2008
    • (2008) J Neurosci , vol.28 , pp. 1213-1223
    • Wang, W.-X.1    Rajeev, B.W.2    Stromberg, A.J.3
  • 237
    • 33847203593 scopus 로고    scopus 로고
    • Micro-RNA speciation in fetal, adult and Alzheimer's disease hippocampus
    • 10.1097/WNR.0b013e3280148e8b 1:CAS:528:DC%2BD2sXhvFWrtLw%3D 17314675
    • Lukiw WJ (2007) Micro-RNA speciation in fetal, adult and Alzheimer's disease hippocampus. NeuroReport 18:297-300. doi: 10.1097/WNR.0b013e3280148e8b
    • (2007) NeuroReport , vol.18 , pp. 297-300
    • Lukiw, W.J.1
  • 238
    • 79960135400 scopus 로고    scopus 로고
    • MicroRNA profiling of Parkinson's disease brains identifies early downregulation of miR-34b/c which modulate mitochondrial function
    • 10.1093/hmg/ddr210 21558425
    • Miñones-Moyano E, Porta S, Escaramís G et al (2011) MicroRNA profiling of Parkinson's disease brains identifies early downregulation of miR-34b/c which modulate mitochondrial function. Hum Mol Genet 20:3067-3078. doi: 10.1093/hmg/ddr210
    • (2011) Hum Mol Genet , vol.20 , pp. 3067-3078
    • Miñones-Moyano, E.1    Porta, S.2    Escaramís, G.3
  • 239
    • 84921521998 scopus 로고    scopus 로고
    • Inhibition of miR-34b and miR-34c enhances α-synuclein expression in Parkinson's disease
    • 10.1016/j.febslet.2014.12.014 1:CAS:528:DC%2BC2cXitFygur%2FO 25541488
    • Kabaria S, Choi DC, Chaudhuri AD et al (2015) Inhibition of miR-34b and miR-34c enhances α-synuclein expression in Parkinson's disease. FEBS Lett 589:319-325. doi: 10.1016/j.febslet.2014.12.014
    • (2015) FEBS Lett , vol.589 , pp. 319-325
    • Kabaria, S.1    Choi, D.C.2    Chaudhuri, A.D.3
  • 240
    • 78650954319 scopus 로고    scopus 로고
    • Altered microRNA regulation in Huntington's disease models
    • 10.1016/j.expneurol.2010.10.012 1:CAS:528:DC%2BC3MXjsFSiuw%3D%3D 21035445
    • Lee S-T, Chu K, Im W-S et al (2011) Altered microRNA regulation in Huntington's disease models. Exp Neurol 227:172-179. doi: 10.1016/j.expneurol.2010.10.012
    • (2011) Exp Neurol , vol.227 , pp. 172-179
    • Lee, S.-T.1    Chu, K.2    Im, W.-S.3
  • 241
    • 77958471215 scopus 로고    scopus 로고
    • A myriad of miRNA variants in control and Huntington's disease brain regions detected by massively parallel sequencing
    • 10.1093/nar/gkq575 2978354 1:CAS:528:DC%2BC3cXhsVektr7L 20591823
    • Marti E, Pantano L, Banez-Coronel M et al (2010) A myriad of miRNA variants in control and Huntington's disease brain regions detected by massively parallel sequencing. Nucleic Acids Res 38:7219-7235. doi: 10.1093/nar/gkq575
    • (2010) Nucleic Acids Res , vol.38 , pp. 7219-7235
    • Marti, E.1    Pantano, L.2    Banez-Coronel, M.3
  • 242
    • 39649092720 scopus 로고    scopus 로고
    • A microRNA-based gene dysregulation pathway in Huntington's disease
    • 10.1016/j.nbd.2007.11.001 1:CAS:528:DC%2BD1cXisVWns78%3D 18082412
    • Johnson R, Zuccato C, Belyaev ND et al (2008) A microRNA-based gene dysregulation pathway in Huntington's disease. Neurobiology of Disease 29:438-445. doi: 10.1016/j.nbd.2007.11.001
    • (2008) Neurobiology of Disease , vol.29 , pp. 438-445
    • Johnson, R.1    Zuccato, C.2    Belyaev, N.D.3
  • 243
    • 52949137369 scopus 로고    scopus 로고
    • MiR-19, miR-101 and miR-130 co-regulate ATXN1 levels to potentially modulate SCA1 pathogenesis
    • 10.1038/nn.2183 2574629 1:CAS:528:DC%2BD1cXhtFKhsLzP 18758459
    • Lee Y, Samaco RC, Gatchel JR et al (2008) miR-19, miR-101 and miR-130 co-regulate ATXN1 levels to potentially modulate SCA1 pathogenesis. Nat Neurosci 11:1137-1139. doi: 10.1038/nn.2183
    • (2008) Nat Neurosci , vol.11 , pp. 1137-1139
    • Lee, Y.1    Samaco, R.C.2    Gatchel, J.R.3
  • 244
    • 58149375393 scopus 로고    scopus 로고
    • The Bifunctional microRNA miR-9/miR-9∗Regulates REST and CoREST and Is Downregulated in Huntington's Disease
    • 10.1523/JNEUROSCI.2390-08.2008 3124002 1:CAS:528:DC%2BD1MXnsF2huw%3D%3D 19118166
    • Packer AN, Xing Y, Harper SQ et al (2008) The Bifunctional microRNA miR-9/miR-9∗Regulates REST and CoREST and Is Downregulated in Huntington's Disease. J Neurosci 28:14341-14346. doi: 10.1523/JNEUROSCI.2390-08.2008
    • (2008) J Neurosci , vol.28 , pp. 14341-14346
    • Packer, A.N.1    Xing, Y.2    Harper, S.Q.3
  • 245
    • 84867732569 scopus 로고    scopus 로고
    • Speeding with control: Codon usage, tRNAs, and ribosomes
    • 10.1016/j.tig.2012.07.006 1:CAS:528:DC%2BC38Xht1GksLvF 22921354
    • Novoa EM, Ribas de Pouplana L (2012) Speeding with control: codon usage, tRNAs, and ribosomes. Trends Genet 28:574-581. doi: 10.1016/j.tig.2012.07.006
    • (2012) Trends Genet , vol.28 , pp. 574-581
    • Novoa, E.M.1    Ribas De Pouplana, L.2
  • 246
    • 33845635732 scopus 로고    scopus 로고
    • Diversity of tRNA genes in eukaryotes
    • 10.1093/nar/gkl725 1693877 1:CAS:528:DC%2BD28XhtlCru7bK 17088292
    • Goodenbour JM, Pan T (2006) Diversity of tRNA genes in eukaryotes. Nucleic Acids Res 34:6137-6146. doi: 10.1093/nar/gkl725
    • (2006) Nucleic Acids Res , vol.34 , pp. 6137-6146
    • Goodenbour, J.M.1    Pan, T.2
  • 247
    • 84904806049 scopus 로고    scopus 로고
    • RNA function. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration
    • 10.1126/science.1249749 4281038 1:CAS:528:DC%2BC2cXhtFyks7rN 25061210
    • Ishimura R, Nagy G, Dotu I et al (2014) RNA function. Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration. Science 345:455-459. doi: 10.1126/science.1249749
    • (2014) Science , vol.345 , pp. 455-459
    • Ishimura, R.1    Nagy, G.2    Dotu, I.3
  • 248
    • 79953110006 scopus 로고    scopus 로고
    • Impairment of the tRNA-splicing endonuclease subunit 54 (tsen54) gene causes neurological abnormalities and larval death in zebrafish models of pontocerebellar hypoplasia
    • 10.1093/hmg/ddr034 1:CAS:528:DC%2BC3MXjvVKruro%3D 21273289
    • Kasher PR, Namavar Y, van Tijn P et al (2011) Impairment of the tRNA-splicing endonuclease subunit 54 (tsen54) gene causes neurological abnormalities and larval death in zebrafish models of pontocerebellar hypoplasia. Hum Mol Genet 20:1574-1584. doi: 10.1093/hmg/ddr034
    • (2011) Hum Mol Genet , vol.20 , pp. 1574-1584
    • Kasher, P.R.1    Namavar, Y.2    Van Tijn, P.3
  • 249
    • 78650693958 scopus 로고    scopus 로고
    • Clinical, neuroradiological and genetic findings in pontocerebellar hypoplasia
    • 10.1093/brain/awq287 20952379
    • Namavar Y, Barth PG, Kasher PR et al (2011) Clinical, neuroradiological and genetic findings in pontocerebellar hypoplasia. Brain 134:143-156. doi: 10.1093/brain/awq287
    • (2011) Brain , vol.134 , pp. 143-156
    • Namavar, Y.1    Barth, P.G.2    Kasher, P.R.3
  • 250
    • 50449096432 scopus 로고    scopus 로고
    • TRNA splicing endonuclease mutations cause pontocerebellar hypoplasia
    • 10.1038/ng.204 1:CAS:528:DC%2BD1cXhtVGgtrfL 18711368
    • Budde BS, Namavar Y, Barth PG et al (2008) tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia. Nat Genet 40:1113-1118. doi: 10.1038/ng.204
    • (2008) Nat Genet , vol.40 , pp. 1113-1118
    • Budde, B.S.1    Namavar, Y.2    Barth, P.G.3
  • 251
    • 35348983348 scopus 로고    scopus 로고
    • Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia
    • 10.1086/521227 2227936 1:CAS:528:DC%2BD2sXhtFSktrjE 17847012
    • Edvardson S, Shaag A, Kolesnikova O et al (2007) Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia. Am J Hum Genet 81:857-862. doi: 10.1086/521227
    • (2007) Am J Hum Genet , vol.81 , pp. 857-862
    • Edvardson, S.1    Shaag, A.2    Kolesnikova, O.3
  • 252
    • 33644832850 scopus 로고    scopus 로고
    • Motor neuron disease in a patient with a mitochondrial tRNAIle mutation
    • 10.1002/ana.20758 1:CAS:528:DC%2BD28XjtV2ltrc%3D 16358336
    • Borthwick GM, Taylor RW, Walls TJ et al (2006) Motor neuron disease in a patient with a mitochondrial tRNAIle mutation. Ann Neurol 59:570-574. doi: 10.1002/ana.20758
    • (2006) Ann Neurol , vol.59 , pp. 570-574
    • Borthwick, G.M.1    Taylor, R.W.2    Walls, T.J.3
  • 254
    • 33745001194 scopus 로고    scopus 로고
    • Cleavage of pre-tRNAs by the splicing endonuclease requires a composite active site
    • 10.1038/nature04741 1:CAS:528:DC%2BD28XksleltLg%3D 16710424
    • Trotta CR, Paushkin SV, Patel M et al (2006) Cleavage of pre-tRNAs by the splicing endonuclease requires a composite active site. Nature 441:375-377. doi: 10.1038/nature04741
    • (2006) Nature , vol.441 , pp. 375-377
    • Trotta, C.R.1    Paushkin, S.V.2    Patel, M.3
  • 255
    • 84875623194 scopus 로고    scopus 로고
    • CLP1 links tRNA metabolism to progressive motor-neuron loss
    • 10.1038/nature11923 3674495 23474986
    • Hanada T, Weitzer S, Mair B et al (2013) CLP1 links tRNA metabolism to progressive motor-neuron loss. Nature. doi: 10.1038/nature11923
    • (2013) Nature
    • Hanada, T.1    Weitzer, S.2    Mair, B.3
  • 256
    • 84899576549 scopus 로고    scopus 로고
    • Human CLP1 mutations Alter tRNA biogenesis, affecting Both peripheral and central nervous system function
    • 10.1016/j.cell.2014.02.058 4146440 1:CAS:528:DC%2BC2cXntFGgsr0%3D 24766809
    • Karaca E, Weitzer S, Pehlivan D et al (2014) Human CLP1 mutations Alter tRNA biogenesis, affecting Both peripheral and central nervous system function. Cell 157:636-650. doi: 10.1016/j.cell.2014.02.058
    • (2014) Cell , vol.157 , pp. 636-650
    • Karaca, E.1    Weitzer, S.2    Pehlivan, D.3
  • 257
    • 84899581919 scopus 로고    scopus 로고
    • CLP1 Founder Mutation Links tRNA Splicing and Maturation to Cerebellar Development and Neurodegeneration
    • 10.1016/j.cell.2014.03.049 4128918 1:CAS:528:DC%2BC2cXntFGit7c%3D 24766810
    • Schaffer AE, Eggens VRC, Caglayan AO et al (2014) CLP1 Founder Mutation Links tRNA Splicing and Maturation to Cerebellar Development and Neurodegeneration. Cell 157:651-663. doi: 10.1016/j.cell.2014.03.049
    • (2014) Cell , vol.157 , pp. 651-663
    • Schaffer, A.E.1    Eggens, V.R.C.2    Caglayan, A.O.3
  • 258
    • 77952581350 scopus 로고    scopus 로고
    • Long non-coding RNAs in nervous system function and disease
    • 10.1016/j.brainres.2010.03.110 1:CAS:528:DC%2BC3cXmslShsr0%3D 20380817
    • Qureshi IA, Mattick JS, Mehler MF (2010) Long non-coding RNAs in nervous system function and disease. Brain Res 1338:20-35. doi: 10.1016/j.brainres.2010.03.110
    • (2010) Brain Res , vol.1338 , pp. 20-35
    • Qureshi, I.A.1    Mattick, J.S.2    Mehler, M.F.3
  • 259
    • 77952698932 scopus 로고    scopus 로고
    • Evidence for natural antisense transcript-mediated inhibition of microRNA function
    • 10.1186/gb-2010-11-5-r56 2898074 20507594
    • Faghihi MA, Zhang M, Huang J et al (2010) Evidence for natural antisense transcript-mediated inhibition of microRNA function. Genome Biol 11:R56. doi: 10.1186/gb-2010-11-5-r56
    • (2010) Genome Biol , vol.11 , pp. R56
    • Faghihi, M.A.1    Zhang, M.2    Huang, J.3
  • 260
    • 84908870790 scopus 로고    scopus 로고
    • Cross-talking noncoding RNAs contribute to cell-specific neurodegeneration in SCA7
    • 10.1038/nsmb.2902 4255225 1:CAS:528:DC%2BC2cXhslelsLfI 25306109
    • Tan JY, Vance KW, Varela MA et al (2014) Cross-talking noncoding RNAs contribute to cell-specific neurodegeneration in SCA7. Nat Struct Mol Biol 21:955-961. doi: 10.1038/nsmb.2902
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 955-961
    • Tan, J.Y.1    Vance, K.W.2    Varela, M.A.3
  • 261
    • 84923568472 scopus 로고    scopus 로고
    • The striatal long noncoding RNA Abhd11os is neuroprotective against an N-terminal fragment of mutant huntingtin in vivo
    • 10.1016/j.neurobiolaging.2014.11.014 25619660
    • Francelle L, Galvan L, Gaillard M-C et al (2015) The striatal long noncoding RNA Abhd11os is neuroprotective against an N-terminal fragment of mutant huntingtin in vivo. Neurobiol Aging 36(1601):e7-e16. doi: 10.1016/j.neurobiolaging.2014.11.014
    • (2015) Neurobiol Aging , vol.36 , Issue.1601 , pp. e7-e16
    • Francelle, L.1    Galvan, L.2    Gaillard, M.-C.3
  • 262
    • 0024148501 scopus 로고
    • Spliceosomal snRNAs
    • 10.1146/annurev.ge.22.120188.002131 1:CAS:528:DyaL1MXhsV2rt74%3D 2977088
    • Guthrie C, Patterson B (1988) Spliceosomal snRNAs. Annu Rev Genet 22:387-419. doi: 10.1146/annurev.ge.22.120188.002131
    • (1988) Annu Rev Genet , vol.22 , pp. 387-419
    • Guthrie, C.1    Patterson, B.2
  • 263
    • 0023127048 scopus 로고
    • The role of small nuclear ribonucleoprotein particles in pre-mRNA splicing
    • 10.1038/325673a0 1:CAS:528:DyaL2sXhtFCgsbw%3D 2950324
    • Maniatis T, Reed R (1987) The role of small nuclear ribonucleoprotein particles in pre-mRNA splicing. Nature 325:673-678. doi: 10.1038/325673a0
    • (1987) Nature , vol.325 , pp. 673-678
    • Maniatis, T.1    Reed, R.2
  • 264
    • 43049168361 scopus 로고    scopus 로고
    • SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing
    • 10.1016/j.cell.2008.03.031 2446403 1:CAS:528:DC%2BD1cXmsVOrur0%3D 18485868
    • Zhang Z, Lotti F, Dittmar K et al (2008) SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell 133:585-600. doi: 10.1016/j.cell.2008.03.031
    • (2008) Cell , vol.133 , pp. 585-600
    • Zhang, Z.1    Lotti, F.2    Dittmar, K.3
  • 265
    • 84856103324 scopus 로고    scopus 로고
    • Mutation of a U2 snRNA gene causes global disruption of alternative splicing and neurodegeneration
    • 10.1016/j.cell.2011.11.057 3488875 1:CAS:528:DC%2BC38XhtFKgsbg%3D 22265417
    • Jia Y, Mu JC, Ackerman SL (2012) Mutation of a U2 snRNA gene causes global disruption of alternative splicing and neurodegeneration. Cell 148:296-308. doi: 10.1016/j.cell.2011.11.057
    • (2012) Cell , vol.148 , pp. 296-308
    • Jia, Y.1    Mu, J.C.2    Ackerman, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.