메뉴 건너뛰기




Volumn 127, Issue , 2014, Pages 155-182

Mitochondrial acetylation and genetic models of parkinson's disease

Author keywords

Alpha Synuclein; Deacylases; Mitochondrial lysine acetylation; Mitophagy; PARKIN; Parkinson's disease; PINK1; Respiratory complex V; SIRT3

Indexed keywords

LYSINE; MITOCHONDRIAL PROTEIN; PARKIN; PINK1 PROTEIN; SILENT INFORMATION REGULATOR PROTEIN; SIRTUIN; SIRTUIN 3; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 84906656472     PISSN: 18771173     EISSN: 18780814     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394625-6.00006-4     Document Type: Chapter
Times cited : (20)

References (133)
  • 1
    • 50649101095 scopus 로고    scopus 로고
    • Puzzles, promises and a cure for ageing
    • J. Vijg, and J. Campisi Puzzles, promises and a cure for ageing Nature 454 7208 2008 1065 1071
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1065-1071
    • Vijg, J.1    Campisi, J.2
  • 2
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • DOI 10.1101/gad.13.19.2570
    • M. Kaeberlein, M. McVey, and L. Guarente The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms Genes Dev 13 19 1999 2570 2580 (Pubitemid 29489648)
    • (1999) Genes and Development , vol.13 , Issue.19 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 3
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • DOI 10.1038/35065638
    • H.A. Tissenbaum, and L. Guarente Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans Nature 410 6825 2001 227 230 (Pubitemid 32216597)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 4
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • S. Imai, C.M. Armstrong, M. Kaeberlein, and L. Guarente Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase Nature 403 6771 2000 795 800 (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 7
    • 80053460544 scopus 로고    scopus 로고
    • The evolutionarily conserved longevity determinants HCF-1 and SIR-2.1/SIRT1 collaborate to regulate DAF-16/FOXO
    • G. Rizki, T.N. Iwata, and J. Li et al. The evolutionarily conserved longevity determinants HCF-1 and SIR-2.1/SIRT1 collaborate to regulate DAF-16/FOXO PLoS Genet 7 9 2011 e1002235
    • (2011) PLoS Genet , vol.7 , Issue.9 , pp. 1002235
    • Rizki, G.1    Iwata, T.N.2    Li, J.3
  • 8
    • 84879059766 scopus 로고    scopus 로고
    • SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage
    • A.H. Tseng, S.S. Shieh, and D.L. Wang SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage Free Radic Biol Med 63 2013 222 234
    • (2013) Free Radic Biol Med , vol.63 , pp. 222-234
    • Tseng, A.H.1    Shieh, S.S.2    Wang, D.L.3
  • 9
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via sirt-dependent deacetylation promotes expression of glucogenetic genes
    • DOI 10.1074/jbc.M412357200
    • D. Frescas, L. Valenti, and D. Accili Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes J Biol Chem 280 21 2005 20589 20595 (Pubitemid 40776761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 12
    • 84886476382 scopus 로고    scopus 로고
    • Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide
    • K. Schmeisser, J. Mansfeld, and D. Kuhlow et al. Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide Nat Chem Biol 9 11 2013 693 700
    • (2013) Nat Chem Biol , vol.9 , Issue.11 , pp. 693-700
    • Schmeisser, K.1    Mansfeld, J.2    Kuhlow, D.3
  • 13
    • 82955233648 scopus 로고    scopus 로고
    • Old enzymes, new tricks: Sirtuins are NAD(+)-dependent de-acylases
    • M.D. Hirschey Old enzymes, new tricks: sirtuins are NAD(+)-dependent de-acylases Cell Metab 14 6 2011 718 719
    • (2011) Cell Metab , vol.14 , Issue.6 , pp. 718-719
    • Hirschey, M.D.1
  • 16
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span
    • T.L. Kawahara, E. Michishita, and A.S. Adler et al. SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span Cell 136 1 2009 62 74
    • (2009) Cell , vol.136 , Issue.1 , pp. 62-74
    • Kawahara, T.L.1    Michishita, E.2    Adler, A.S.3
  • 17
    • 84875881601 scopus 로고    scopus 로고
    • SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine
    • H. Jiang, S. Khan, and Y. Wang et al. SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine Nature 496 7443 2013 110 113
    • (2013) Nature , vol.496 , Issue.7443 , pp. 110-113
    • Jiang, H.1    Khan, S.2    Wang, Y.3
  • 18
    • 84863453769 scopus 로고    scopus 로고
    • SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
    • M.F. Barber, E. Michishita-Kioi, and Y. Xi et al. SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation Nature 487 7405 2012 114 118
    • (2012) Nature , vol.487 , Issue.7405 , pp. 114-118
    • Barber, M.F.1    Michishita-Kioi, E.2    Xi, Y.3
  • 19
    • 84896901019 scopus 로고    scopus 로고
    • Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin
    • G. Ramakrishnan, G. Davaakhuu, and L. Kaplun et al. Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin J Biol Chem 289 9 2014 6054 6066
    • (2014) J Biol Chem , vol.289 , Issue.9 , pp. 6054-6066
    • Ramakrishnan, G.1    Davaakhuu, G.2    Kaplun, L.3
  • 20
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • B.J. North, B.L. Marshall, M.T. Borra, J.M. Denu, and E. Verdin The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase Mol Cell 11 2 2003 437 444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 21
    • 80053137033 scopus 로고    scopus 로고
    • The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS
    • M.M. Maxwell, E.M. Tomkinson, and J. Nobles et al. The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS Hum Mol Genet 20 20 2011 3986 3996
    • (2011) Hum Mol Genet , vol.20 , Issue.20 , pp. 3986-3996
    • Maxwell, M.M.1    Tomkinson, E.M.2    Nobles, J.3
  • 22
    • 79958041601 scopus 로고    scopus 로고
    • The SirT3 divining rod points to oxidative stress
    • E.L. Bell, and L. Guarente The SirT3 divining rod points to oxidative stress Mol Cell 42 5 2011 561 568
    • (2011) Mol Cell , vol.42 , Issue.5 , pp. 561-568
    • Bell, E.L.1    Guarente, L.2
  • 24
    • 69249084890 scopus 로고    scopus 로고
    • PGC-1{alpha} and PGC-1{beta} regulate mitochondrial density in neurons
    • P. Wareski, A. Vaarmann, and V. Choubey et al. PGC-1{alpha} and PGC-1{beta} regulate mitochondrial density in neurons J Biol Chem 284 32 2009 21379 21385
    • (2009) J Biol Chem , vol.284 , Issue.32 , pp. 21379-21385
    • Wareski, P.1    Vaarmann, A.2    Choubey, V.3
  • 26
    • 84859339977 scopus 로고    scopus 로고
    • Comprehensive research synopsis and systematic meta-analyses in Parkinson's disease genetics: The PDGene database
    • C.M. Lill, J.T. Roehr, and M.B. McQueen et al. Comprehensive research synopsis and systematic meta-analyses in Parkinson's disease genetics: the PDGene database PLoS Genet 8 3 2012 e1002548
    • (2012) PLoS Genet , vol.8 , Issue.3 , pp. 1002548
    • Lill, C.M.1    Roehr, J.T.2    McQueen, M.B.3
  • 27
    • 84884216544 scopus 로고    scopus 로고
    • Mechanistic insight into the relationship between N-terminal acetylation of alpha-synuclein and fibril formation rates by NMR and fluorescence
    • L. Kang, M.K. Janowska, G.M. Moriarty, and J. Baum Mechanistic insight into the relationship between N-terminal acetylation of alpha-synuclein and fibril formation rates by NMR and fluorescence PLoS One 8 9 2013 e75018
    • (2013) PLoS One , vol.8 , Issue.9 , pp. 75018
    • Kang, L.1    Janowska, M.K.2    Moriarty, G.M.3    Baum, J.4
  • 28
    • 84893667535 scopus 로고    scopus 로고
    • N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound alpha-synuclein and increases its affinity for physiological membranes
    • I. Dikiy, and D. Eliezer N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound alpha-synuclein and increases its affinity for physiological membranes J Biol Chem 289 6 2014 3652 3665
    • (2014) J Biol Chem , vol.289 , Issue.6 , pp. 3652-3665
    • Dikiy, I.1    Eliezer, D.2
  • 29
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • S.W. Min, S.H. Cho, and Y. Zhou et al. Acetylation of tau inhibits its degradation and contributes to tauopathy Neuron 67 6 2010 953 966
    • (2010) Neuron , vol.67 , Issue.6 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3
  • 31
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • J. Du, Y. Zhou, and X. Su et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase Science 334 6057 2011 806 809
    • (2011) Science , vol.334 , Issue.6057 , pp. 806-809
    • Du, J.1    Zhou, Y.2    Su, X.3
  • 32
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: Regulation by sirtuins and implications for metabolic disease
    • J.C. Newman, W. He, and E. Verdin Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease J Biol Chem 287 51 2012 42436 42443
    • (2012) J Biol Chem , vol.287 , Issue.51 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 33
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • DOI 10.1074/jbc.M414670200
    • T. Shi, F. Wang, E. Stieren, and Q. Tong SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes J Biol Chem 280 14 2005 13560 13567 (Pubitemid 40517248)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 34
    • 58149345928 scopus 로고    scopus 로고
    • Endurance exercise as a countermeasure for aging
    • I.R. Lanza, D.K. Short, and K.R. Short et al. Endurance exercise as a countermeasure for aging Diabetes 57 11 2008 2933 2942
    • (2008) Diabetes , vol.57 , Issue.11 , pp. 2933-2942
    • Lanza, I.R.1    Short, D.K.2    Short, K.R.3
  • 35
    • 77952940043 scopus 로고    scopus 로고
    • Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle
    • O.M. Palacios, J.J. Carmona, and S. Michan et al. Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle Aging (Albany NY) 1 9 2009 771 783
    • (2009) Aging (Albany NY) , vol.1 , Issue.9 , pp. 771-783
    • Palacios, O.M.1    Carmona, J.J.2    Michan, S.3
  • 36
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • M.D. Hirschey, T. Shimazu, and E. Goetzman et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation Nature 464 7285 2010 121 125
    • (2010) Nature , vol.464 , Issue.7285 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3
  • 37
    • 80052291180 scopus 로고    scopus 로고
    • Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
    • E. Jing, B. Emanuelli, and M.D. Hirschey et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production Proc Natl Acad Sci U S A 108 35 2011 14608 14613
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.35 , pp. 14608-14613
    • Jing, E.1    Emanuelli, B.2    Hirschey, M.D.3
  • 38
    • 79960241384 scopus 로고    scopus 로고
    • PPARalpha-LXR as a novel metabolostatic signalling axis in skeletal muscle that acts to optimize substrate selection in response to nutrient status
    • P.W. Caton, M.J. Holness, D. Bishop-Bailey, and M.C. Sugden PPARalpha-LXR as a novel metabolostatic signalling axis in skeletal muscle that acts to optimize substrate selection in response to nutrient status Biochem J 437 3 2011 521 530
    • (2011) Biochem J , vol.437 , Issue.3 , pp. 521-530
    • Caton, P.W.1    Holness, M.J.2    Bishop-Bailey, D.3    Sugden, M.C.4
  • 39
    • 82455212901 scopus 로고    scopus 로고
    • SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
    • M.D. Hirschey, T. Shimazu, and E. Jing et al. SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome Mol Cell 44 2 2011 177 190
    • (2011) Mol Cell , vol.44 , Issue.2 , pp. 177-190
    • Hirschey, M.D.1    Shimazu, T.2    Jing, E.3
  • 40
    • 77956173286 scopus 로고    scopus 로고
    • SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
    • J. Bao, I. Scott, and Z. Lu et al. SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity Free Radic Biol Med 49 7 2010 1230 1237
    • (2010) Free Radic Biol Med , vol.49 , Issue.7 , pp. 1230-1237
    • Bao, J.1    Scott, I.2    Lu, Z.3
  • 41
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • X. Kong, R. Wang, and Y. Xue et al. Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis PLoS One 5 7 2010 e11707
    • (2010) PLoS One , vol.5 , Issue.7 , pp. 11707
    • Kong, X.1    Wang, R.2    Xue, Y.3
  • 44
    • 77952288176 scopus 로고    scopus 로고
    • Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice
    • S. Hayashida, A. Arimoto, and Y. Kuramoto et al. Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice Mol Cell Biochem 339 1-2 2010 285 292
    • (2010) Mol Cell Biochem , vol.339 , Issue.12 , pp. 285-292
    • Hayashida, S.1    Arimoto, A.2    Kuramoto, Y.3
  • 46
    • 84884248040 scopus 로고    scopus 로고
    • Circadian clock NAD + cycle drives mitochondrial oxidative metabolism in mice
    • C.B. Peek, A.H. Affinati, and K.M. Ramsey et al. Circadian clock NAD + cycle drives mitochondrial oxidative metabolism in mice Science 342 6158 2013 1243417
    • (2013) Science , vol.342 , Issue.6158 , pp. 1243417
    • Peek, C.B.1    Affinati, A.H.2    Ramsey, K.M.3
  • 47
    • 74149085437 scopus 로고    scopus 로고
    • Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats
    • E. Koltai, Z. Szabo, and M. Atalay et al. Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats Mech Ageing Dev 131 1 2010 21 28
    • (2010) Mech Ageing Dev , vol.131 , Issue.1 , pp. 21-28
    • Koltai, E.1    Szabo, Z.2    Atalay, M.3
  • 49
    • 73949123433 scopus 로고    scopus 로고
    • Calorie restriction alters mitochondrial protein acetylation
    • B. Schwer, M. Eckersdorff, and Y. Li et al. Calorie restriction alters mitochondrial protein acetylation Aging Cell 8 5 2009 604 606
    • (2009) Aging Cell , vol.8 , Issue.5 , pp. 604-606
    • Schwer, B.1    Eckersdorff, M.2    Li, Y.3
  • 50
    • 77957762687 scopus 로고    scopus 로고
    • SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells
    • N. Nasrin, X. Wu, and E. Fortier et al. SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells J Biol Chem 285 42 2010 31995 32002
    • (2010) J Biol Chem , vol.285 , Issue.42 , pp. 31995-32002
    • Nasrin, N.1    Wu, X.2    Fortier, E.3
  • 51
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA Synthetase 2, a Mitochondrial Matrix Enzyme Involved in the Oxidation of Acetate
    • DOI 10.1074/jbc.M008782200
    • T. Fujino, J. Kondo, M. Ishikawa, K. Morikawa, and T.T. Yamamoto Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate J Biol Chem 276 14 2001 11420 11426 (Pubitemid 38089336)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 52
    • 0036079706 scopus 로고    scopus 로고
    • Acetyl-coenzyme A synthetase is a lipogenic enzyme controlled by SREBP-1 and energy status
    • H. Sone, H. Shimano, and Y. Sakakura et al. Acetyl-coenzyme A synthetase is a lipogenic enzyme controlled by SREBP-1 and energy status Am J Physiol Endocrinol Metab 282 1 2002 E222 E230
    • (2002) Am J Physiol Endocrinol Metab , vol.282 , Issue.1
    • Sone, H.1    Shimano, H.2    Sakakura, Y.3
  • 53
    • 79960797509 scopus 로고    scopus 로고
    • Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation
    • B.T. Weinert, S.A. Wagner, and H. Horn et al. Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation Sci Signal 4 183 2011 ra48
    • (2011) Sci Signal , vol.4 , Issue.183 , pp. 48
    • Weinert, B.T.1    Wagner, S.A.2    Horn, H.3
  • 54
    • 84860192261 scopus 로고    scopus 로고
    • Identification of a molecular component of the mitochondrial acetyltransferase programme: A novel role for GCN5L1
    • I. Scott, B.R. Webster, J.H. Li, and M.N. Sack Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1 Biochem J 443 3 2012 655 661
    • (2012) Biochem J , vol.443 , Issue.3 , pp. 655-661
    • Scott, I.1    Webster, B.R.2    Li, J.H.3    Sack, M.N.4
  • 55
    • 34547879583 scopus 로고    scopus 로고
    • The SAGA continues: Expanding the cellular role of a transcriptional co-activator complex
    • DOI 10.1038/sj.onc.1210603, PII 1210603
    • S.P. Baker, and P.A. Grant The SAGA continues: expanding the cellular role of a transcriptional co-activator complex Oncogene 26 37 2007 5329 5340 (Pubitemid 47255919)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5329-5340
    • Baker, S.P.1    Grant, P.A.2
  • 56
    • 79959819034 scopus 로고    scopus 로고
    • SirT3 suppresses hypoxia inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS production
    • E.L. Bell, B.M. Emerling, S.J. Ricoult, and L. Guarente SirT3 suppresses hypoxia inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS production Oncogene 30 26 2011 2986 2996
    • (2011) Oncogene , vol.30 , Issue.26 , pp. 2986-2996
    • Bell, E.L.1    Emerling, B.M.2    Ricoult, S.J.3    Guarente, L.4
  • 57
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • X. Qiu, K. Brown, M.D. Hirschey, E. Verdin, and D. Chen Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation Cell Metab 12 6 2010 662 667
    • (2010) Cell Metab , vol.12 , Issue.6 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 58
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress
    • R. Tao, M.C. Coleman, and J.D. Pennington et al. Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress Mol Cell 40 6 2010 893 904
    • (2010) Mol Cell , vol.40 , Issue.6 , pp. 893-904
    • Tao, R.1    Coleman, M.C.2    Pennington, J.D.3
  • 59
    • 74049094817 scopus 로고    scopus 로고
    • SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress
    • H.S. Kim, K. Patel, and K. Muldoon-Jacobs et al. SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress Cancer Cell 17 1 2010 41 52
    • (2010) Cancer Cell , vol.17 , Issue.1 , pp. 41-52
    • Kim, H.S.1    Patel, K.2    Muldoon-Jacobs, K.3
  • 60
    • 79952501323 scopus 로고    scopus 로고
    • SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization
    • L.W. Finley, A. Carracedo, and J. Lee et al. SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization Cancer Cell 19 3 2011 416 428
    • (2011) Cancer Cell , vol.19 , Issue.3 , pp. 416-428
    • Finley, L.W.1    Carracedo, A.2    Lee, J.3
  • 61
    • 84897108383 scopus 로고    scopus 로고
    • SIRT3 expression as a biomarker for better prognosis in gastric cancer
    • K.H. Huang, C.C. Hsu, and W.L. Fang et al. SIRT3 expression as a biomarker for better prognosis in gastric cancer World J Surg 2013
    • (2013) World J Surg
    • Huang, K.H.1    Hsu, C.C.2    Fang, W.L.3
  • 62
    • 84890858374 scopus 로고    scopus 로고
    • Aberrant expression of SIRT3 is conversely correlated with the progression and prognosis of human gastric cancer
    • B. Yang, X. Fu, L. Shao, Y. Ding, and D. Zeng Aberrant expression of SIRT3 is conversely correlated with the progression and prognosis of human gastric cancer Biochem Biophys Res Commun 443 1 2014 156 160
    • (2014) Biochem Biophys Res Commun , vol.443 , Issue.1 , pp. 156-160
    • Yang, B.1    Fu, X.2    Shao, L.3    Ding, Y.4    Zeng, D.5
  • 63
    • 84885069988 scopus 로고    scopus 로고
    • SIRT3 regulates cell proliferation and apoptosis related to energy metabolism in non-small cell lung cancer cells through deacetylation of NMNAT2
    • H. Li, Z. Feng, W. Wu, J. Li, J. Zhang, and T. Xia SIRT3 regulates cell proliferation and apoptosis related to energy metabolism in non-small cell lung cancer cells through deacetylation of NMNAT2 Int J Oncol 43 5 2013 1420 1430
    • (2013) Int J Oncol , vol.43 , Issue.5 , pp. 1420-1430
    • Li, H.1    Feng, Z.2    Wu, W.3    Li, J.4    Zhang, J.5    Xia, T.6
  • 64
    • 84880592756 scopus 로고    scopus 로고
    • Sirt3 is a tumor suppressor in lung adenocarcinoma cells
    • K. Xiao, J. Jiang, and W. Wang et al. Sirt3 is a tumor suppressor in lung adenocarcinoma cells Oncol Rep 30 3 2013 1323 1328
    • (2013) Oncol Rep , vol.30 , Issue.3 , pp. 1323-1328
    • Xiao, K.1    Jiang, J.2    Wang, W.3
  • 65
    • 84879205714 scopus 로고    scopus 로고
    • SIRT3 expression in hepatocellular carcinoma and its impact on proliferation and invasion of hepatoma cells
    • B. Zhang, L. Qin, C.J. Zhou, Y.L. Liu, H.X. Qian, and S.B. He SIRT3 expression in hepatocellular carcinoma and its impact on proliferation and invasion of hepatoma cells Asian Pac J Trop Med 6 8 2013 649 652
    • (2013) Asian Pac J Trop Med , vol.6 , Issue.8 , pp. 649-652
    • Zhang, B.1    Qin, L.2    Zhou, C.J.3    Liu, Y.L.4    Qian, H.X.5    He, S.B.6
  • 66
    • 84871271176 scopus 로고    scopus 로고
    • Low SIRT3 expression correlates with poor differentiation and unfavorable prognosis in primary hepatocellular carcinoma
    • C.Z. Zhang, L. Liu, and M. Cai et al. Low SIRT3 expression correlates with poor differentiation and unfavorable prognosis in primary hepatocellular carcinoma PLoS One 7 12 2012 e51703
    • (2012) PLoS One , vol.7 , Issue.12 , pp. 51703
    • Zhang, C.Z.1    Liu, L.2    Cai, M.3
  • 67
    • 84878721346 scopus 로고    scopus 로고
    • Altered expression of SIRT gene family in head and neck squamous cell carcinoma
    • C.C. Lai, P.M. Lin, and S.F. Lin et al. Altered expression of SIRT gene family in head and neck squamous cell carcinoma Tumour Biol 34 3 2013 1847 1854
    • (2013) Tumour Biol , vol.34 , Issue.3 , pp. 1847-1854
    • Lai, C.C.1    Lin, P.M.2    Lin, S.F.3
  • 68
    • 84883293249 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase and SIRT3 expression are increased in well-differentiated thyroid carcinomas
    • R. Shackelford, S. Hirsh, K. Henry, A. Abdel-Mageed, E. Kandil, and D. Coppola Nicotinamide phosphoribosyltransferase and SIRT3 expression are increased in well-differentiated thyroid carcinomas Anticancer Res 33 8 2013 3047 3052
    • (2013) Anticancer Res , vol.33 , Issue.8 , pp. 3047-3052
    • Shackelford, R.1    Hirsh, S.2    Henry, K.3    Abdel-Mageed, A.4    Kandil, E.5    Coppola, D.6
  • 71
    • 84887597972 scopus 로고    scopus 로고
    • Restricted mitochondrial protein acetylation initiates mitochondrial autophagy
    • B.R. Webster, I. Scott, and K. Han et al. Restricted mitochondrial protein acetylation initiates mitochondrial autophagy J Cell Sci 126 Pt 21 2013 4843 4849
    • (2013) J Cell Sci , vol.126 , Issue.PART 21 , pp. 4843-4849
    • Webster, B.R.1    Scott, I.2    Han, K.3
  • 72
    • 84893500088 scopus 로고    scopus 로고
    • GCN5-like protein 1 (GCN5L1) controls mitochondrial content through coordinated regulation of mitochondrial biogenesis and mitophagy
    • I. Scott, B.R. Webster, C.K. Chan, J.U. Okonkwo, K. Han, and M.N. Sack GCN5-like protein 1 (GCN5L1) controls mitochondrial content through coordinated regulation of mitochondrial biogenesis and mitophagy J Biol Chem 289 5 2014 2864 2872
    • (2014) J Biol Chem , vol.289 , Issue.5 , pp. 2864-2872
    • Scott, I.1    Webster, B.R.2    Chan, C.K.3    Okonkwo, J.U.4    Han, K.5    Sack, M.N.6
  • 73
    • 84877903301 scopus 로고    scopus 로고
    • Lysine deacetylases and mitochondrial dynamics in neurodegeneration
    • P. Guedes-Dias, and J.M. Oliveira Lysine deacetylases and mitochondrial dynamics in neurodegeneration Biochim Biophys Acta 1832 8 2013 1345 1359
    • (2013) Biochim Biophys Acta , vol.1832 , Issue.8 , pp. 1345-1359
    • Guedes-Dias, P.1    Oliveira, J.M.2
  • 74
    • 79952693640 scopus 로고    scopus 로고
    • Mitophagy and Parkinson's disease: The PINK1-Parkin link
    • E. Deas, N.W. Wood, and H. Plun-Favreau Mitophagy and Parkinson's disease: the PINK1-Parkin link Biochim Biophys Acta 1813 4 2011 623 633
    • (2011) Biochim Biophys Acta , vol.1813 , Issue.4 , pp. 623-633
    • Deas, E.1    Wood, N.W.2    Plun-Favreau, H.3
  • 75
    • 84867773087 scopus 로고    scopus 로고
    • Mitophagy: Mechanisms, pathophysiological roles, and analysis
    • W.X. Ding, and X.M. Yin Mitophagy: mechanisms, pathophysiological roles, and analysis Biol Chem 393 7 2012 547 564
    • (2012) Biol Chem , vol.393 , Issue.7 , pp. 547-564
    • Ding, W.X.1    Yin, X.M.2
  • 76
    • 76949092128 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway: A mitochondrial quality control system?
    • A.J. Whitworth, and L.J. Pallanck The PINK1/Parkin pathway: a mitochondrial quality control system? J Bioenerg Biomembr 41 6 2009 499 503
    • (2009) J Bioenerg Biomembr , vol.41 , Issue.6 , pp. 499-503
    • Whitworth, A.J.1    Pallanck, L.J.2
  • 77
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • J.M. Tan, E.S. Wong, and D.S. Kirkpatrick et al. Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases Hum Mol Genet 17 3 2008 431 439
    • (2008) Hum Mol Genet , vol.17 , Issue.3 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3
  • 78
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • S. Geisler, K.M. Holmstrom, and D. Skujat et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1 Nat Cell Biol 12 2 2010 119 131
    • (2010) Nat Cell Biol , vol.12 , Issue.2 , pp. 119-131
    • Geisler, S.1    Holmstrom, K.M.2    Skujat, D.3
  • 79
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • S.A. Sarraf, M. Raman, and V. Guarani-Pereira et al. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization Nature 496 7445 2013 372 376
    • (2013) Nature , vol.496 , Issue.7445 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3
  • 80
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy
    • J.Y. Lee, H. Koga, and Y. Kawaguchi et al. HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy EMBO J 29 5 2010 969 980
    • (2010) EMBO J , vol.29 , Issue.5 , pp. 969-980
    • Lee, J.Y.1    Koga, H.2    Kawaguchi, Y.3
  • 81
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • J.Y. Lee, Y. Nagano, J.P. Taylor, K.L. Lim, and T.P. Yao Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy J Cell Biol 189 4 2010 671 679
    • (2010) J Cell Biol , vol.189 , Issue.4 , pp. 671-679
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 82
    • 84875621300 scopus 로고    scopus 로고
    • Mitophagy and Parkinson's disease: Be eaten to stay healthy
    • R.L. de Vries, and S. Przedborski Mitophagy and Parkinson's disease: be eaten to stay healthy Mol Cell Neurosci 55 2013 37 43
    • (2013) Mol Cell Neurosci , vol.55 , pp. 37-43
    • De Vries, R.L.1    Przedborski, S.2
  • 83
    • 79952324644 scopus 로고    scopus 로고
    • Regulation of PINK1-Parkin-mediated mitophagy
    • W. Springer, and P.J. Kahle Regulation of PINK1-Parkin-mediated mitophagy Autophagy 7 3 2011 266 278
    • (2011) Autophagy , vol.7 , Issue.3 , pp. 266-278
    • Springer, W.1    Kahle, P.J.2
  • 84
    • 84866610524 scopus 로고    scopus 로고
    • Lysosome-dependent pathways as a unifying theme in Parkinson's disease
    • G.K. Tofaris Lysosome-dependent pathways as a unifying theme in Parkinson's disease Mov Disord 27 11 2012 1364 1369
    • (2012) Mov Disord , vol.27 , Issue.11 , pp. 1364-1369
    • Tofaris, G.K.1
  • 85
    • 78650738739 scopus 로고    scopus 로고
    • Culling sick mitochondria from the herd
    • L.J. Pallanck Culling sick mitochondria from the herd J Cell Biol 191 7 2010 1225 1227
    • (2010) J Cell Biol , vol.191 , Issue.7 , pp. 1225-1227
    • Pallanck, L.J.1
  • 87
    • 77951199668 scopus 로고    scopus 로고
    • Decreased expression of Drp1 and Fis1 mediates mitochondrial elongation in senescent cells and enhances resistance to oxidative stress through PINK1
    • S. Mai, M. Klinkenberg, G. Auburger, J. Bereiter-Hahn, and M. Jendrach Decreased expression of Drp1 and Fis1 mediates mitochondrial elongation in senescent cells and enhances resistance to oxidative stress through PINK1 J Cell Sci 123 Pt 6 2010 917 926
    • (2010) J Cell Sci , vol.123 , Issue.PART 6 , pp. 917-926
    • Mai, S.1    Klinkenberg, M.2    Auburger, G.3    Bereiter-Hahn, J.4    Jendrach, M.5
  • 90
    • 84863308390 scopus 로고    scopus 로고
    • Pink1 kinase and its membrane potential (Deltapsi)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode
    • D. Becker, J. Richter, M.A. Tocilescu, S. Przedborski, and W. Voos Pink1 kinase and its membrane potential (Deltapsi)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode J Biol Chem 287 27 2012 22969 22987
    • (2012) J Biol Chem , vol.287 , Issue.27 , pp. 22969-22987
    • Becker, D.1    Richter, J.2    Tocilescu, M.A.3    Przedborski, S.4    Voos, W.5
  • 92
    • 80054787664 scopus 로고    scopus 로고
    • What genetics tells us about the causes and mechanisms of Parkinson's disease
    • O. Corti, S. Lesage, and A. Brice What genetics tells us about the causes and mechanisms of Parkinson's disease Physiol Rev 91 4 2011 1161 1218
    • (2011) Physiol Rev , vol.91 , Issue.4 , pp. 1161-1218
    • Corti, O.1    Lesage, S.2    Brice, A.3
  • 95
    • 68549136513 scopus 로고    scopus 로고
    • Differential effects of PINK1 nonsense and missense mutations on mitochondrial function and morphology
    • A. Grunewald, M.E. Gegg, and J.W. Taanman et al. Differential effects of PINK1 nonsense and missense mutations on mitochondrial function and morphology Exp Neurol 219 1 2009 266 273
    • (2009) Exp Neurol , vol.219 , Issue.1 , pp. 266-273
    • Grunewald, A.1    Gegg, M.E.2    Taanman, J.W.3
  • 98
    • 77951925834 scopus 로고    scopus 로고
    • Enhanced vulnerability of PARK6 patient skin fibroblasts to apoptosis induced by proteasomal stress
    • M. Klinkenberg, N. Thurow, and S. Gispert et al. Enhanced vulnerability of PARK6 patient skin fibroblasts to apoptosis induced by proteasomal stress Neuroscience 166 2 2010 422 434
    • (2010) Neuroscience , vol.166 , Issue.2 , pp. 422-434
    • Klinkenberg, M.1    Thurow, N.2    Gispert, S.3
  • 99
    • 84872860661 scopus 로고    scopus 로고
    • Mitochondrial quality control turns out to be the principal suspect in Parkin and PINK1-related autosomal recessive Parkinson's disease
    • O. Corti, and A. Brice Mitochondrial quality control turns out to be the principal suspect in Parkin and PINK1-related autosomal recessive Parkinson's disease Curr Opin Neurobiol 23 1 2013 100 108
    • (2013) Curr Opin Neurobiol , vol.23 , Issue.1 , pp. 100-108
    • Corti, O.1    Brice, A.2
  • 100
    • 79952369437 scopus 로고    scopus 로고
    • Mutations in PINK1 and Parkin impair ubiquitination of mitofusins in human fibroblasts
    • A. Rakovic, A. Grunewald, and J. Kottwitz et al. Mutations in PINK1 and Parkin impair ubiquitination of mitofusins in human fibroblasts PLoS One 6 3 2011 e16746
    • (2011) PLoS One , vol.6 , Issue.3 , pp. 16746
    • Rakovic, A.1    Grunewald, A.2    Kottwitz, J.3
  • 101
    • 77955029885 scopus 로고    scopus 로고
    • Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients
    • A. Rakovic, A. Grunewald, and P. Seibler et al. Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients Hum Mol Genet 19 16 2010 3124 3137
    • (2010) Hum Mol Genet , vol.19 , Issue.16 , pp. 3124-3137
    • Rakovic, A.1    Grunewald, A.2    Seibler, P.3
  • 102
    • 79955786943 scopus 로고    scopus 로고
    • Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells
    • P. Seibler, J. Graziotto, H. Jeong, F. Simunovic, C. Klein, and D. Krainc Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells J Neurosci 31 16 2011 5970 5976
    • (2011) J Neurosci , vol.31 , Issue.16 , pp. 5970-5976
    • Seibler, P.1    Graziotto, J.2    Jeong, H.3    Simunovic, F.4    Klein, C.5    Krainc, D.6
  • 103
    • 84873843566 scopus 로고    scopus 로고
    • Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: Study in human primary fibroblasts and induced pluripotent stem cell-derived neurons
    • A. Rakovic, K. Shurkewitsch, and P. Seibler et al. Phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem cell-derived neurons J Biol Chem 288 4 2013 2223 2237
    • (2013) J Biol Chem , vol.288 , Issue.4 , pp. 2223-2237
    • Rakovic, A.1    Shurkewitsch, K.2    Seibler, P.3
  • 105
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • DOI 10.1038/nature04779, PII N04779
    • I.E. Clark, M.W. Dodson, and C. Jiang et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with Parkin Nature 441 7097 2006 1162 1166 (Pubitemid 43990738)
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 112
    • 84861476741 scopus 로고    scopus 로고
    • Dopamine induced neurodegeneration in a PINK1 model of Parkinson's disease
    • S. Gandhi, A. Vaarmann, Z. Yao, M.R. Duchen, N.W. Wood, and A.Y. Abramov Dopamine induced neurodegeneration in a PINK1 model of Parkinson's disease PLoS One 7 5 2012 e37564
    • (2012) PLoS One , vol.7 , Issue.5 , pp. 37564
    • Gandhi, S.1    Vaarmann, A.2    Yao, Z.3    Duchen, M.R.4    Wood, N.W.5    Abramov, A.Y.6
  • 113
    • 66749163493 scopus 로고    scopus 로고
    • Parkinson phenotype in aged PINK1-deficient mice is accompanied by progressive mitochondrial dysfunction in absence of neurodegeneration
    • S. Gispert, F. Ricciardi, and A. Kurz et al. Parkinson phenotype in aged PINK1-deficient mice is accompanied by progressive mitochondrial dysfunction in absence of neurodegeneration PLoS One 4 6 2009 e5777
    • (2009) PLoS One , vol.4 , Issue.6 , pp. 5777
    • Gispert, S.1    Ricciardi, F.2    Kurz, A.3
  • 114
    • 84870975698 scopus 로고    scopus 로고
    • Subthalamic lesion or levodopa treatment rescues giant GABAergic currents of PINK1-deficient striatum
    • N. Dehorter, N. Lozovaya, and B.J. Mdzomba et al. Subthalamic lesion or levodopa treatment rescues giant GABAergic currents of PINK1-deficient striatum J Neurosci 32 50 2012 18047 18053
    • (2012) J Neurosci , vol.32 , Issue.50 , pp. 18047-18053
    • Dehorter, N.1    Lozovaya, N.2    Mdzomba, B.J.3
  • 116
    • 34249946941 scopus 로고    scopus 로고
    • Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage
    • DOI 10.1093/hmg/ddm083
    • C.C. Stichel, X.R. Zhu, V. Bader, B. Linnartz, S. Schmidt, and H. Lubbert Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage Hum Mol Genet 16 20 2007 2377 2393 (Pubitemid 47514484)
    • (2007) Human Molecular Genetics , vol.16 , Issue.20 , pp. 2377-2393
    • Stichel, C.C.1    Zhu, X.-R.2    Bader, V.3    Linnartz, B.4    Schmidt, S.5    Lubbert, H.6
  • 117
    • 79952020818 scopus 로고    scopus 로고
    • Genetic mouse models for Parkinson's disease display severe pathology in glial cell mitochondria
    • S. Schmidt, B. Linnartz, and S. Mendritzki et al. Genetic mouse models for Parkinson's disease display severe pathology in glial cell mitochondria Hum Mol Genet 20 6 2011 1197 1211
    • (2011) Hum Mol Genet , vol.20 , Issue.6 , pp. 1197-1211
    • Schmidt, S.1    Linnartz, B.2    Mendritzki, S.3
  • 120
    • 77958450202 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fusion by alpha-synuclein is rescued by PINK1, Parkin and DJ-1
    • F. Kamp, N. Exner, and A.K. Lutz et al. Inhibition of mitochondrial fusion by alpha-synuclein is rescued by PINK1, Parkin and DJ-1 EMBO J 29 20 2010 3571 3589
    • (2010) EMBO J , vol.29 , Issue.20 , pp. 3571-3589
    • Kamp, F.1    Exner, N.2    Lutz, A.K.3
  • 121
    • 84930486348 scopus 로고    scopus 로고
    • Expression of Pink1 with alpha-synuclein in the dopaminergic neurons of Drosophila leads to increases in both lifespan and healthspan
    • A.M. Todd, and B.E. Staveley Expression of Pink1 with alpha-synuclein in the dopaminergic neurons of Drosophila leads to increases in both lifespan and healthspan Genet Mol Res 11 2 2012 1497 1502
    • (2012) Genet Mol Res , vol.11 , Issue.2 , pp. 1497-1502
    • Todd, A.M.1    Staveley, B.E.2
  • 122
    • 47349127878 scopus 로고    scopus 로고
    • Parkinson patient fibroblasts show increased alpha-synuclein expression
    • H.H. Hoepken, S. Gispert, and M. Azizov et al. Parkinson patient fibroblasts show increased alpha-synuclein expression Exp Neurol 212 2 2008 307 313
    • (2008) Exp Neurol , vol.212 , Issue.2 , pp. 307-313
    • Hoepken, H.H.1    Gispert, S.2    Azizov, M.3
  • 123
    • 77950855127 scopus 로고    scopus 로고
    • PINK1-linked Parkinsonism is associated with Lewy body pathology
    • L. Samaranch, O. Lorenzo-Betancor, and J.M. Arbelo et al. PINK1-linked Parkinsonism is associated with Lewy body pathology Brain 133 Pt 4 2010 1128 1142
    • (2010) Brain , vol.133 , Issue.PART 4 , pp. 1128-1142
    • Samaranch, L.1    Lorenzo-Betancor, O.2    Arbelo, J.M.3
  • 124
    • 84864278260 scopus 로고    scopus 로고
    • PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease
    • W. Liu, C. Vives-Bauza, and R. Acin-Perez et al. PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease PLoS One 4 2 2009 e4597
    • (2009) PLoS One , vol.4 , Issue.2 , pp. 4597
    • Liu, W.1    Vives-Bauza, C.2    Acin-Perez, R.3
  • 125
    • 77957347060 scopus 로고    scopus 로고
    • Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro
    • J. Burre, M. Sharma, T. Tsetsenis, V. Buchman, M.R. Etherton, and T.C. Sudhof Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro Science 329 5999 2010 1663 1667
    • (2010) Science , vol.329 , Issue.5999 , pp. 1663-1667
    • Burre, J.1    Sharma, M.2    Tsetsenis, T.3    Buchman, V.4    Etherton, M.R.5    Sudhof, T.C.6
  • 127
    • 77955347330 scopus 로고    scopus 로고
    • A53T-alpha-synuclein overexpression impairs dopamine signaling and striatal synaptic plasticity in old mice
    • A. Kurz, K.L. Double, and I. Lastres-Becker et al. A53T-alpha-synuclein overexpression impairs dopamine signaling and striatal synaptic plasticity in old mice PLoS One 5 7 2010 e11464
    • (2010) PLoS One , vol.5 , Issue.7 , pp. 11464
    • Kurz, A.1    Double, K.L.2    Lastres-Becker, I.3
  • 128
    • 84861898518 scopus 로고    scopus 로고
    • Mechanisms underlying altered striatal synaptic plasticity in old A53T-alpha synuclein overexpressing mice
    • A. Tozzi, C. Costa, and S. Siliquini et al. Mechanisms underlying altered striatal synaptic plasticity in old A53T-alpha synuclein overexpressing mice Neurobiol Aging 33 8 2012 1792 1799
    • (2012) Neurobiol Aging , vol.33 , Issue.8 , pp. 1792-1799
    • Tozzi, A.1    Costa, C.2    Siliquini, S.3
  • 129
    • 84857637973 scopus 로고    scopus 로고
    • A53T-alpha-synuclein-overexpression in the mouse nigrostriatal pathway leads to early increase of 14-3-3 epsilon and late increase of GFAP
    • A. Kurz, C. May, and O. Schmidt et al. A53T-alpha-synuclein- overexpression in the mouse nigrostriatal pathway leads to early increase of 14-3-3 epsilon and late increase of GFAP J Neural Transm 119 3 2012 297 312
    • (2012) J Neural Transm , vol.119 , Issue.3 , pp. 297-312
    • Kurz, A.1    May, C.2    Schmidt, O.3
  • 130
    • 84860538863 scopus 로고    scopus 로고
    • Striatal dopamine transmission is subtly modified in human A53Talpha-synuclein overexpressing mice
    • N.J. Platt, S. Gispert, G. Auburger, and S.J. Cragg Striatal dopamine transmission is subtly modified in human A53Talpha-synuclein overexpressing mice PLoS One 7 5 2012 e36397
    • (2012) PLoS One , vol.7 , Issue.5 , pp. 36397
    • Platt, N.J.1    Gispert, S.2    Auburger, G.3    Cragg, S.J.4
  • 131
    • 84873415220 scopus 로고    scopus 로고
    • Biomarkers for trials of neuroprotection in Parkinson's disease
    • P.A. Agarwal, and A.J. Stoessl Biomarkers for trials of neuroprotection in Parkinson's disease Mov Disord 28 1 2013 71 85
    • (2013) Mov Disord , vol.28 , Issue.1 , pp. 71-85
    • Agarwal, P.A.1    Stoessl, A.J.2
  • 132
    • 84874948898 scopus 로고    scopus 로고
    • Cerebrospinal fluid biomarkers in Parkinson disease
    • L. Parnetti, A. Castrioto, and D. Chiasserini et al. Cerebrospinal fluid biomarkers in Parkinson disease Nat Rev Neurol 9 3 2013 131 140
    • (2013) Nat Rev Neurol , vol.9 , Issue.3 , pp. 131-140
    • Parnetti, L.1    Castrioto, A.2    Chiasserini, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.