메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Aggrephagy: Selective disposal of protein aggregates by macroautophagy

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALPHA 1 ANTICHYMOTRYPSIN; ALPHA 1 ANTITRYPSIN; ANTITHROMBIN; ATAXIN 7; CHAPERONE; GLYCOGEN SYNTHASE KINASE 3BETA; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HUNTINGTIN; MITOGEN ACTIVATED PROTEIN KINASE; MUTANT PROTEIN; NEUROSERPIN; PEPTIDE; PROTEASOME; PROTEIN; PROTEIN KINASE B; TAU PROTEIN; UBIQUILIN 1; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84859736977     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2012/736905     Document Type: Review
Times cited : (377)

References (238)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson C. M., Protein folding and misfolding Nature 2003 426 6968 884 890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D., The emerging complexity of protein ubiquitination Biochemical Society Transactions 2009 37 5 937 953
    • (2009) Biochemical Society Transactions , vol.37 , Issue.5 , pp. 937-953
    • Komander, D.1
  • 3
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' Review Series
    • DOI 10.1038/embor.2008.93, PII EMBOR200893
    • Ikeda F., Dikic I., Atypical ubiquitin chains: new molecular signals. protein modifications: beyond the usual suspects review series EMBO Reports 2008 9 6 536 542 (Pubitemid 351772916)
    • (2008) EMBO Reports , vol.9 , Issue.6 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 5
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A., Heller H., Elias S., Ciechanover A., Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown Journal of Biological Chemistry 1983 258 13 8206 8214
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.13 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 6
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • DOI 10.1146/annurev.biochem.70.1.503
    • Pickart C. M., Mechanisms underlying ubiquitination Annual Review of Biochemistry 2001 70 503 533 (Pubitemid 32663902)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 7
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman B. A., Harper J. W., Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways Nature Reviews Molecular Cell Biology 2009 10 5 319 331
    • (2009) Nature Reviews Molecular Cell Biology , vol.10 , Issue.5 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 8
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (E2s): Deciding between life and death of proteins
    • Van Wijk S. J., Timmers H. T., The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins The FASEB Journal 2010 24 4 981 993
    • (2010) The FASEB Journal , vol.24 , Issue.4 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 9
    • 77749341438 scopus 로고    scopus 로고
    • Ubiquitin ligase complexes: From substrate selectivity to conjugational specificity
    • Nagy V., Dikic I., Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity Biological Chemistry 2010 391 2-3 163 169
    • (2010) Biological Chemistry , vol.391 , Issue.23 , pp. 163-169
    • Nagy, V.1    Dikic, I.2
  • 11
    • 59249084491 scopus 로고    scopus 로고
    • The proteasome: Overview of structure and functions
    • Tanaka K., The proteasome: overview of structure and functions Proceedings of the Japan Academy B 2009 85 1 12 36
    • (2009) Proceedings of the Japan Academy B , vol.85 , Issue.1 , pp. 12-36
    • Tanaka, K.1
  • 13
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D., Recognition and processing of ubiquitin-protein conjugates by the proteasome Annual Review of Biochemistry 2009 78 477 513
    • (2009) Annual Review of Biochemistry , vol.78 , pp. 477-513
    • Finley, D.1
  • 14
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • DOI 10.1101/gad.1599207
    • Mizushima N., Autophagy: process and function Genes and Development 2007 21 22 2861 2873 (Pubitemid 350133435)
    • (2007) Genes and Development , vol.21 , Issue.22 , pp. 2861-2873
    • Mizushima, N.1
  • 15
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima N., Levine B., Cuervo A. M., Klionsky D. J., Autophagy fights disease through cellular self-digestion Nature 2008 451 7182 1069 1075 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 17
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum
    • Mijaljica D., Prescott M., Devenish R. J., Microautophagy in mammalian cells: revisiting a 40-year-old conundrum Autophagy 2011 7 7 673 682
    • (2011) Autophagy , vol.7 , Issue.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 18
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J. F., Chaperone-mediated autophagy Autophagy 2007 3 295 299 (Pubitemid 46986334)
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 295-299
    • Dice, J.F.1
  • 19
    • 77950506157 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in health and disease
    • Kon M., Cuervo A. M., Chaperone-mediated autophagy in health and disease FEBS Letters 2010 584 7 1399 1404
    • (2010) FEBS Letters , vol.584 , Issue.7 , pp. 1399-1404
    • Kon, M.1    Cuervo, A.M.2
  • 21
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • DOI 10.1038/ncb1007-1102, PII NCB1007-1102
    • Xie Z., Klionsky D. J., Autophagosome formation: core machinery and adaptations Nature Cell Biology 2007 9 10 1102 1109 (Pubitemid 47500484)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 22
    • 79960878784 scopus 로고    scopus 로고
    • Atg8: An autophagy-related ubiquitin-like protein family
    • Shpilka T., Weidberg H., Pietrokovski S., Elazar Z., Atg8: an autophagy-related ubiquitin-like protein family Genome Biology 2011 12 7, article 226
    • (2011) Genome Biology , vol.12 , Issue.7 ARTICLE 226
    • Shpilka, T.1    Weidberg, H.2    Pietrokovski, S.3    Elazar, Z.4
  • 23
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a Ubiquitin-like Protein Required for Autophagosome Formation, Mediates Membrane Tethering and Hemifusion
    • DOI 10.1016/j.cell.2007.05.021, PII S0092867407006587
    • Nakatogawa H., Ichimura Y., Ohsumi Y., Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion Cell 2007 130 1 165 178 (Pubitemid 47031316)
    • (2007) Cell , vol.130 , Issue.1 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 24
    • 3242888703 scopus 로고    scopus 로고
    • LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
    • DOI 10.1242/jcs.01131
    • Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T., LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation Journal of Cell Science 2004 117 13 2805 2812 (Pubitemid 38997262)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2805-2812
    • Kabeya, Y.1    Mizushima, N.2    Yamamoto, A.3    Oshitani-Okamoto, S.4    Ohsumi, Y.5    Yoshimori, T.6
  • 25
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitin-mediated recognition and beyond
    • Kraft C., Peter M., Hofmann K., Selective autophagy: ubiquitin-mediated recognition and beyond Nature Cell Biology 2010 12 9 836 841
    • (2010) Nature Cell Biology , vol.12 , Issue.9 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 26
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T., Lamark T., Selective autophagy mediated by autophagic adapter proteins Autophagy 2011 7 3 279 296
    • (2011) Autophagy , vol.7 , Issue.3 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 27
    • 65549142204 scopus 로고    scopus 로고
    • A Role for Ubiquitin in Selective Autophagy
    • Kirkin V., McEwan D. G., Novak I., Dikic I., A Role for Ubiquitin in Selective Autophagy Molecular Cell 2009 34 3 259 269
    • (2009) Molecular Cell , vol.34 , Issue.3 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 28
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjrky G., Lamark T., Brech A., Outzen H., Perander M., vervatn A., Stenmark H., Johansen T., p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death Journal of Cell Biology 2005 171 4 603 614 (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 33
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • Arrasate M., Mitra S., Schweitzer E. S., Segal M. R., Finkbeiner S., Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 2004 431 7010 805 810 (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 34
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R. R., Aggresomes, inclusion bodies and protein aggregation Trends in Cell Biology 2000 10 12 524 530
    • (2000) Trends in Cell Biology , vol.10 , Issue.12 , pp. 524-530
    • Kopito, R.R.1
  • 35
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey B., Lansbury P. T., Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annual Review of Neuroscience 2003 26 267 298 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 36
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F., Dobson C. M., Protein misfolding, functional amyloid, and human disease Annual Review of Biochemistry 2006 75 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 37
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z., Daz-Hernndez M., Maynard C. J., Hernndez F., Dantuma N. P., Lucas J. J., Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation Journal of Neuroscience 2010 30 10 3675 3688
    • (2010) Journal of Neuroscience , vol.30 , Issue.10 , pp. 3675-3688
    • Ortega, Z.1    Daz-Hernndez, M.2    Maynard, C.J.3    Hernndez, F.4    Dantuma, N.P.5    Lucas, J.J.6
  • 38
    • 80052830376 scopus 로고    scopus 로고
    • Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes
    • Zhang X., Qian S. -B., Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes Molecular Biology of the Cell 2011 22 18 3277 3288
    • (2011) Molecular Biology of the Cell , vol.22 , Issue.18 , pp. 3277-3288
    • Zhang, X.1    Qian, S.-B.2
  • 39
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • Rubinsztein D. C., The roles of intracellular protein-degradation pathways in neurodegeneration Nature 2006 443 7113 780 786 (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 40
    • 78651282673 scopus 로고    scopus 로고
    • P62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
    • Itakura E., Mizushima N., p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding Journal of Cell Biology 2011 192 1 17 27
    • (2011) Journal of Cell Biology , vol.192 , Issue.1 , pp. 17-27
    • Itakura, E.1    Mizushima, N.2
  • 41
    • 34250828455 scopus 로고    scopus 로고
    • Proteomic analysis of membrane-associated proteins from rat liver autophagosomes
    • verbye A., Fengsrud M., Seglen P. O., Proteomic analysis of membrane-associated proteins from rat liver autophagosomes Autophagy 2007 3 4 300 322 (Pubitemid 46986335)
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 300-322
    • Overbye, A.1    Fengsrud, M.2    Seglen, P.O.3
  • 43
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y., A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation Molecular Cell 2011 42 6 758 770
    • (2011) Molecular Cell , vol.42 , Issue.6 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 44
    • 77950224150 scopus 로고    scopus 로고
    • Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage
    • Pratt W. B., Morishima Y., Peng H. M., Osawa Y., Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage Experimental Biology and Medicine 2010 235 3 278 289
    • (2010) Experimental Biology and Medicine , vol.235 , Issue.3 , pp. 278-289
    • Pratt, W.B.1    Morishima, Y.2    Peng, H.M.3    Osawa, Y.4
  • 50
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • Kaushik S., Massey A. C., Mizushima N., Cuervo A. M., Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy Molecular Biology of the Cell 2008 19 5 2179 2192
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.5 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.C.2    Mizushima, N.3    Cuervo, A.M.4
  • 52
    • 57049094929 scopus 로고    scopus 로고
    • Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease
    • DOI 10.1093/hmg/ddn292
    • Raben N., Hill V., Shea L., Takikita S., Baum R., Mizushima N., Ralston E., Plotz P., Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease Human Molecular Genetics 2008 17 24 3897 3908 (Pubitemid 352762852)
    • (2008) Human Molecular Genetics , vol.17 , Issue.24 , pp. 3897-3908
    • Raben, N.1    Hill, V.2    Shea, L.3    Takikita, S.4    Baum, R.5    Mizushima, N.6    Ralston, E.7    Plotz, P.8
  • 56
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice J. F., Peptide sequences that target cytosolic proteins for lysosomal proteolysis Trends in Biochemical Sciences 1990 15 8 305 309 (Pubitemid 20223216)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.8 , pp. 305-309
    • Dice, J.F.1
  • 57
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • DOI 10.1091/mbc.E04-06-0477
    • Kiffin R., Christian C., Knecht E., Cuervo A. M., Activation of chaperone-mediated autophagy during oxidative stress Molecular Biology of the Cell 2004 15 11 4829 4840 (Pubitemid 39392200)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 58
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C. A., Connell P., Wu Y., Hu Z., Thompson L. J., Yin L. Y., Patterson C., Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Molecular and Cellular Biology 1999 19 6 4535 4545 (Pubitemid 29242026)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 59
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • DOI 10.1038/35050618
    • Connell P., Ballinger C. A., Jiang J., Wu Y., Thompson L. J., Hhfeld J., Patterson C., The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins Nature Cell Biology 2001 3 1 93 96 (Pubitemid 32114838)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6    Patterson, C.7
  • 60
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham G. C., Patterson C., Zhang W., Younger J. M., Cyr D. M., The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Nature Cell Biology 2001 3 1 100 105 (Pubitemid 32114840)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 62
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisted degradation: Multiple paths to destruction
    • Kettern N., Dreiseidler M., Tawo R., Hhfeld J., Chaperone-assisted degradation: multiple paths to destruction Biological Chemistry 2010 391 5 481 489
    • (2010) Biological Chemistry , vol.391 , Issue.5 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Hhfeld, J.4
  • 63
    • 38349105324 scopus 로고    scopus 로고
    • HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy
    • Carra S., Seguin S. J., Lambert H., Landry J., HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy Journal of Biological Chemistry 2008 283 3 1437 1444
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.3 , pp. 1437-1444
    • Carra, S.1    Seguin, S.J.2    Lambert, H.3    Landry, J.4
  • 68
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • Gamerdinger M., Hajieva P., Kaya A. M., Wolfrum U., Hartl F. U., Behl C., Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3 The EMBO Journal 2009 28 7 889 901
    • (2009) The EMBO Journal , vol.28 , Issue.7 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hartl, F.U.5    Behl, C.6
  • 69
    • 1442358797 scopus 로고    scopus 로고
    • Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins
    • DOI 10.1083/jcb.200312073
    • Lelouard H., Ferrand V., Marguet D., Bania J., Camosseto V., David A., Gatti E., Pierre P., Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins Journal of Cell Biology 2004 164 5 667 675 (Pubitemid 38282951)
    • (2004) Journal of Cell Biology , vol.164 , Issue.5 , pp. 667-675
    • Lelouard, H.1    Ferrand, V.2    Marguet, D.3    Bania, J.4    Camosseto, V.5    David, A.6    Gatti, E.7    Pierre, P.8
  • 70
    • 0037046536 scopus 로고    scopus 로고
    • Transient aggregation of ubiquitinated proteins during dendritic cell maturation
    • DOI 10.1038/417177a
    • Lelouard H., Gatti E., Cappello F., Gresser O., Camosseto V., Pierre P., Transient aggregation of ubiquitinated proteins during dendritic cell maturation Nature 2002 417 6885 177 182 (Pubitemid 34506798)
    • (2002) Nature , vol.417 , Issue.6885 , pp. 177-182
    • Lelouard, H.1    Gatti, E.2    Cappello, F.3    Gresser, O.4    Camosseto, V.5    Pierre, P.6
  • 72
    • 79251634318 scopus 로고    scopus 로고
    • The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells
    • Kettern N., Rogon C., Limmer A., Schild H., Hhfeld J., The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells Plos ONE 2011 6 1
    • (2011) Plos ONE , vol.6 , Issue.1
    • Kettern, N.1    Rogon, C.2    Limmer, A.3    Schild, H.4    Hhfeld, J.5
  • 73
    • 77249112669 scopus 로고    scopus 로고
    • Antigen processing via autophagy - Not only for MHC class II presentation anymore?
    • Munz C., Antigen processing via autophagy-not only for MHC class II presentation anymore? Current Opinion in Immunology 2010 22 1 89 93
    • (2010) Current Opinion in Immunology , vol.22 , Issue.1 , pp. 89-93
    • Munz, C.1
  • 74
    • 84859119158 scopus 로고    scopus 로고
    • Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation
    • Wenger T., Terawaki S., Camosseto V., Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation Autophagy 2012 8 3
    • (2012) Autophagy , vol.8 , Issue.3
    • Wenger, T.1    Terawaki, S.2    Camosseto, V.3
  • 75
    • 34047179973 scopus 로고    scopus 로고
    • Ubiquitinated-protein aggregates form in pancreatic β-cells during diabetes-induced oxidative stress and are regulated by autophagy
    • DOI 10.2337/db06-1160
    • Kaniuk N. A., Kiraly M., Bates H., Vranic M., Volchuk A., Brumell J. H., Ubiquitinated-protein aggregates form in pancreatic -cells during diabetes-induced oxidative stress and are regulated by autophagy Diabetes 2007 56 4 930 939 (Pubitemid 46525060)
    • (2007) Diabetes , vol.56 , Issue.4 , pp. 930-939
    • Kaniuk, N.A.1    Kiraly, M.2    Bates, H.3    Vranic, M.4    Volchuk, A.5    Brumell, J.H.6
  • 76
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • DOI 10.1083/jcb.143.7.1883
    • Johnston J. A., Ward C. L., Kopito R. R., Aggresomes: a cellular response to misfolded proteins Journal of Cell Biology 1998 143 7 1883 1898 (Pubitemid 29022611)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 77
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y., Kovacs J. J., McLaurin A., Vance J. M., Ito A., Yao T. P., The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress Cell 2003 115 6 727 738 (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 78
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J., Misfolded proteins partition between two distinct quality control compartments Nature 2008 454 7208 1088 1095
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 81
    • 77953139736 scopus 로고    scopus 로고
    • Fighting disease by selective autophagy of aggregate-prone proteins
    • Knvelsrud H., Simonsen A., Fighting disease by selective autophagy of aggregate-prone proteins FEBS Letters 2010 584 12 2635 2645
    • (2010) FEBS Letters , vol.584 , Issue.12 , pp. 2635-2645
    • Knvelsrud, H.1    Simonsen, A.2
  • 82
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated Huntingtin
    • DOI 10.1074/jbc.M508786200
    • Iwata A., Riley B. E., Johnston J. A., Kopito R. R., HDAC6 and microtubules are required for autophagic degradation of aggregated Huntingtin Journal of Biological Chemistry 2005 280 48 40282 40292 (Pubitemid 41779165)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 83
    • 79952843826 scopus 로고    scopus 로고
    • The role of ubiquitin in autophagy-dependent protein aggregate processing
    • Yao T., The role of ubiquitin in autophagy-dependent protein aggregate processing Genes and Cancer 2010 1 7 779 786
    • (2010) Genes and Cancer , vol.1 , Issue.7 , pp. 779-786
    • Yao, T.1
  • 84
    • 41549114279 scopus 로고    scopus 로고
    • The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease
    • Pan T., Kondo S., Le W., Jankovic J., The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease Brain 2008 131 8 1969 1978
    • (2008) Brain , vol.131 , Issue.8 , pp. 1969-1978
    • Pan, T.1    Kondo, S.2    Le, W.3    Jankovic, J.4
  • 85
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • DOI 10.1083/jcb.200611128
    • Olzmann J. A., Li A., Chudaev M. V., Chen J., Perez F. A., Palmiter R. D., Chin L. S., Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6 Journal of Cell Biology 2007 178 6 1025 1038 (Pubitemid 47443324)
    • (2007) Journal of Cell Biology , vol.178 , Issue.6 , pp. 1025-1038
    • Olzmann, J.A.1    Li, A.2    Chudaev, M.V.3    Chen, J.4    Perez, F.A.5    Palmiter, R.D.6    Chin, L.-S.7
  • 87
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger M., Kaya A. M., Wolfrum U., Clement A. M., Behl C., BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins EMBO Reports 2011 12 2 149 156
    • (2011) EMBO Reports , vol.12 , Issue.2 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 89
    • 84855195340 scopus 로고    scopus 로고
    • Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways
    • Dargemont C., Ossareh-Nazari B., Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways Biochimica et Biophysica Acta 2012 1823 1 138 144
    • (2012) Biochimica et Biophysica Acta , vol.1823 , Issue.1 , pp. 138-144
    • Dargemont, C.1    Ossareh-Nazari, B.2
  • 90
    • 0742323006 scopus 로고    scopus 로고
    • Distinct Roles for the AAA ATPases NSF and p97 in the Secretory Pathway
    • DOI 10.1091/mbc.E03-02-0097
    • Dalal S., Rosser M. F. N., Cyr D. M., Hanson P. I., Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway Molecular Biology of the Cell 2004 15 2 637 648 (Pubitemid 38146480)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.N.2    Cyr, D.M.3    Hanson, P.I.4
  • 91
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • DOI 10.1091/mbc.E06-05-0432
    • Wjcik C., Rowicka M., Kudlicki A., Nowis D., McConnell E., Kujawa M., DeMartino G. N., Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells Molecular Biology of the Cell 2006 17 11 4606 4618 (Pubitemid 44665732)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4606-4618
    • Wojcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5    Kujawa, M.6    DeMartino, G.N.7
  • 92
    • 18544394748 scopus 로고    scopus 로고
    • RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis
    • DOI 10.1242/jcs.00841
    • Wjcik C., Yano M., DeMartino G. N., RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis Journal of Cell Science 2004 117 2 281 292 (Pubitemid 38128906)
    • (2004) Journal of Cell Science , vol.117 , Issue.2 , pp. 281-292
    • Wojcik, C.1    Yano, M.2    DeMartino, G.N.3
  • 94
    • 0037084028 scopus 로고    scopus 로고
    • UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates
    • DOI 10.1093/emboj/21.4.615
    • Braun S., Matuschewski K., Rape M., Thoms S., Jentsch S., Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates The EMBO Journal 2002 21 4 615 621 (Pubitemid 34174042)
    • (2002) EMBO Journal , vol.21 , Issue.4 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 95
    • 37549068963 scopus 로고    scopus 로고
    • Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
    • Ramadan K., Bruderer R., Spiga F. M., Popp O., Baur T., Gotta M., Meyer H. H., Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin Nature 2007 450 7173 1258 1262
    • (2007) Nature , vol.450 , Issue.7173 , pp. 1258-1262
    • Ramadan, K.1    Bruderer, R.2    Spiga, F.M.3    Popp, O.4    Baur, T.5    Gotta, M.6    Meyer, H.H.7
  • 96
    • 0035977095 scopus 로고    scopus 로고
    • UFD1/NPL4, a ubiquitin-selective chaperone
    • DOI 10.1016/S0092-8674(01)00595-5
    • Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S., Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48UFD1/NPL4, a ubiquitin-selective chaperone Cell 2001 107 5 667 677 (Pubitemid 34014867)
    • (2001) Cell , vol.107 , Issue.5 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 97
    • 80455164551 scopus 로고    scopus 로고
    • Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant -1 antitrypsin from the endoplasmic reticulum
    • Greenblatt E. J., Olzmann J. A., Kopito R. R., Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant -1 antitrypsin from the endoplasmic reticulum Nature Structural and Molecular Biology 2011 18 10 1147 1152
    • (2011) Nature Structural and Molecular Biology , vol.18 , Issue.10 , pp. 1147-1152
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 98
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch C., Gauss R., Horn S. C., Neuber O., Sommer T., The ubiquitylation machinery of the endoplasmic reticulum Nature 2009 458 7237 453 460
    • (2009) Nature , vol.458 , Issue.7237 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 100
    • 79551663809 scopus 로고    scopus 로고
    • The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
    • Xu S., Peng G., Wang Y., Fang S., Karbowsk M., The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover Molecular Biology of the Cell 2011 22 3 291 300
    • (2011) Molecular Biology of the Cell , vol.22 , Issue.3 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowsk, M.5
  • 101
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk V. I., Mansilla A., Menzies F. M., Rubinsztein D. C., Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates Molecular Cell 2009 33 4 517 527
    • (2009) Molecular Cell , vol.33 , Issue.4 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 102
    • 57649198447 scopus 로고    scopus 로고
    • Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease
    • Ju J. S., Miller S. E., Hanson P. I., Weihl C. C., Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease Journal of Biological Chemistry 2008 283 44 30289 30299
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.44 , pp. 30289-30299
    • Ju, J.S.1    Miller, S.E.2    Hanson, P.I.3    Weihl, C.C.4
  • 103
    • 30644465041 scopus 로고    scopus 로고
    • Dominant-negative effect of mutant valosin-containing protein in aggresome formation
    • DOI 10.1016/j.febslet.2005.12.044, PII S001457930501519X
    • Kitami M. I., Kitami T., Nagahama M., Tagaya M., Hori S., Kakizuka A., Mizuno Y., Hattori N., Dominant-negative effect of mutant valosin-containing protein in aggresome formation FEBS Letters 2006 580 2 474 478 (Pubitemid 43089674)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 474-478
    • Kitami, M.-I.1    Kitami, T.2    Nagahama, M.3    Tagaya, M.4    Hori, S.5    Kakizuka, A.6    Mizuno, Y.7    Hattori, N.8
  • 104
    • 34250735508 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein (VCP)/p97 in the formation and clearance of abnormal protein aggregates
    • DOI 10.1111/j.1365-2443.2007.01099.x
    • Kobayashi T., Manno A., Kakizuka A., Involvement of valosin-containing protein (VCP)/p97 in the formation and clearance of abnormal protein aggregates Genes to Cells 2007 12 7 889 901 (Pubitemid 46965402)
    • (2007) Genes to Cells , vol.12 , Issue.7 , pp. 889-901
    • Kobayashi, T.1    Manno, A.2    Kakizuka, A.3
  • 106
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E., Salomons F. A., Vesa J., Bott L. C., Kimonis V., Yao T. P., Dantuma N. P., Taylor J. P., VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD Autophagy 2010 6 2 217 227
    • (2010) Autophagy , vol.6 , Issue.2 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 107
    • 77953894192 scopus 로고    scopus 로고
    • Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: A disorder of autophagy
    • Ju J. S., Weihl C. C., Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy Human Molecular Genetics 2010 19 1 R38 R45
    • (2010) Human Molecular Genetics , vol.19 , Issue.1
    • Ju, J.S.1    Weihl, C.C.2
  • 108
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
    • Tang W. K., Li D., Li C. C., Esser L., Dai R., Guo L., Xia D., A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants The EMBO Journal 2010 29 13 2217 2229
    • (2010) The EMBO Journal , vol.29 , Issue.13 , pp. 2217-2229
    • Tang, W.K.1    Li, D.2    Li, C.C.3    Esser, L.4    Dai, R.5    Guo, L.6    Xia, D.7
  • 109
    • 77953121380 scopus 로고    scopus 로고
    • Imbalances in p97 co-factor interactions in human proteinopathy
    • Fernndez-Siz V., Buchberger A., Imbalances in p97 co-factor interactions in human proteinopathy EMBO Reports 2010 11 6 479 485
    • (2010) EMBO Reports , vol.11 , Issue.6 , pp. 479-485
    • Fernndez-Siz, V.1    Buchberger, A.2
  • 110
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
    • DOI 10.1093/hmg/ddi426
    • Weihl C. C., Dalal S., Pestronk A., Hanson P. I., Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation Human Molecular Genetics 2006 15 2 189 199 (Pubitemid 43125974)
    • (2006) Human Molecular Genetics , vol.15 , Issue.2 , pp. 189-199
    • Weihl, C.C.1    Dalal, S.2    Pestronk, A.3    Hanson, P.I.4
  • 111
    • 34447093377 scopus 로고    scopus 로고
    • Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
    • DOI 10.1093/hmg/ddm037
    • Weihl C. C., Miller S. E., Hanson P. I., Pestronk A., Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice Human Molecular Genetics 2007 16 8 919 928 (Pubitemid 47062736)
    • (2007) Human Molecular Genetics , vol.16 , Issue.8 , pp. 919-928
    • Weihl, C.C.1    Miller, S.E.2    Hanson, P.I.3    Pestronk, A.4
  • 112
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • DOI 10.1016/S0962-8924(02)02269-9, PII S0962892402022699
    • Buchberger A., From UBA to UBX: new words in the ubiquitin vocabulary Trends in Cell Biology 2002 12 5 216 221 (Pubitemid 34327613)
    • (2002) Trends in Cell Biology , vol.12 , Issue.5 , pp. 216-221
    • Buchberger, A.1
  • 113
    • 0037065732 scopus 로고    scopus 로고
    • Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a
    • DOI 10.1021/bi011892y
    • Walters K. J., Kleijnen M. F., Goh A. M., Wagner G., Howley P. M., Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a Biochemistry 2002 41 6 1767 1777 (Pubitemid 34132251)
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1767-1777
    • Walters, K.J.1    Kleijnen, M.F.2    Goh, A.M.3    Wagner, G.4    Howley, P.M.5
  • 116
  • 119
    • 33644771265 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin
    • DOI 10.1093/hmg/ddl017
    • Wang H., Lim P. J., Yin C., Rieckher M., Vogel B. E., Monteiro M. J., Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin Human Molecular Genetics 2006 15 6 1025 1041 (Pubitemid 43338242)
    • (2006) Human Molecular Genetics , vol.15 , Issue.6 , pp. 1025-1041
    • Wang, H.1    Lim, P.J.2    Yin, C.3    Rieckher, M.4    Vogel, B.E.5    Monteiro, M.J.6
  • 120
    • 34447095637 scopus 로고    scopus 로고
    • Ubiquilin interacts and enhances the degradation of expanded- polyglutamine proteins
    • DOI 10.1016/j.bbrc.2007.06.097, PII S0006291X07013046
    • Wang H., Monteiro M. J., Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins Biochemical and Biophysical Research Communications 2007 360 2 423 427 (Pubitemid 47030361)
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , Issue.2 , pp. 423-427
    • Wang, H.1    Monteiro, M.J.2
  • 121
    • 66349128939 scopus 로고    scopus 로고
    • Ubiquilins accelerate autophagosome maturation and promote cell survival during nutrient starvation
    • N'Diaye E. N., Debnath J., Brown E. J., Ubiquilins accelerate autophagosome maturation and promote cell survival during nutrient starvation Autophagy 2009 5 4 573 575
    • (2009) Autophagy , vol.5 , Issue.4 , pp. 573-575
    • N'Diaye, E.N.1    Debnath, J.2    Brown, E.J.3
  • 122
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation
    • N'Diaye E. N., Kajihara K. K., Hsieh I., Morisaki H., Debnath J., Brown E. J., PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation EMBO Reports 2009 10 2 173 179
    • (2009) EMBO Reports , vol.10 , Issue.2 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6
  • 127
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda N. N., Ohsumi Y., Inagaki F., Atg8-family interacting motif crucial for selective autophagy FEBS Letters 2010 584 7 1379 1385
    • (2010) FEBS Letters , vol.584 , Issue.7 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 128
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • DOI 10.1016/S1097-2765(03)00246-6
    • Wilson M. I., Gill D. J., Perisic O., Quinn M. T., Williams R. L., PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62 Molecular Cell 2003 12 1 39 50 (Pubitemid 36957832)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 129
    • 80052363973 scopus 로고    scopus 로고
    • Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic adapters NBR1 and p62/SQSTM1
    • Svenning S., Lamark T., Krause K., Johansen T., Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic adapters NBR1 and p62/SQSTM1 Autophagy 2011 7 9 993 1010
    • (2011) Autophagy , vol.7 , Issue.9 , pp. 993-1010
    • Svenning, S.1    Lamark, T.2    Krause, K.3    Johansen, T.4
  • 130
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T., Wang K., Cao Y., Baba M., Klionsky D. J., Atg32 is a mitochondrial protein that confers selectivity during mitophagy Developmental Cell 2009 17 1 98 109
    • (2009) Developmental Cell , vol.17 , Issue.1 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 131
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K., Kondo-Okamoto N., Ohsumi Y., Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy Developmental Cell 2009 17 1 87 97
    • (2009) Developmental Cell , vol.17 , Issue.1 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 133
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston T. L., Ryzhakov G., Bloor S., von Muhlinen N., Randow F., The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria Nature Immunology 2009 10 11 1215 1221
    • (2009) Nature Immunology , vol.10 , Issue.11 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 135
    • 80053338210 scopus 로고    scopus 로고
    • Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1
    • Jiang S., Wells C. D., Roach P. J., Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1 Biochemical and Biophysical Research Communications 2011 413 3 420 425
    • (2011) Biochemical and Biophysical Research Communications , vol.413 , Issue.3 , pp. 420-425
    • Jiang, S.1    Wells, C.D.2    Roach, P.J.3
  • 137
    • 79961142199 scopus 로고    scopus 로고
    • P62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate
    • Watanabe Y., Tanaka M., p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate Journal of Cell Science 2011 124 16 2692 2701
    • (2011) Journal of Cell Science , vol.124 , Issue.16 , pp. 2692-2701
    • Watanabe, Y.1    Tanaka, M.2
  • 139
    • 58249085224 scopus 로고    scopus 로고
    • SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans
    • Zhang Y., Yan L., Zhou Z., Yang P., Tian E., Zhang K., Zhao Y., Li Z., Song B., Han J., Miao L., Zhang H., SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans Cell 2009 136 2 308 321
    • (2009) Cell , vol.136 , Issue.2 , pp. 308-321
    • Zhang, Y.1    Yan, L.2    Zhou, Z.3    Yang, P.4    Tian, E.5    Zhang, K.6    Zhao, Y.7    Li, Z.8    Song, B.9    Han, J.10    Miao, L.11    Zhang, H.12
  • 141
    • 58149344946 scopus 로고    scopus 로고
    • Midbody ring disposal by autophagy is a post-abscission event of cytokinesis
    • Pohl C., Jentsch S., Midbody ring disposal by autophagy is a post-abscission event of cytokinesis Nature Cell Biology 2009 11 1 65 70
    • (2009) Nature Cell Biology , vol.11 , Issue.1 , pp. 65-70
    • Pohl, C.1    Jentsch, S.2
  • 145
    • 79955949858 scopus 로고    scopus 로고
    • The elimination of accumulated and aggregated proteins: A role for aggrephagy in neurodegeneration
    • Yamamoto A., Simonsen A., The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration Neurobiology of Disease 2011 43 1 17 28
    • (2011) Neurobiology of Disease , vol.43 , Issue.1 , pp. 17-28
    • Yamamoto, A.1    Simonsen, A.2
  • 146
    • 79953163464 scopus 로고    scopus 로고
    • The three musketeers of autophagy: Phosphorylation, ubiquitylation and acetylation
    • McEwan D. G., Dikic I., The three musketeers of autophagy: phosphorylation, ubiquitylation and acetylation Trends in Cell Biology 2011 21 4 195 201
    • (2011) Trends in Cell Biology , vol.21 , Issue.4 , pp. 195-201
    • McEwan, D.G.1    Dikic, I.2
  • 147
    • 38949162988 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy
    • Tan J. M., Wong E. S., Dawson V. L., Dawson T. M., Lim K. L., Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy Autophagy 2008 4 2 251 253 (Pubitemid 351231194)
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 251-253
    • Tan, J.M.M.1    Wong, E.S.P.2    Dawson, V.L.3    Dawson, T.M.4    Lim, K.-L.5
  • 149
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • DOI 10.1128/MCB.24.18.8055-8068.2004
    • Seibenhener M. L., Babu J. R., Geetha T., Wong H. C., Krishna N. R., Wooten M. W., Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation Molecular and Cellular Biology 2004 24 18 8055 8068 (Pubitemid 39167456)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.18 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 150
    • 33846692198 scopus 로고    scopus 로고
    • Signal integration and diversification through the p62 scaffold protein
    • DOI 10.1016/j.tibs.2006.12.002, PII S0968000406003276
    • Moscat J., Diaz-Meco M. T., Wooten M. W., Signal integration and diversification through the p62 scaffold protein Trends in Biochemical Sciences 2007 32 2 95 100 (Pubitemid 46199192)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.2 , pp. 95-100
    • Moscat, J.1    Diaz-Meco, M.T.2    Wooten, M.W.3
  • 153
    • 74249103961 scopus 로고    scopus 로고
    • Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3
    • Menzies F. M., Huebener J., Renna M., Bonin M., Riess O., Rubinsztein D. C., Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3 Brain 2010 133 1 93 104
    • (2010) Brain , vol.133 , Issue.1 , pp. 93-104
    • Menzies, F.M.1    Huebener, J.2    Renna, M.3    Bonin, M.4    Riess, O.5    Rubinsztein, D.C.6
  • 156
    • 77956526505 scopus 로고    scopus 로고
    • TRAF6 promotes atypical ubiquitination of mutant DJ-1 and alpha-synuclein and is localized to Lewy bodies in sporadic Parkinson's disease brains
    • Zucchelli S., Codrich M., Marcuzzi F., Pinto M., Vilotti S., Biagioli M., Ferrer I., Gustincich S., TRAF6 promotes atypical ubiquitination of mutant DJ-1 and alpha-synuclein and is localized to Lewy bodies in sporadic Parkinson's disease brains Human Molecular Genetics 2010 19 19 3759 3770
    • (2010) Human Molecular Genetics , vol.19 , Issue.19 , pp. 3759-3770
    • Zucchelli, S.1    Codrich, M.2    Marcuzzi, F.3    Pinto, M.4    Vilotti, S.5    Biagioli, M.6    Ferrer, I.7    Gustincich, S.8
  • 157
    • 77953858790 scopus 로고    scopus 로고
    • TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced Autophagy
    • Shi C. S., Kehrl J. H., TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced Autophagy Science Signaling 2010 3 123, article ra42
    • (2010) Science Signaling , vol.3 , Issue.123 ARTICLE RA42
    • Shi, C.S.1    Kehrl, J.H.2
  • 159
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto G., Wada K., Okuno M., Kurosawa M., Nukina N., Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins Molecular Cell 2011 44 2 279 289
    • (2011) Molecular Cell , vol.44 , Issue.2 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 162
    • 84855204007 scopus 로고    scopus 로고
    • Optineurin in Huntington's disease intranuclear inclusions
    • Schwab C., Yu S., McGeer E. G., McGeer P. L., Optineurin in Huntington's disease intranuclear inclusions Neuroscience Letters 2012 506 1 149 154
    • (2012) Neuroscience Letters , vol.506 , Issue.1 , pp. 149-154
    • Schwab, C.1    Yu, S.2    McGeer, E.G.3    McGeer, P.L.4
  • 164
    • 65249106104 scopus 로고    scopus 로고
    • Regulation of autophagy by the p300 acetyltransferase
    • Lee I. H., Finkel T., Regulation of autophagy by the p300 acetyltransferase Journal of Biological Chemistry 2009 284 10 6322 6328
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.10 , pp. 6322-6328
    • Lee, I.H.1    Finkel, T.2
  • 167
    • 77955352128 scopus 로고    scopus 로고
    • Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy
    • Fan W., Tang Z., Chen D., Moughon D., Ding X., Chen S., Zhu M., Zhong Q., Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy Autophagy 2010 6 5 614 621
    • (2010) Autophagy , vol.6 , Issue.5 , pp. 614-621
    • Fan, W.1    Tang, Z.2    Chen, D.3    Moughon, D.4    Ding, X.5    Chen, S.6    Zhu, M.7    Zhong, Q.8
  • 168
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain A., Lamark T., Sjttem E., Larsen K. B., Awuh J. A., vervatn A., McMahon M., Hayes J. D., Johansen T., p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription Journal of Biological Chemistry 2010 285 29 22576 22591
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.29 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjttem, E.3    Larsen, K.B.4    Awuh, J.A.5    Vervatn, A.6    McMahon, M.7    Hayes, J.D.8    Johansen, T.9
  • 171
    • 28844501852 scopus 로고    scopus 로고
    • Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins
    • DOI 10.1016/j.bbrc.2005.11.095, PII S0006291X05026070
    • Nakaso K., Nakamura C., Sato H., Imamura K., Takeshima T., Nakashima K., Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins Biochemical and Biophysical Research Communications 2006 339 3 915 922 (Pubitemid 41772899)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.3 , pp. 915-922
    • Nakaso, K.1    Nakamura, C.2    Sato, H.3    Imamura, K.4    Takeshima, T.5    Nakashima, K.6
  • 172
    • 2442585133 scopus 로고    scopus 로고
    • Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: Possible mechanisms and the role in Lewy body formation in Parkinson's disease
    • DOI 10.1016/j.brainres.2004.03.029, PII S0006899304004743
    • Nakaso K., Yoshimoto Y., Nakano T., Takeshima T., Fukuhara Y., Yasui K., Araga S., Yanagawa T., Ishii T., Nakashima K., Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease Brain Research 2004 1012 1-2 42 51 (Pubitemid 38648897)
    • (2004) Brain Research , vol.1012 , Issue.1-2 , pp. 42-51
    • Nakaso, K.1    Yoshimoto, Y.2    Nakano, T.3    Takeshima, T.4    Fukuhara, Y.5    Yasui, K.6    Araga, S.7    Yanagawa, T.8    Ishii, T.9    Nakashima, K.10
  • 173
    • 77949324195 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies
    • Pankiv S., Lamark T., Bruun J. A., vervatn A., Bjrky G., Johansen T., Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies Journal of Biological Chemistry 2010 285 8 5941 5953
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.8 , pp. 5941-5953
    • Pankiv, S.1    Lamark, T.2    Bruun, J.A.3    Vervatn, A.4    Bjrky, G.5    Johansen, T.6
  • 174
    • 33749074277 scopus 로고    scopus 로고
    • Neuronal macroautophagy: From development to degeneration
    • DOI 10.1016/j.mam.2006.08.009, PII S0098299706000240
    • Boland B., Nixon R. A., Neuronal macroautophagy: from development to degeneration Molecular Aspects of Medicine 2006 27 5-6 503 519 (Pubitemid 44466657)
    • (2006) Molecular Aspects of Medicine , vol.27 , Issue.5-6 , pp. 503-519
    • Boland, B.1    Nixon, R.A.2
  • 175
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., Duden R., Rubinsztein D. C., Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy Human Molecular Genetics 2002 11 9 1107 1117 (Pubitemid 34521091)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 176
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto A., Cremona M. L., Rothman J. E., Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway Journal of Cell Biology 2006 172 5 719 731
    • (2006) Journal of Cell Biology , vol.172 , Issue.5 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 177
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B., Kumar A., Lee S., Platt F. M., Wegiel J., Yu W. H., Nixon R. A., Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease Journal of Neuroscience 2008 28 27 6926 6937
    • (2008) Journal of Neuroscience , vol.28 , Issue.27 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 178
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: Protein disaggregating machines
    • Doyle S. M., Wickner S., Hsp104 and ClpB: protein disaggregating machines Trends in Biochemical Sciences 2009 34 1 40 48
    • (2009) Trends in Biochemical Sciences , vol.34 , Issue.1 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 179
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • Shorter J., The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system Plos ONE 2011 6 10
    • (2011) Plos ONE , vol.6 , Issue.10
    • Shorter, J.1
  • 180
  • 181
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E., Cuervo A. M., Autophagy gone awry in neurodegenerative diseases Nature Neuroscience 2010 13 7 805 811
    • (2010) Nature Neuroscience , vol.13 , Issue.7 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 182
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo A. M., Dice J. F., Age-related decline in chaperone-mediated autophagy Journal of Biological Chemistry 2000 275 40 31505 31513
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.40 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 184
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • Simonsen A., Cumming R. C., Brech A., Isakson P., Schubert D. R., Finley K. D., Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila Autophagy 2008 4 2 176 184 (Pubitemid 351231181)
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 176-184
    • Simonsen, A.1    Cumming, R.C.2    Brech, A.3    Isakson, P.4    Schubert, D.R.5    Finley, K.D.6
  • 186
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E., Salminen A., Alafuzoff I., Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies NeuroReport 2001 12 10 2085 2090 (Pubitemid 32646250)
    • (2001) NeuroReport , vol.12 , Issue.10 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 190
    • 4744349602 scopus 로고    scopus 로고
    • Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions
    • DOI 10.1111/j.1471-4159.2004.02692.x
    • Nagaoka U., Kim K., Nihar R. J., Doi H., Maruyama M., Mitsui K., Oyama F., Nukina N., Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions Journal of Neurochemistry 2004 91 1 57 68 (Pubitemid 39314937)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.1 , pp. 57-68
    • Nagaoka, U.1    Kim, K.2    Nihar, R.J.3    Doi, H.4    Maruyama, M.5    Mitsui, K.6    Oyama, F.7    Nukina, N.8
  • 191
    • 33645243056 scopus 로고    scopus 로고
    • Are the Mallory bodies and intracellular hyaline bodies in neoplastic and non-neoplastic hepatocytes related?
    • Denk H., Stumptner C., Fuchsbichler A., Are the Mallory bodies and intracellular hyaline bodies in neoplastic and non-neoplastic hepatocytes related? The Journal of Pathology 2006 208 5 653 661
    • (2006) The Journal of Pathology , vol.208 , Issue.5 , pp. 653-661
    • Denk, H.1    Stumptner, C.2    Fuchsbichler, A.3
  • 192
    • 77449094358 scopus 로고    scopus 로고
    • Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration
    • Liang C. C., Wang C., Peng X., Gan B., Guan J. L., Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration Journal of Biological Chemistry 2010 285 5 3499 3509
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.5 , pp. 3499-3509
    • Liang, C.C.1    Wang, C.2    Peng, X.3    Gan, B.4    Guan, J.L.5
  • 197
    • 36849021043 scopus 로고    scopus 로고
    • Atg7-dependent autophagy promotes neuronal health, stress tolerance, and longevity but is dispensable for metamorphosis in Drosophila
    • DOI 10.1101/gad.1600707
    • Juhsz G., rdi B., Sass M., Neufeld T. P., Atg7-dependent autophagy promotes neuronal health, stress tolerance, and longevity but is dispensable for metamorphosis in Drosophila Genes and Development 2007 21 23 3061 3066 (Pubitemid 350223523)
    • (2007) Genes and Development , vol.21 , Issue.23 , pp. 3061-3066
    • Juhasz, G.1    Erdi, B.2    Sass, M.3    Neufeld, T.P.4
  • 198
    • 41549151641 scopus 로고    scopus 로고
    • Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
    • DOI 10.1083/jcb.200711108
    • Nezis I. P., Simonsen A., Sagona A. P., Finley K., Gaumer S., Contamine D., Rusten T. E., Stenmark H., Brech A., Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain Journal of Cell Biology 2008 180 6 1065 1071 (Pubitemid 351468465)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , pp. 1065-1071
    • Nezis, I.P.1    Simonsen, A.2    Sagona, A.P.3    Finley, K.4    Gaumer, S.5    Contamine, D.6    Rusten, T.E.7    Stenmark, H.8    Brech, A.9
  • 199
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino C., Nogalska A., Cacciottolo M., King Engel W., Askanas V., Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis Acta Neuropathologica 2011 122 5 627 636
    • (2011) Acta Neuropathologica , vol.122 , Issue.5 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3    King Engel, W.4    Askanas, V.5
  • 200
    • 68349097450 scopus 로고    scopus 로고
    • P62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • Nogalska A., Terracciano C., D'Agostino C., King Engel W., Askanas V., p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis Acta Neuropathologica 2009 118 3 407 413
    • (2009) Acta Neuropathologica , vol.118 , Issue.3 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3    King Engel, W.4    Askanas, V.5
  • 203
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D. F., Youle R. J., Parkin is recruited selectively to impaired mitochondria and promotes their autophagy Journal of Cell Biology 2008 183 5 795 803
    • (2008) Journal of Cell Biology , vol.183 , Issue.5 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 204
    • 0242531029 scopus 로고    scopus 로고
    • Inhibition of Proteasomal Activity Causes Inclusion Formation in Neuronal and Non-Neuronal Cells Overexpressing Parkin
    • DOI 10.1091/mbc.E03-02-0078
    • Ardley H. C., Scott G. B., Rose S. A., Tan N. G. S., Markham A. F., Robinson P. A., Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing parkin Molecular Biology of the Cell 2003 14 11 4541 4556 (Pubitemid 37444654)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.11 , pp. 4541-4556
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.S.4    Markham, A.F.5    Robinson, P.A.6
  • 205
    • 3142540683 scopus 로고    scopus 로고
    • Lewy-body formation is an aggresome-related process: A hypothesis
    • DOI 10.1016/S1474-4422(04)00827-0, PII S1474442204008270
    • Olanow C. W., Perl D. P., DeMartino G. N., McNaught K. S. P., Lewy-body formation is an aggresome-related process: a hypothesis Lancet Neurology 2004 3 8 496 503 (Pubitemid 38903101)
    • (2004) Lancet Neurology , vol.3 , Issue.8 , pp. 496-503
    • Olanow, C.W.1    Perl, D.P.2    DeMartino, G.N.3    McNaught, K.St.P.4
  • 206
  • 207
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo A. M., Stafanis L., Fredenburg R., Lansbury P. T., Sulzer D., Impaired degradation of mutant -synuclein by chaperone-mediated autophagy Science 2004 305 5688 1292 1295 (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 208
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of α-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway
    • DOI 10.1523/JNEUROSCI.3809-03.2004
    • Lee H. J., Khoshaghideh F., Patel S., Lee S. J., Clearance of -synuclein oligomeric intermediates via the lysosomal degradation pathway Journal of Neuroscience 2004 24 8 1888 1896 (Pubitemid 38292800)
    • (2004) Journal of Neuroscience , vol.24 , Issue.8 , pp. 1888-1896
    • Lee, H.-J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.-J.4
  • 213
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in -synuclein models of Parkinson's and Lewy body diseases
    • Spencer B., Potkar R., Trejo M., Rockenstein E., Patrick C., Gindi R., Adame A., Wyss-Coray T., Masliah E., Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in -synuclein models of Parkinson's and Lewy body diseases Journal of Neuroscience 2009 29 43 13578 13588
    • (2009) Journal of Neuroscience , vol.29 , Issue.43 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 221
    • 80053243942 scopus 로고    scopus 로고
    • Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits
    • Majumder S., Richardson A., Strong R., Oddo S., Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits Plos ONE 2011 6 9
    • (2011) Plos ONE , vol.6 , Issue.9
    • Majumder, S.1    Richardson, A.2    Strong, R.3    Oddo, S.4
  • 222
    • 79960951303 scopus 로고    scopus 로고
    • Proteasome inhibition drives HDAC6-dependent recruitment of tau to aggresomes
    • Guthrie C. R., Kraemer B. C., Proteasome inhibition drives HDAC6-dependent recruitment of tau to aggresomes Journal of Molecular Neuroscience 2011 45 1 32 41
    • (2011) Journal of Molecular Neuroscience , vol.45 , Issue.1 , pp. 32-41
    • Guthrie, C.R.1    Kraemer, B.C.2
  • 223
    • 49549083278 scopus 로고    scopus 로고
    • Histone deacetylase 6 interacts with the microtubule-associated protein tau
    • Ding H., Dolan P. J., Johnson G. V. W., Histone deacetylase 6 interacts with the microtubule-associated protein tau Journal of Neurochemistry 2008 106 5 2119 2130
    • (2008) Journal of Neurochemistry , vol.106 , Issue.5 , pp. 2119-2130
    • Ding, H.1    Dolan, P.J.2    Johnson, G.V.W.3
  • 224
    • 82055164435 scopus 로고    scopus 로고
    • Accumulation of histone deacetylase 6, an aggresome-related protein, is specific to Lewy bodies and glial cytoplasmic inclusions
    • Miki Y., Mori F., Tanji K., Kakita A., Takahashi H., Wakabayashi K., Accumulation of histone deacetylase 6, an aggresome-related protein, is specific to Lewy bodies and glial cytoplasmic inclusions Neuropathology 2011 31 6 561 568
    • (2011) Neuropathology , vol.31 , Issue.6 , pp. 561-568
    • Miki, Y.1    Mori, F.2    Tanji, K.3    Kakita, A.4    Takahashi, H.5    Wakabayashi, K.6
  • 230
    • 84455169931 scopus 로고    scopus 로고
    • Regulation of autophagy by neuropathological protein TDP-43
    • Bose J. K., Huang C. C., Shen C. K., Regulation of autophagy by neuropathological protein TDP-43 Journal of Biological Chemistry 2011 286 52 44441 44448
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.52 , pp. 44441-44448
    • Bose, J.K.1    Huang, C.C.2    Shen, C.K.3
  • 236
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant 1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman J. H., Perlmutter D. H., Retention of mutant 1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response American Journal of Physiology 2000 279 5 G961 G974
    • (2000) American Journal of Physiology , vol.279 , Issue.5
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 237
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra D. P., Kane L. A., Hauser D. N., Fearnley I. M., Youle R. J., p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both Autophagy 2010 6 8 1090 1106
    • (2010) Autophagy , vol.6 , Issue.8 , pp. 1090-1106
    • Narendra, D.P.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.