메뉴 건너뛰기




Volumn 22, Issue 9, 2015, Pages 1413-1424

Primary cilia and autophagic dysfunction in Huntington's disease

Author keywords

[No Author keywords available]

Indexed keywords

HUNTINGTIN; POLYGLUTAMINE;

EID: 84938959019     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2015.80     Document Type: Review
Times cited : (29)

References (150)
  • 1
    • 77956069555 scopus 로고    scopus 로고
    • Huntington's disease
    • Novak MJU, Tabrizi SJ. Huntington's disease. BMJ 2010; 340: c3109-c3109.
    • (2010) BMJ , vol.340 , pp. c3109-c3109
    • Novak, M.J.U.1    Tabrizi, S.J.2
  • 2
    • 78650031174 scopus 로고    scopus 로고
    • Huntington's disease: From molecular pathogenesis to clinical treatment
    • Ross CA, Tabrizi SJ. Huntington's disease: from molecular pathogenesis to clinical treatment. Lancet Neurol 2011; 10: 83-98.
    • (2011) Lancet Neurol , vol.10 , pp. 83-98
    • Ross, C.A.1    Tabrizi, S.J.2
  • 3
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • Walker FO. Huntington's disease. Lancet 2007; 369: 218-228.
    • (2007) Lancet , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 4
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • MacDonald ME, Ambrose CM, Duyao MP, Myers RH, Lin C, Srinidhi L et al. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993; 72: 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
    • MacDonald, M.E.1    Ambrose, C.M.2    Duyao, M.P.3    Myers, R.H.4    Lin, C.5    Srinidhi, L.6
  • 5
    • 0027176364 scopus 로고
    • The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease
    • Andrew SE, Paul Goldberg Y, Kremer B, Telenius H, Theilmann J, Adam S et al. The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease. Nat Genet 1993; 4: 398-403.
    • (1993) Nat Genet , vol.4 , pp. 398-403
    • Andrew, S.E.1    Paul Goldberg, Y.2    Kremer, B.3    Telenius, H.4    Theilmann, J.5    Adam, S.6
  • 6
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I, Levine MS, Zeitlin S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet 2000; 26: 300-306.
    • (2000) Nat Genet , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 7
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S, Liu J-P, Chapman DL, Papaioannou VE, Efstratiadis A. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nat Genet 1995; 11: 155-163.
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.-P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 8
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier LR, Charrin BC, Borrell-Pagès M, Dompierre JP, Rangone H, Cordelières FP et al. Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell 2004; 118: 127-138.
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1    Charrin, B.C.2    Borrell-Pagès, M.3    Dompierre, J.P.4    Rangone, H.5    Cordelières, F.P.6
  • 10
    • 84903770556 scopus 로고    scopus 로고
    • The many faces of autophagy dysfunction in Huntington's disease: From mechanism to therapy
    • Cortes CJ, La Spada AR. The many faces of autophagy dysfunction in Huntington's disease: from mechanism to therapy. Drug Discov Today 2014; 19: 963-971.
    • (2014) Drug Discov Today , vol.19 , pp. 963-971
    • Cortes, C.J.1    La Spada, A.R.2
  • 12
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade MA, Bork P. HEAT repeats in the Huntington's disease protein. Nat Genet 1995; 11: 115-116.
    • (1995) Nat Genet , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 13
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • Cattaneo E, Zuccato C, Tartari M. Normal huntingtin function: an alternative approach to Huntington's disease. Nat Rev Neurosci 2005; 6: 919-930.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 14
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • Landles C, Sathasivam K, Weiss A, Woodman B, Moffitt H, Finkbeiner S et al. Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J Biol Chem 2010; 285: 8808-8823.
    • (2010) J Biol Chem , vol.285 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Weiss, A.3    Woodman, B.4    Moffitt, H.5    Finkbeiner, S.6
  • 15
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim YJ, Yi Y, Sapp E, Wang Y, Cuiffo B, Kegel KB et al. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci USA 2001; 98: 12784-12789.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6
  • 17
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ, Haigh B, Bissada N, Lu G et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 2006; 125: 1179-1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3    Haigh, B.4    Bissada, N.5    Lu, G.6
  • 18
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: Accumulation of calpain/caspase fragments in the nucleus
    • Gafni J, Hermel E, Young JE, Wellington CL, Hayden MR, Ellerby LM. Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 2004; 279: 20211-20220.
    • (2004) J Biol Chem , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5    Ellerby, L.M.6
  • 19
    • 77955500335 scopus 로고    scopus 로고
    • Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease
    • Miller JP, Holcomb J, Al-Ramahi I, de Haro M, Gafni J, Zhang N et al. Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease. Neuron 2010; 67: 199-212.
    • (2010) Neuron , vol.67 , pp. 199-212
    • Miller, J.P.1    Holcomb, J.2    Al-Ramahi, I.3    De Haro, M.4    Gafni, J.5    Zhang, N.6
  • 20
    • 84859760185 scopus 로고    scopus 로고
    • Native mutant huntingtin in human brain: Evidence for prevalence of full-length monomer
    • Sapp E, Valencia A, Li X, Aronin N, Kegel KB, Vonsattel J-P et al. Native mutant huntingtin in human brain: evidence for prevalence of full-length monomer. J Biol Chem 2012; 287: 13487-13499.
    • (2012) J Biol Chem , vol.287 , pp. 13487-13499
    • Sapp, E.1    Valencia, A.2    Li, X.3    Aronin, N.4    Kegel, K.B.5    Vonsattel, J.-P.6
  • 21
    • 63449090757 scopus 로고    scopus 로고
    • Huntingtin as an essential integrator of intracellular vesicular trafficking
    • Caviston JP, Holzbaur ELF. Huntingtin as an essential integrator of intracellular vesicular trafficking. Trends Cell Biol 2009; 19: 147-155.
    • (2009) Trends Cell Biol , vol.19 , pp. 147-155
    • Caviston, J.P.1    Holzbaur, E.L.F.2
  • 22
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn CL, Sun T, Sadri-Vakili G, McFarland KN, DiRocco DP, Yohrling GJ et al. Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J Neurosci 2008; 28: 10720-10733.
    • (2008) J Neurosci , vol.28 , pp. 10720-10733
    • Benn, C.L.1    Sun, T.2    Sadri-Vakili, G.3    McFarland, K.N.4    DiRocco, D.P.5    Yohrling, G.J.6
  • 23
    • 68849083063 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor in neurodegenerative diseases
    • Zuccato C, Cattaneo E. Brain-derived neurotrophic factor in neurodegenerative diseases. Nat Rev Neurol 2009; 5: 311-322.
    • (2009) Nat Rev Neurol , vol.5 , pp. 311-322
    • Zuccato, C.1    Cattaneo, E.2
  • 24
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1? by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L, Jeong H, Borovecki F, Parkhurst CN, Tanese N, Krainc D. Transcriptional repression of PGC-1? by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 2006; 127: 59-69.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 26
    • 79952443408 scopus 로고    scopus 로고
    • Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity
    • Song W, Chen J, Petrilli A, Liot G, Klinglmayr E, Zhou Y et al. Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity. Nat Med 2011; 17: 377-382.
    • (2011) Nat Med , vol.17 , pp. 377-382
    • Song, W.1    Chen, J.2    Petrilli, A.3    Liot, G.4    Klinglmayr, E.5    Zhou, Y.6
  • 27
    • 84863923855 scopus 로고    scopus 로고
    • PGC-1? Rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function
    • Tsunemi T, Ashe TD, Morrison BE, Soriano KR, Au J, Roque RAV et al. PGC-1? rescues Huntington's disease proteotoxicity by preventing oxidative stress and promoting TFEB function. Sci Transl Med 2012; 4: 142ra97.
    • (2012) Sci Transl Med , vol.4 , pp. 142-197
    • Tsunemi, T.1    Ashe, T.D.2    Morrison, B.E.3    Soriano, K.R.4    Au, J.5    Roque, R.A.V.6
  • 28
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: Revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant R, Atwal RS, Desmond C, Munsie L, Tran T. Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J 2008; 275: 4252-4262.
    • (2008) FEBS J , vol.275 , pp. 4252-4262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3    Munsie, L.4    Tran, T.5
  • 29
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 30
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 1998; 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 33
    • 84877139837 scopus 로고    scopus 로고
    • A novel human embryonic stem cell-derived Huntington's disease neuronal model exhibits mutant huntingtin (mHTT) aggregates and soluble mHTTdependent neurodegeneration
    • Lu B, Palacino J. A novel human embryonic stem cell-derived Huntington's disease neuronal model exhibits mutant huntingtin (mHTT) aggregates and soluble mHTTdependent neurodegeneration. FASEB J 2013; 27: 1820-1829.
    • (2013) FASEB J , vol.27 , pp. 1820-1829
    • Lu, B.1    Palacino, J.2
  • 34
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • Martinez-Vicente M, Talloczy Z, Wong E, Tang G, Koga H, Kaushik S et al. Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease. Nat Neurosci 2010; 13: 567-576.
    • (2010) Nat Neurosci , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3    Tang, G.4    Koga, H.5    Kaushik, S.6
  • 35
    • 84859983420 scopus 로고    scopus 로고
    • Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease
    • Hipp MS, Patel CN, Bersuker K, Riley BE, Kaiser SE, Shaler TA et al. Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease. J Cell Biol 2012; 196: 573-587.
    • (2012) J Cell Biol , vol.196 , pp. 573-587
    • Hipp, M.S.1    Patel, C.N.2    Bersuker, K.3    Riley, B.E.4    Kaiser, S.E.5    Shaler, T.A.6
  • 36
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441: 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 37
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441: 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 39
    • 0141891952 scopus 로고    scopus 로고
    • Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity
    • Zhou H, Cao F, Wang Z, Yu Z-X, Nguyen H-P, Evans J et al. Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. J Cell Biol 2003; 163: 109-118.
    • (2003) J Cell Biol , vol.163 , pp. 109-118
    • Zhou, H.1    Cao, F.2    Wang, Z.3    Yu, Z.-X.4    Nguyen, H.-P.5    Evans, J.6
  • 40
    • 33846540080 scopus 로고    scopus 로고
    • The first 17 amino acids of huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis
    • Rockabrand E, Slepko N, Pantalone A, Nukala VN, Kazantsev A, Marsh JL et al. The first 17 amino acids of huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Hum Mol Genet 2007; 16: 61-77.
    • (2007) Hum Mol Genet , vol.16 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Pantalone, A.3    Nukala, V.N.4    Kazantsev, A.5    Marsh, J.L.6
  • 41
    • 65249141171 scopus 로고    scopus 로고
    • Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus
    • Toro D, del, Alberch J, Lázaro-Diéguez F, Martín-Ibáñez R, Xifró X, Egea G et al. Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus. Mol Biol Cell 2009; 20: 1478-1492.
    • (2009) Mol Biol Cell , vol.20 , pp. 1478-1492
    • Toro, D.1    Del Alberch, J.2    Lázaro-Diéguez, F.3    Martín-Ibáñez, R.4    Xifró, X.5    Egea, G.6
  • 42
    • 84919619341 scopus 로고    scopus 로고
    • Huntingtin is required for ER-to-Golgi transport and for secretory vesicle fusion at the plasma membrane
    • Brandstaetter H, Kruppa AJ, Buss F. Huntingtin is required for ER-to-Golgi transport and for secretory vesicle fusion at the plasma membrane. Dis Model Mech 2014; 7: 1335-1340.
    • (2014) Dis Model Mech , vol.7 , pp. 1335-1340
    • Brandstaetter, H.1    Kruppa, A.J.2    Buss, F.3
  • 43
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald ML, Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 2008; 22: 3308-3319.
    • (2008) Genes Dev , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 44
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon RA. The role of autophagy in neurodegenerative disease. Nat Med 2013; 19: 983-997.
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 45
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990; 15: 305-309.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 46
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • Kaushik S, Cuervo AM. Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol 2012; 22: 407-417.
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 47
    • 84867427022 scopus 로고    scopus 로고
    • The role of chaperone-mediated autophagy in Huntingtin degradation
    • Qi L, Zhang X-D, Wu J-C, Lin F, Wang J, DiFiglia M et al. The role of chaperone-mediated autophagy in Huntingtin degradation. PLoS ONE 2012; 7: e46834.
    • (2012) PLoS ONE , vol.7 , pp. e46834
    • Qi, L.1    Zhang, X.-D.2    Wu, J.-C.3    Lin, F.4    Wang, J.5    DiFiglia, M.6
  • 52
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux
    • Lee H, Noh J-Y, Oh Y, Kim Y, Chang J-W, Chung C-W et al. IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux. Hum Mol Genet 2012; 21: 101-114.
    • (2012) Hum Mol Genet , vol.21 , pp. 101-114
    • Lee, H.1    Noh, J.-Y.2    Oh, Y.3    Kim, Y.4    Chang, J.-W.5    Chung, C.-W.6
  • 53
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, Oroz LG et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004; 36: 585-595.
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6
  • 54
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice
    • Gu X, Greiner ER, Mishra R, Kodali R, Osmand A, Finkbeiner S et al. Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 2009; 64: 828-840.
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1    Greiner, E.R.2    Mishra, R.3    Kodali, R.4    Osmand, A.5    Finkbeiner, S.6
  • 55
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson LM, Aiken CT, Kaltenbach LS, Agrawal N, Illes K, Khoshnan A et al. IKK phosphorylates huntingtin and targets it for degradation by the proteasome and lysosome. J Cell Biol 2009; 187: 1083-1099.
    • (2009) J Cell Biol , vol.187 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Kaltenbach, L.S.3    Agrawal, N.4    Illes, K.5    Khoshnan, A.6
  • 57
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H, Then F, Melia Jr TJ, Mazzulli JR, Cui L, Savas JN et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 2009; 137: 60-72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.3    Mazzulli, J.R.4    Cui, L.5    Savas, J.N.6
  • 58
    • 84901323796 scopus 로고    scopus 로고
    • Identification of a post-translationally myristoylated autophagy-inducing domain released by caspase cleavage of huntingtin
    • Martin DDO, Heit RJ, Yap MC, Davidson MW, Hayden MR, Berthiaume LG. Identification of a post-translationally myristoylated autophagy-inducing domain released by caspase cleavage of huntingtin. Hum Mol Genet 2014; 23: 3166-3179.
    • (2014) Hum Mol Genet , vol.23 , pp. 3166-3179
    • Martin, D.D.O.1    Heit, R.J.2    Yap, M.C.3    Davidson, M.W.4    Hayden, M.R.5    Berthiaume, L.G.6
  • 60
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, Manifava M, Chandra P, Roderick HL, Habermann A et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 2008; 182: 685-701.
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6
  • 61
    • 84880777164 scopus 로고    scopus 로고
    • Identification of ROCK1 kinase as a critical regulator of Beclin1-mediated autophagy during metabolic stress
    • Gurkar AU, Chu K, Raj L, Bouley R, Lee S-H, Kim Y-B et al. Identification of ROCK1 kinase as a critical regulator of Beclin1-mediated autophagy during metabolic stress. Nat Commun 2013; 4: 2189.
    • (2013) Nat Commun , vol.4 , pp. 2189
    • Gurkar, A.U.1    Chu, K.2    Raj, L.3    Bouley, R.4    Lee, S.-H.5    Kim, Y.-B.6
  • 62
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant huntingtin by Beclin 1
    • Shibata M, Lu T, Furuya T, Degterev A, Mizushima N, Yoshimori T et al. Regulation of intracellular accumulation of mutant huntingtin by Beclin 1. J Biol Chem 2006; 281: 14474-14485.
    • (2006) J Biol Chem , vol.281 , pp. 14474-14485
    • Shibata, M.1    Lu, T.2    Furuya, T.3    Degterev, A.4    Mizushima, N.5    Yoshimori, T.6
  • 63
    • 84892755229 scopus 로고    scopus 로고
    • The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation
    • Wong YC, Holzbaur ELF. The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation. J Neurosci 2014; 34: 1293-1305.
    • (2014) J Neurosci , vol.34 , pp. 1293-1305
    • Wong, Y.C.1    Holzbaur, E.L.F.2
  • 64
    • 34548259958 scopus 로고    scopus 로고
    • P62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun J-A, Outzen H et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282: 24131-24145.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.-A.5    Outzen, H.6
  • 65
    • 77649219699 scopus 로고    scopus 로고
    • Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
    • Zheng S, Clabough EBD, Sarkar S, Futter M, Rubinsztein DC, Zeitlin SO. Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice. PLoS Genet 2010; 6: e1000838.
    • (2010) PLoS Genet , vol.6 , pp. e1000838
    • Zheng, S.1    Clabough, E.B.D.2    Sarkar, S.3    Futter, M.4    Rubinsztein, D.C.5    Zeitlin, S.O.6
  • 66
    • 84923789937 scopus 로고    scopus 로고
    • Huntingtin functions as a scaffold for selective macroautophagy
    • Rui Y-N, Xu Z, Patel B, Chen Z, Chen D, Tito A et al. Huntingtin functions as a scaffold for selective macroautophagy. Nat Cell Biol 2015; 17: 262-275.
    • (2015) Nat Cell Biol , vol.17 , pp. 262-275
    • Rui, Y.-N.1    Xu, Z.2    Patel, B.3    Chen, Z.4    Chen, D.5    Tito, A.6
  • 67
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates Hedgehog signaling at the primary cilium
    • Rohatgi R, Milenkovic L, Scott MP. Patched1 regulates Hedgehog signaling at the primary cilium. Science 2007; 317: 372-376.
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 70
    • 37749054886 scopus 로고    scopus 로고
    • Kif3a constrains ?-catenin-dependent Wnt signalling through dual ciliary and non-ciliary mechanisms
    • Corbit KC, Shyer AE, Dowdle WE, Gaulden J, Singla V, Reiter JF. Kif3a constrains ?-catenin-dependent Wnt signalling through dual ciliary and non-ciliary mechanisms. Nat Cell Biol 2008; 10: 70-76.
    • (2008) Nat Cell Biol , vol.10 , pp. 70-76
    • Corbit, K.C.1    Shyer, A.E.2    Dowdle, W.E.3    Gaulden, J.4    Singla, V.5    Reiter, J.F.6
  • 71
    • 84899893563 scopus 로고    scopus 로고
    • Primary cilia in the developing and mature brain
    • Guemez-Gamboa A, Coufal NG, Gleeson JG. Primary cilia in the developing and mature brain. Neuron 2014; 82: 511-521.
    • (2014) Neuron , vol.82 , pp. 511-521
    • Guemez-Gamboa, A.1    Coufal, N.G.2    Gleeson, J.G.3
  • 73
    • 70349876742 scopus 로고    scopus 로고
    • A1-42 stimulates adult SVZ neurogenesis through the p75 neurotrophin receptor
    • Sotthibundhu A, Li Q-X, Thangnipon W, Coulson EJ. A?1-42 stimulates adult SVZ neurogenesis through the p75 neurotrophin receptor. Neurobiol Aging 2009; 30: 1975-1985.
    • (2009) Neurobiol Aging , vol.30 , pp. 1975-1985
    • Sotthibundhu, A.1    Li, Q.-X.2    Thangnipon, W.3    Coulson, E.J.4
  • 74
    • 80555136825 scopus 로고    scopus 로고
    • Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease
    • Keryer G, Pineda JR, Liot G, Kim J, Dietrich P, Benstaali C et al. Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease. J Clin Invest 2011; 121: 4372-4382.
    • (2011) J Clin Invest , vol.121 , pp. 4372-4382
    • Keryer, G.1    Pineda, J.R.2    Liot, G.3    Kim, J.4    Dietrich, P.5    Benstaali, C.6
  • 75
    • 33746891890 scopus 로고    scopus 로고
    • The primary cilium as the cell's antenna: Signaling at a sensory organelle
    • Singla V, Reiter JF. The primary cilium as the cell's antenna: signaling at a sensory organelle. Science 2006; 313: 629-633.
    • (2006) Science , vol.313 , pp. 629-633
    • Singla, V.1    Reiter, J.F.2
  • 76
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET et al. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 2010; 329: 436-439.
    • (2010) Science , vol.329 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3    Scott, M.P.4    Nachury, M.V.5    Spiliotis, E.T.6
  • 79
    • 84865803552 scopus 로고    scopus 로고
    • The BBSome controls IFT assembly and turnaround in cilia
    • Wei Q, Zhang Y, Li Y, Zhang Q, Ling K, Hu J. The BBSome controls IFT assembly and turnaround in cilia. Nat Cell Biol 2012; 14: 950-957.
    • (2012) Nat Cell Biol , vol.14 , pp. 950-957
    • Wei, Q.1    Zhang, Y.2    Li, Y.3    Zhang, Q.4    Ling, K.5    Hu, J.6
  • 80
    • 79953032655 scopus 로고    scopus 로고
    • Ciliogenesis: Building the cell's antenna
    • Ishikawa H, Marshall WF. Ciliogenesis: building the cell's antenna. Nat Rev Mol Cell Biol 2011; 12: 222-234.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 222-234
    • Ishikawa, H.1    Marshall, W.F.2
  • 81
    • 34250012834 scopus 로고    scopus 로고
    • A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis
    • Nachury MV, Loktev AV, Zhang Q,Westlake CJ, Peränen J, Merdes A et al. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 2007; 129: 1201-1213.
    • (2007) Cell , vol.129 , pp. 1201-1213
    • Nachury, M.V.1    Loktev, A.V.2    Zhang Qwestlake, C.J.3    Peränen, J.4    Merdes, A.5
  • 82
    • 58149326846 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT): Role in ciliary assembly, resorption and signalling
    • Pedersen LB, Rosenbaum JL. Intraflagellar transport (IFT): role in ciliary assembly, resorption and signalling. Curr Top Dev Biol 2008; 85: 23-61.
    • (2008) Curr Top Dev Biol , vol.85 , pp. 23-61
    • Pedersen, L.B.1    Rosenbaum, J.L.2
  • 83
    • 84904439368 scopus 로고    scopus 로고
    • Primary cilium: An elaborate structure that blocks cell division
    • Ke Y-N, Yang W-X. Primary cilium: an elaborate structure that blocks cell division? Gene 2014; 547: 175-185.
    • (2014) Gene , vol.547 , pp. 175-185
    • Ke, Y.-N.1    Yang, W.-X.2
  • 84
    • 34250758641 scopus 로고    scopus 로고
    • HEF1-Dependent Aurora A. Activation induces disassembly of the primary cilium
    • Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA, HEF1-Dependent Aurora A. Activation induces disassembly of the primary cilium. Cell 2007; 129: 1351-1363.
    • (2007) Cell , vol.129 , pp. 1351-1363
    • Pugacheva, E.N.1    Jablonski, S.A.2    Hartman, T.R.3    Henske, E.P.4    Golemis, E.A.5
  • 85
    • 76649103368 scopus 로고    scopus 로고
    • The perennial organelle: Assembly and disassembly of the primary cilium
    • Seeley ES, Nachury MV. The perennial organelle: assembly and disassembly of the primary cilium. J Cell Sci 2010; 123: 511-518.
    • (2010) J Cell Sci , vol.123 , pp. 511-518
    • Seeley, E.S.1    Nachury, M.V.2
  • 86
    • 33846064322 scopus 로고    scopus 로고
    • Leptin and its receptors are present in the rat olfactory mucosa and modulated by the nutritional status
    • Baly C, Aioun J, Badonnel K, Lacroix M-C, Durieux D, Schlegel C et al. Leptin and its receptors are present in the rat olfactory mucosa and modulated by the nutritional status. Brain Res 2007; 1129: 130-141.
    • (2007) Brain Res , vol.1129 , pp. 130-141
    • Baly, C.1    Aioun, J.2    Badonnel, K.3    Lacroix, M.-C.4    Durieux, D.5    Schlegel, C.6
  • 89
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, Guan K-L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011; 13: 132-141.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.-L.4
  • 90
    • 40849142136 scopus 로고    scopus 로고
    • Human embryonic stem cells in culture possess primary cilia with hedgehog signaling machinery
    • Kiprilov EN, Awan A, Desprat R, Velho M, Clement CA, Byskov AG et al. Human embryonic stem cells in culture possess primary cilia with hedgehog signaling machinery. J Cell Biol 2008; 180: 897-904.
    • (2008) J Cell Biol , vol.180 , pp. 897-904
    • Kiprilov, E.N.1    Awan, A.2    Desprat, R.3    Velho, M.4    Clement, C.A.5    Byskov, A.G.6
  • 91
    • 33947250696 scopus 로고    scopus 로고
    • The energy sensing LKB1-AMPK pathway regulates p27kip1 phosphorylation mediating the decision to enter autophagy or apoptosis
    • Liang J, Shao SH, Xu Z-X, Hennessy B, Ding Z, Larrea M et al. The energy sensing LKB1-AMPK pathway regulates p27kip1 phosphorylation mediating the decision to enter autophagy or apoptosis. Nat Cell Biol 2007; 9: 218-224.
    • (2007) Nat Cell Biol , vol.9 , pp. 218-224
    • Liang, J.1    Shao, S.H.2    Xu, Z.-X.3    Hennessy, B.4    Ding, Z.5    Larrea, M.6
  • 92
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • Ravikumar B, Moreau K, Jahreiss L, Puri C, Rubinsztein DC. Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat Cell Biol 2010; 12: 747-757.
    • (2010) Nat Cell Biol , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 95
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009; 43: 67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 96
    • 84885638436 scopus 로고    scopus 로고
    • Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites
    • Tang Z, Lin MG, Stowe TR, Chen S, Zhu M, Stearns T et al. Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites. Nature 2013; 502: 254-257.
    • (2013) Nature , vol.502 , pp. 254-257
    • Tang, Z.1    Lin, M.G.2    Stowe, T.R.3    Chen, S.4    Zhu, M.5    Stearns, T.6
  • 97
    • 29444439981 scopus 로고    scopus 로고
    • Oral-facial-digital type i protein is required for primary cilia formation and left-right axis specification
    • Ferrante MI, Zullo A, Barra A, Bimonte S, Messaddeq N, Studer M et al. Oral-facial-digital type I protein is required for primary cilia formation and left-right axis specification. Nat Genet 2006; 38: 112-117.
    • (2006) Nat Genet , vol.38 , pp. 112-117
    • Ferrante, M.I.1    Zullo, A.2    Barra, A.3    Bimonte, S.4    Messaddeq, N.5    Studer, M.6
  • 99
    • 0030726894 scopus 로고    scopus 로고
    • Huntingtinassociated Protein 1 (HAP1) interacts with the p150 Glued Bubunit of Dynactin
    • Engelender S, Sharp AH, Colomer V, Tokito MK, Lanahan A, Worley P et al. Huntingtinassociated Protein 1 (HAP1) interacts with the p150Glued Bubunit of Dynactin. Hum Mol Genet 1997; 6: 2205-2212.
    • (1997) Hum Mol Genet , vol.6 , pp. 2205-2212
    • Engelender, S.1    Sharp, A.H.2    Colomer, V.3    Tokito, M.K.4    Lanahan, A.5    Worley, P.6
  • 100
    • 0028803757 scopus 로고
    • A huntingtin-associated protein enriched in brain with implications for pathology
    • Li X-J, Li S-H, Sharp AH, Nucifora FC, Schilling G, Lanahan A et al. A huntingtin-associated protein enriched in brain with implications for pathology. Nature 1995; 378: 398-402.
    • (1995) Nature , vol.378 , pp. 398-402
    • Li, X.-J.1    Li, S.-H.2    Sharp, A.H.3    Nucifora, F.C.4    Schilling, G.5    Lanahan, A.6
  • 101
    • 77949317804 scopus 로고    scopus 로고
    • Huntingtin-associated protein-1 interacts with probrain-derived neurotrophic factor and mediates its transport and release
    • Wu LL, Fan Y, Li S, Li X-J, Zhou X-F. Huntingtin-associated protein-1 interacts with probrain-derived neurotrophic factor and mediates its transport and release. J Biol Chem 2010; 285: 5614-5623.
    • (2010) J Biol Chem , vol.285 , pp. 5614-5623
    • Wu, L.L.1    Fan, Y.2    Li, S.3    Li, X.-J.4    Zhou, X.-F.5
  • 103
    • 0037191046 scopus 로고    scopus 로고
    • Assembly of centrosomal proteins and microtubule organization depends on PCM-1
    • Dammermann A, Merdes A. Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J Cell Biol 2002; 159: 255-266.
    • (2002) J Cell Biol , vol.159 , pp. 255-266
    • Dammermann, A.1    Merdes, A.2
  • 104
    • 56049117628 scopus 로고    scopus 로고
    • CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium
    • Kim J, Krishnaswami SR, Gleeson JG. CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium. Hum Mol Genet 2008; 17: 3796-3805.
    • (2008) Hum Mol Genet , vol.17 , pp. 3796-3805
    • Kim, J.1    Krishnaswami, S.R.2    Gleeson, J.G.3
  • 106
    • 84903627709 scopus 로고    scopus 로고
    • Impaired TrkB receptor signaling underlies corticostriatal dysfunction in Huntington's disease
    • Plotkin JL, Day M, Peterson JD, Xie Z, Kress GJ, Rafalovich I et al. Impaired TrkB receptor signaling underlies corticostriatal dysfunction in Huntington's disease. Neuron 2014; 83: 178-188.
    • (2014) Neuron , vol.83 , pp. 178-188
    • Plotkin, J.L.1    Day, M.2    Peterson, J.D.3    Xie, Z.4    Kress, G.J.5    Rafalovich, I.6
  • 107
    • 84875509193 scopus 로고    scopus 로고
    • Mutant huntingtin alters retrograde transport of TrkB receptors in striatal dendrites
    • Liot G, Zala D, Pla P, Mottet G, Piel M, Saudou F. Mutant huntingtin alters retrograde transport of TrkB receptors in striatal dendrites. J Neurosci Off J Soc Neurosci 2013; 33: 6298-6309.
    • (2013) J Neurosci off J Soc Neurosci , vol.33 , pp. 6298-6309
    • Liot, G.1    Zala, D.2    Pla, P.3    Mottet, G.4    Piel, M.5    Saudou, F.6
  • 108
    • 84876932695 scopus 로고    scopus 로고
    • Imbalance of p75(NTR)/TrkB protein expression in Huntington's disease: Implication for neuroprotective therapies
    • Brito V, Puigdellívol M, Giralt A, del Toro D, Alberch J, Ginés S. Imbalance of p75(NTR)/TrkB protein expression in Huntington's disease: implication for neuroprotective therapies. Cell Death Dis 2013; 4: e595.
    • (2013) Cell Death Dis , vol.4 , pp. e595
    • Brito, V.1    Puigdelli Vol, M.2    Giralt, A.3    Del Toro, D.4    Alberch, J.5    Gines, S.6
  • 109
    • 77954362528 scopus 로고    scopus 로고
    • Impaired TrkB-mediated ERK1/2 activation in huntington disease knock-in striatal cells involves reduced p52/p46 Shc expression
    • Ginés S, Paoletti P, Alberch J. Impaired TrkB-mediated ERK1/2 activation in huntington disease knock-in striatal cells involves reduced p52/p46 Shc expression. J Biol Chem 2010; 285: 21537-21548.
    • (2010) J Biol Chem , vol.285 , pp. 21537-21548
    • Ginés, S.1    Paoletti, P.2    Alberch, J.3
  • 110
    • 84901446307 scopus 로고    scopus 로고
    • BBS4 is necessary for ciliary localization of TrkB receptor and activation by BDNF
    • Leitch CC, Zaghloul NA. BBS4 is necessary for ciliary localization of TrkB receptor and activation by BDNF. PLoS ONE 2014; 9: e98687.
    • (2014) PLoS ONE , vol.9 , pp. e98687
    • Leitch, C.C.1    Zaghloul, N.A.2
  • 111
    • 77958150452 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor is localized to primary cilia in adult murine hippocampal dentate gyrus granule cells
    • Chakravarthy B, Gaudet C, Ménard M, Atkinson T, Chiarini A, Dal Prà I et al. The p75 neurotrophin receptor is localized to primary cilia in adult murine hippocampal dentate gyrus granule cells. Biochem Biophys Res Commun 2010; 401: 458-462.
    • (2010) Biochem Biophys Res Commun , vol.401 , pp. 458-462
    • Chakravarthy, B.1    Gaudet, C.2    Ménard, M.3    Atkinson, T.4    Chiarini, A.5    Dal Prà, I.6
  • 112
    • 84873340106 scopus 로고    scopus 로고
    • The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal
    • Maiuri T, Woloshansky T, Xia J, Truant R. The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal. Hum Mol Genet 2013; 22: 1383-1394.
    • (2013) Hum Mol Genet , vol.22 , pp. 1383-1394
    • Maiuri, T.1    Woloshansky, T.2    Xia, J.3    Truant, R.4
  • 114
    • 70449517408 scopus 로고    scopus 로고
    • Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse
    • Finetti F, Paccani SR, Riparbelli MG, Giacomello E, Perinetti G, Pazour GJ et al. Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse. Nat Cell Biol 2009; 11: 1332-1339.
    • (2009) Nat Cell Biol , vol.11 , pp. 1332-1339
    • Finetti, F.1    Paccani, S.R.2    Riparbelli, M.G.3    Giacomello, E.4    Perinetti, G.5    Pazour, G.J.6
  • 115
    • 75749090851 scopus 로고    scopus 로고
    • Intraflagellar transport: It's not just for cilia anymore
    • Baldari CT, Rosenbaum J. Intraflagellar transport: it's not just for cilia anymore. Curr Opin Cell Biol 2010; 22: 75-80.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 75-80
    • Baldari, C.T.1    Rosenbaum, J.2
  • 117
    • 84878545597 scopus 로고    scopus 로고
    • Ciliary secretion: Switching the cellular antenna totransmit
    • Avasthi P, Marshall W. Ciliary secretion: switching the cellular antenna to "transmit.". Curr Biol 2013; 23: R471-R473.
    • (2013) Curr Biol , vol.23 , pp. R471-R473
    • Avasthi, P.1    Marshall, W.2
  • 118
    • 84897606897 scopus 로고    scopus 로고
    • C. Elegans ciliated sensory neurons release extracellular vesicles that function in animal communication
    • Wang J, Silva M, Haas LA, Morsci NS, Nguyen KCQ, Hall DH et al. C. elegans ciliated sensory neurons release extracellular vesicles that function in animal communication. Curr Biol 2014; 24: 519-525.
    • (2014) Curr Biol , vol.24 , pp. 519-525
    • Wang, J.1    Silva, M.2    Haas, L.A.3    Morsci, N.S.4    Nguyen, K.C.Q.5    Hall, D.H.6
  • 119
    • 33847005413 scopus 로고    scopus 로고
    • Midbody and primary cilium of neural progenitors release extracellular membrane particles enriched in the stem cell marker prominin-1
    • Dubreuil V, Marzesco A-M, Corbeil D, Huttner WB, Wilsch-Braüninger M. Midbody and primary cilium of neural progenitors release extracellular membrane particles enriched in the stem cell marker prominin-1. J Cell Biol 2007; 176: 483-495.
    • (2007) J Cell Biol , vol.176 , pp. 483-495
    • Dubreuil, V.1    Marzesco, A.-M.2    Corbeil, D.3    Huttner, W.B.4    Wilsch-Braüninger, M.5
  • 121
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B, Diamond MI. Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 2010; 11: 155-159.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 122
    • 2942625910 scopus 로고    scopus 로고
    • Differential loss of striatal projection systems in Huntington's disease: A quantitative immunohistochemical study
    • Deng YP, Albin RL, Penney JB, Young AB, Anderson KD, Reiner A. Differential loss of striatal projection systems in Huntington's disease: a quantitative immunohistochemical study. J Chem Neuroanat 2004; 27: 143-164.
    • (2004) J Chem Neuroanat , vol.27 , pp. 143-164
    • Deng, Y.P.1    Albin, R.L.2    Penney, J.B.3    Young, A.B.4    Anderson, K.D.5    Reiner, A.6
  • 123
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010; 11: 301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 124
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo JL, Lee VMY. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 2014; 20: 130-138.
    • (2014) Nat Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.Y.2
  • 126
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • Desplats P, Lee H-J, Bae E-J, Patrick C, Rockenstein E, Crews L et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 2009; 106: 13010-13015.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.-J.2    Bae, E.-J.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6
  • 127
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284: 12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 128
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of Tau aggregation by fibrillar species
    • Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI. Trans-cellular propagation of Tau aggregation by fibrillar species. J Biol Chem 2012; 287: 19440-19451.
    • (2012) J Biol Chem , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 129
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in ALS
    • Polymenidou M, Cleveland DW. The seeds of neurodegeneration: prion-like spreading in ALS. Cell 2011; 147: 498-508.
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 130
    • 77956270117 scopus 로고    scopus 로고
    • Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis
    • Chia R, Tattum MH, Jones S, Collinge J, Fisher EMC, Jackson GS. Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis. PLoS ONE 2010; 5: e10627.
    • (2010) PLoS ONE , vol.5 , pp. e10627
    • Chia, R.1    Tattum, M.H.2    Jones, S.3    Collinge, J.4    Fisher, E.M.C.5    Jackson, G.S.6
  • 131
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions
    • Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N. A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. J Biol Chem 2011; 286: 18664-18672.
    • (2011) J Biol Chem , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 132
    • 84895796816 scopus 로고    scopus 로고
    • Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and-independent mechanisms
    • Grad LI, Yerbury JJ, Turner BJ, Guest WC, Pokrishevsky E, O'Neill MA et al. Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and-independent mechanisms. Proc Natl Acad Sci USA 2014; 111: 3620-3625.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 3620-3625
    • Grad, L.I.1    Yerbury, J.J.2    Turner, B.J.3    Guest, W.C.4    Pokrishevsky, E.5    O'Neill, M.A.6
  • 133
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren P-H, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11: 219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.-H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 134
    • 84883348572 scopus 로고    scopus 로고
    • Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes
    • Costanzo M, Abounit S, Marzo L, Danckaert A, Chamoun Z, Roux P et al. Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes. J Cell Sci 2013; 126: 3678-3685.
    • (2013) J Cell Sci , vol.126 , pp. 3678-3685
    • Costanzo, M.1    Abounit, S.2    Marzo, L.3    Danckaert, A.4    Chamoun, Z.5    Roux, P.6
  • 135
    • 84905023942 scopus 로고    scopus 로고
    • Transneuronal propagation of mutant huntingtin contributes to non-cell autonomous pathology in neurons
    • Pecho-Vrieseling E, Rieker C, Fuchs S, Bleckmann D, Esposito MS, Botta P et al. Transneuronal propagation of mutant huntingtin contributes to non-cell autonomous pathology in neurons. Nat Neurosci 2014; 17: 1064-1072.
    • (2014) Nat Neurosci , vol.17 , pp. 1064-1072
    • Pecho-Vrieseling, E.1    Rieker, C.2    Fuchs, S.3    Bleckmann, D.4    Esposito, M.S.5    Botta, P.6
  • 136
    • 84869109864 scopus 로고    scopus 로고
    • Pathological ?-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ et al. Pathological ?-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012; 338: 949-953.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 138
    • 84899944338 scopus 로고    scopus 로고
    • A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity
    • Ahmed Z, Cooper J, Murray TK, Garn K, McNaughton E, Clarke H et al. A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity. Acta Neuropathol (Berl) 2014; 127: 667-683.
    • (2014) Acta Neuropathol (Berl) , vol.127 , pp. 667-683
    • Ahmed, Z.1    Cooper, J.2    Murray, T.K.3    Garn, K.4    McNaughton, E.5    Clarke, H.6
  • 141
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M, Walker LC. Pathogenic protein seeding in alzheimer disease and other neurodegenerative disorders. Ann Neurol 2011; 70: 532-540.
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 142
    • 84905020137 scopus 로고    scopus 로고
    • Something wicked this way comes: Huntingtin
    • La Spada AR. Something wicked this way comes: huntingtin. Nat Neurosci 2014; 17: 1014-1015.
    • (2014) Nat Neurosci , vol.17 , pp. 1014-1015
    • La Spada, A.R.1
  • 143
    • 84927949614 scopus 로고    scopus 로고
    • Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain
    • Pearce MMP, Spartz EJ, Hong W, Luo L, Kopito RR. Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain. Nat Commun 2015; 6: 6768.
    • (2015) Nat Commun , vol.6 , pp. 6768
    • Pearce, M.M.P.1    Spartz, E.J.2    Hong, W.3    Luo, L.4    Kopito, R.R.5
  • 144
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
    • Li J-Y, Englund E, Holton JL, Soulet D, Hagell P, Lees AJ et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med 2008; 14: 501-503.
    • (2008) Nat Med , vol.14 , pp. 501-503
    • Li, J.-Y.1    Englund, E.2    Holton, J.L.3    Soulet, D.4    Hagell, P.5    Lees, A.J.6
  • 145
    • 77949820437 scopus 로고    scopus 로고
    • Characterization of Lewy body pathology in 12-and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease
    • Li J-Y, Englund E, Widner H, Rehncrona S, Björklund A, Lindvall O et al. Characterization of Lewy body pathology in 12-and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease. Mov Disord Off J Mov Disord Soc 2010; 25: 1091-1096.
    • (2010) Mov Disord off J Mov Disord Soc , vol.25 , pp. 1091-1096
    • Li, J.-Y.1    Englund, E.2    Widner, H.3    Rehncrona, S.4    Björklund, A.5    Lindvall, O.6
  • 147
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower JH, Chu Y, Hauser RA, Freeman TB, Olanow CW. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat Med 2008; 14: 504-506.
    • (2008) Nat Med , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 149
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 2004; 15: 1101-1111.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 150
    • 84892929122 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 regulates postnatal neurogenesis and neurotrophin receptor sorting
    • Xiang J, Yang H, Zhao T, Sun M, Xu X, Zhou X-F et al. Huntingtin-associated protein 1 regulates postnatal neurogenesis and neurotrophin receptor sorting. J Clin Invest 2014; 124: 85-98.
    • (2014) J Clin Invest , vol.124 , pp. 85-98
    • Xiang, J.1    Yang, H.2    Zhao, T.3    Sun, M.4    Xu, X.5    Zhou, X.-F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.