메뉴 건너뛰기




Volumn 91, Issue 6, 2013, Pages 665-671

Insights into mitochondrial quality control pathways and Parkinson's disease

Author keywords

Mitochondria; Mitochondrial quality control; Neurodegeneration; Protein aggregation

Indexed keywords

DJ 1 PROTEIN; MITOCHONDRIAL DNA; PARKIN; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE OMI;

EID: 84878593326     PISSN: 09462716     EISSN: 14321440     Source Type: Journal    
DOI: 10.1007/s00109-013-1044-y     Document Type: Review
Times cited : (13)

References (50)
  • 1
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • 10.1038/sj.emboj.7601972 18216873 10.1038/sj.emboj.7601972 1:CAS:528:DC%2BD1cXhtVKktLk%3D
    • Tatsuta T, Langer T (2008) Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J 27:306-314. doi: 10.1038/sj.emboj.7601972
    • (2008) EMBO J , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 2
    • 77955498525 scopus 로고    scopus 로고
    • Mitochondrial quality control and neurological disease: An emerging connection
    • 10.1017/S1462399410001456 20398440 10.1017/S1462399410001456
    • de Castro IP, Martins LM, Tufi R (2010) Mitochondrial quality control and neurological disease: an emerging connection. Expert Rev Mol Med 12:e12. doi: 10.1017/S1462399410001456
    • (2010) Expert Rev Mol Med , vol.12 , pp. 12
    • De Castro, I.P.1    Martins, L.M.2    Tufi, R.3
  • 3
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • 10.1038/nrm2952 20683470 10.1038/nrm2952 1:CAS:528:DC%2BC3cXps1egt7w%3D
    • Tait SW, Green DR (2010) Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 11:621-632. doi: 10.1038/nrm2952
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 4
    • 67349249403 scopus 로고    scopus 로고
    • The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1
    • 10.1038/ncb1881 19448625 10.1038/ncb1881 1:CAS:528:DC%2BD1MXms1als74%3D
    • Herrero-Mendez A, Almeida A, Fernandez E, Maestre C, Moncada S, Bolanos JP (2009) The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1. Nat cell biol 11:747-752. doi: 10.1038/ncb1881
    • (2009) Nat Cell Biol , vol.11 , pp. 747-752
    • Herrero-Mendez, A.1    Almeida, A.2    Fernandez, E.3    Maestre, C.4    Moncada, S.5    Bolanos, J.P.6
  • 5
    • 77950583501 scopus 로고    scopus 로고
    • The pentose-phosphate pathway in neuronal survival against nitrosative stress
    • 10.1002/iub.280 19937972 1:CAS:528:DC%2BC3cXktlemsw%3D%3D
    • Bolanos JP, Almeida A (2010) The pentose-phosphate pathway in neuronal survival against nitrosative stress. IUBMB Life 62:14-18. doi: 10.1002/iub.280
    • (2010) IUBMB Life , vol.62 , pp. 14-18
    • Bolanos, J.P.1    Almeida, A.2
  • 6
    • 0029803242 scopus 로고    scopus 로고
    • In situ localization of mitochondrial DNA replication in intact mammalian cells
    • 8922374 10.1083/jcb.135.4.883 1:CAS:528:DyaK28XntVaks70%3D
    • Davis AF, Clayton DA (1996) In situ localization of mitochondrial DNA replication in intact mammalian cells. J cell biol 135:883-893
    • (1996) J Cell Biol , vol.135 , pp. 883-893
    • Davis, A.F.1    Clayton, D.A.2
  • 7
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • 10.1016/j.cub.2012.02.005 22342752 10.1016/j.cub.2012.02.005 1:CAS:528:DC%2BC38XisFKhtL0%3D
    • Cai Q, Zakaria HM, Simone A, Sheng ZH (2012) Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Current biology: CB 22:545-552. doi: 10.1016/j.cub.2012.02.005
    • (2012) Current Biology: CB , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 8
    • 33745921507 scopus 로고    scopus 로고
    • Mitochondria at the synapse
    • 10.1177/1073858406287661 16840705 10.1177/1073858406287661 1:CAS:528:DC%2BD28XotlSms74%3D
    • Ly CV, Verstreken P (2006) Mitochondria at the synapse. Neuroscientist 12:291-299. doi: 10.1177/1073858406287661
    • (2006) Neuroscientist , vol.12 , pp. 291-299
    • Ly, C.V.1    Verstreken, P.2
  • 10
    • 60849097548 scopus 로고    scopus 로고
    • Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
    • 19023330 10.1038/cdd.2008.166 1:CAS:528:DC%2BD1MXit1Wkurw%3D
    • Moisoi N, Klupsch K, Fedele V et al (2009) Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death Differ 16:449-464
    • (2009) Cell Death Differ , vol.16 , pp. 449-464
    • Moisoi, N.1    Klupsch, K.2    Fedele, V.3
  • 11
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans
    • 10.1016/j.devcel.2007.07.016 17925224 10.1016/j.devcel.2007.07.016 1:CAS:528:DC%2BD2sXht1SjsrjM
    • Haynes CM, Petrova K, Benedetti C, Yang Y, Ron D (2007) ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev Cell 13:467-480. doi: 10.1016/j.devcel.2007.07.016
    • (2007) Dev Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 12
    • 33748901113 scopus 로고    scopus 로고
    • Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response
    • 10.1534/genetics.106.061580 16816413 10.1534/genetics.106.061580 1:CAS:528:DC%2BD28XhtFGgsrnE
    • Benedetti C, Haynes CM, Yang Y, Harding HP, Ron D (2006) Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response. Genetics 174:229-239. doi: 10.1534/genetics.106. 061580
    • (2006) Genetics , vol.174 , pp. 229-239
    • Benedetti, C.1    Haynes, C.M.2    Yang, Y.3    Harding, H.P.4    Ron, D.5
  • 13
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans
    • 10.1016/j.molcel.2010.01.015 20188671 10.1016/j.molcel.2010.01.015 1:CAS:528:DC%2BC3cXlt1Kku7o%3D
    • Haynes CM, Yang Y, Blais SP, Neubert TA, Ron D (2010) The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol cell 37:529-540. doi: 10.1016/j.molcel.2010. 01.015
    • (2010) Mol Cell , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 14
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • 10.1126/science.1223560 22700657 10.1126/science.1223560 1:CAS:528:DC%2BC38XhtFWhsbbO
    • Nargund AM, Pellegrino MW, Fiorese CJ, Baker BM, Haynes CM (2012) Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337:587-590. doi: 10.1126/science.1223560
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 15
    • 1542571796 scopus 로고    scopus 로고
    • Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi
    • 10.1074/jbc.M308659200 14512424 10.1074/jbc.M308659200 1:CAS:528:DC%2BD3sXptlGrt74%3D
    • Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC, Downward J (2003) Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi. J Biol Chem 278:49417-49427. doi: 10.1074/jbc.M308659200
    • (2003) J Biol Chem , vol.278 , pp. 49417-49427
    • Martins, L.M.1    Turk, B.E.2    Cowling, V.3    Borg, A.4    Jarrell, E.T.5    Cantley, L.C.6    Downward, J.7
  • 16
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • 17906618 10.1038/ncb1644 1:CAS:528:DC%2BD2sXht1Cgu7fN
    • Plun-Favreau H, Klupsch K, Moisoi N et al (2007) The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol 9:1243-1252
    • (2007) Nat Cell Biol , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3
  • 18
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • 17579517 10.1371/journal.pbio.0050172
    • Pridgeon JW, Olzmann JA, Chin LS, Li L (2007) PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 5:e172
    • (2007) PLoS Biol , vol.5 , pp. 172
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 19
    • 79958731043 scopus 로고    scopus 로고
    • Mitochondrial quality control and Parkinson's disease: A pathway unfolds
    • 10.1007/s12035-010-8150-4 21120708 10.1007/s12035-010-8150-4 1:CAS:528:DC%2BC3MXjs1Cnt7g%3D
    • de Castro IP, Martins LM, Loh SH (2011) Mitochondrial quality control and Parkinson's disease: a pathway unfolds. Mol Neurobiol 43:80-86. doi: 10.1007/s12035-010-8150-4
    • (2011) Mol Neurobiol , vol.43 , pp. 80-86
    • De Castro, I.P.1    Martins, L.M.2    Loh, S.H.3
  • 20
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • 18200046 10.1038/sj.emboj.7601963 1:CAS:528:DC%2BD1cXhtVKkurs%3D
    • Twig G, Elorza A, Molina AJ et al (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 27:433-446
    • (2008) EMBO J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3
  • 21
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • 9230308 10.1016/S0092-8674(00)80319-0 1:CAS:528:DyaK2sXkslSgsro%3D
    • Hales KG, Fuller MT (1997) Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 90:121-129
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 22
    • 0035057837 scopus 로고    scopus 로고
    • Control of mitochondrial morphology by a human mitofusin
    • 11181170 1:CAS:528:DC%2BD3MXit1eitL4%3D
    • Santel A, Fuller MT (2001) Control of mitochondrial morphology by a human mitofusin. J Cell Sci 114:867-874
    • (2001) J Cell Sci , vol.114 , pp. 867-874
    • Santel, A.1    Fuller, M.T.2
  • 23
    • 8644270474 scopus 로고    scopus 로고
    • OPA1 requires mitofusin 1 to promote mitochondrial fusion
    • 10.1073/pnas.0407043101 15509649 10.1073/pnas.0407043101 1:CAS:528:DC%2BD2cXhtVGisrbP
    • Cipolat S, Martins de Brito O, Dal Zilio B, Scorrano L (2004) OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc Natl Acad Sci U S A 101:15927-15932. doi: 10.1073/pnas.0407043101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15927-15932
    • Cipolat, S.1    Martins De Brito, O.2    Dal Zilio, B.3    Scorrano, L.4
  • 24
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • 11514614 1:CAS:528:DC%2BD3MXmtFKgtb8%3D
    • Smirnova E, Griparic L, Shurland DL, van der Bliek AM (2001) Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12:2245-2256
    • (2001) Mol Biol Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 25
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of the mammalian mitochondrial fission machinery
    • 10.1074/jbc.M303758200 12783892 10.1074/jbc.M303758200 1:CAS:528:DC%2BD3sXnt1ejsL8%3D
    • James DI, Parone PA, Mattenberger Y, Martinou JC (2003) hFis1, a novel component of the mammalian mitochondrial fission machinery. J Biol Chem 278:36373-36379. doi: 10.1074/jbc.M303758200
    • (2003) J Biol Chem , vol.278 , pp. 36373-36379
    • James, D.I.1    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 26
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • 10.1038/ncb2012 20098416 10.1038/ncb2012 1:CAS:528:DC%2BC3cXhtlCqtbs%3D
    • Geisler S, Holmstrom KM, Skujat D, Fiesel FC, Rothfuss OC, Kahle PJ, Springer W (2010) PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol 12:119-131. doi: 10.1038/ncb2012
    • (2010) Nat Cell Biol , vol.12 , pp. 119-131
    • Geisler, S.1    Holmstrom, K.M.2    Skujat, D.3    Fiesel, F.C.4    Rothfuss, O.C.5    Kahle, P.J.6    Springer, W.7
  • 27
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • 10.1073/pnas.0913485107 20194754 10.1073/pnas.0913485107 1:CAS:528:DC%2BC3cXjvFGnt7k%3D
    • Ziviani E, Tao RN, Whitworth AJ (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107:5018-5023. doi: 10.1073/pnas.0913485107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 28
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • 10.1016/j.cell.2011.10.018 22078885 10.1016/j.cell.2011.10.018 1:CAS:528:DC%2BC3MXhsVKgsLbP
    • Wang X, Winter D, Ashrafi G, Schlehe J, Wong YL, Selkoe D, Rice S, Steen J, LaVoie MJ, Schwarz TL (2011) PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 147:893-906. doi: 10.1016/j.cell.2011.10.018
    • (2011) Cell , vol.147 , pp. 893-906
    • Wang, X.1    Winter, D.2    Ashrafi, G.3    Schlehe, J.4    Wong, Y.L.5    Selkoe, D.6    Rice, S.7    Steen, J.8    Lavoie, M.J.9    Schwarz, T.L.10
  • 29
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
    • 10.1038/cdd.2009.16 19229244 10.1038/cdd.2009.16 1:CAS:528: DC%2BD1MXnsV2qs7Y%3D
    • Zhang J, Ney PA (2009) Role of BNIP3 and NIX in cell death, autophagy, and mitophagy. Cell Death Differ 16:939-946. doi: 10.1038/cdd.2009.16
    • (2009) Cell Death Differ , vol.16 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 30
    • 84856221632 scopus 로고    scopus 로고
    • A vesicular transport pathway shuttles cargo from mitochondria to lysosomes
    • 10.1016/j.cub.2011.11.057 22226745 10.1016/j.cub.2011.11.057 1:CAS:528:DC%2BC38Xhs1Gitbc%3D
    • Soubannier V, McLelland GL, Zunino R, Braschi E, Rippstein P, Fon EA, McBride HM (2012) A vesicular transport pathway shuttles cargo from mitochondria to lysosomes. Curr Biol 22:135-141. doi: 10.1016/j.cub.2011.11.057
    • (2012) Curr Biol , vol.22 , pp. 135-141
    • Soubannier, V.1    McLelland, G.L.2    Zunino, R.3    Braschi, E.4    Rippstein, P.5    Fon, E.A.6    McBride, H.M.7
  • 31
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • 15087508 10.1126/science.1096284 1:CAS:528:DC%2BD2cXktVyit7k%3D
    • Valente EM, Abou-Sleiman PM, Caputo V et al (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304:1158-1160
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 32
    • 79952303794 scopus 로고    scopus 로고
    • PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson's disease
    • 10.1016/j.cell.2011.02.010 21376232 10.1016/j.cell.2011.02.010 1:CAS:528:DC%2BC3MXjsFeqtrc%3D
    • Shin JH, Ko HS, Kang H, Lee Y, Lee YI, Pletinkova O, Troconso JC, Dawson VL, Dawson TM (2011) PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson's disease. Cell 144:689-702. doi: 10.1016/j.cell.2011.02.010
    • (2011) Cell , vol.144 , pp. 689-702
    • Shin, J.H.1    Ko, H.S.2    Kang, H.3    Lee, Y.4    Lee, Y.I.5    Pletinkova, O.6    Troconso, J.C.7    Dawson, V.L.8    Dawson, T.M.9
  • 33
    • 44849115171 scopus 로고    scopus 로고
    • Genetic variability in the mitochondrial serine protease HTRA2 contributes to risk for Parkinson disease
    • 10.1002/humu.20713 18401856 10.1002/humu.20713 1:CAS:528: DC%2BD1cXnvFegtr4%3D
    • Bogaerts V, Nuytemans K, Reumers J et al (2008) Genetic variability in the mitochondrial serine protease HTRA2 contributes to risk for Parkinson disease. Hum Mutat 29:832-840. doi: 10.1002/humu.20713
    • (2008) Hum Mutat , vol.29 , pp. 832-840
    • Bogaerts, V.1    Nuytemans, K.2    Reumers, J.3
  • 34
    • 25444498785 scopus 로고    scopus 로고
    • Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
    • 15961413 10.1093/hmg/ddi215 1:CAS:528:DC%2BD2MXmt1ersL4%3D
    • Strauss KM, Martins LM, Plun-Favreau H et al (2005) Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum Mol Genet 14:2099-2111
    • (2005) Hum Mol Genet , vol.14 , pp. 2099-2111
    • Strauss, K.M.1    Martins, L.M.2    Plun-Favreau, H.3
  • 35
    • 84862282562 scopus 로고    scopus 로고
    • Mitochondrial stress signalling: HTRA2 and Parkinson's disease
    • doi: 10.1155/2012/607929
    • Desideri E, Martins LM (2012) Mitochondrial stress signalling: HTRA2 and Parkinson's disease. Int J Cell Biol 2012:607929. doi: 10.1155/2012/607929
    • (2012) Int J Cell Biol , vol.2012 , pp. 607929
    • Desideri, E.1    Martins, L.M.2
  • 36
    • 0142246441 scopus 로고    scopus 로고
    • Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
    • 10.1038/nature02052 14534547 10.1038/nature02052 1:CAS:528: DC%2BD3sXotV2hsr8%3D
    • Jones JM, Datta P, Srinivasula SM et al (2003) Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature 425:721-727. doi: 10.1038/nature02052
    • (2003) Nature , vol.425 , pp. 721-727
    • Jones, J.M.1    Datta, P.2    Srinivasula, S.M.3
  • 37
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • 15509788 10.1128/MCB.24.22.9848-9862.2004 1:CAS:528:DC%2BD2cXpslOntbo%3D
    • Martins LM, Morrison A, Klupsch K et al (2004) Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol Cell Biol 24:9848-9862
    • (2004) Mol Cell Biol , vol.24 , pp. 9848-9862
    • Martins, L.M.1    Morrison, A.2    Klupsch, K.3
  • 38
    • 79952900158 scopus 로고    scopus 로고
    • A large-scale genetic association study to evaluate the contribution of Omi/HtrA2 (PARK13) to Parkinson's disease
    • 10.1016/j.neurobiolaging.2009.11.021
    • Kruger R, Sharma M, Riess O et al (2011) A large-scale genetic association study to evaluate the contribution of Omi/HtrA2 (PARK13) to Parkinson's disease. Neurobiol Aging 32(548):e549-518. doi: 10.1016/j. neurobiolaging.2009.11.021
    • (2011) Neurobiol Aging , vol.32 , Issue.548 , pp. 549-518
    • Kruger, R.1    Sharma, M.2    Riess, O.3
  • 39
    • 45749135862 scopus 로고    scopus 로고
    • Sequencing analysis of OMI/HTRA2 shows previously reported pathogenic mutations in neurologically normal controls
    • 10.1093/hmg/ddn096 18364387 10.1093/hmg/ddn096 1:CAS:528: DC%2BD1cXntFOkt7w%3D
    • Simon-Sanchez J, Singleton AB (2008) Sequencing analysis of OMI/HTRA2 shows previously reported pathogenic mutations in neurologically normal controls. Hum Mol Genet 17:1988-1993. doi: 10.1093/hmg/ddn096
    • (2008) Hum Mol Genet , vol.17 , pp. 1988-1993
    • Simon-Sanchez, J.1    Singleton, A.B.2
  • 41
    • 84878533362 scopus 로고    scopus 로고
    • Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease
    • 23328674 10.1038/cddis.2012.205 1:STN:280:DC%2BC3szgsVamsg%3D%3D
    • Costa AC, Lo HS, Martins LM (2013) Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease. Cell Death Dis 4:e467
    • (2013) Cell Death Dis , vol.4 , pp. 467
    • Costa, A.C.1    Lo, H.S.2    Martins, L.M.3
  • 42
    • 84878529485 scopus 로고    scopus 로고
    • TRAP1 rescues PINK1 loss-of-function phenotypes
    • 10.1093/hmg/ddt132
    • Zhang L, Karsten P, Hamm S et al (2013) TRAP1 rescues PINK1 loss-of-function phenotypes. Hum Mol Genet. doi: 10.1093/hmg/ddt132
    • (2013) Hum Mol Genet
    • Zhang, L.1    Karsten, P.2    Hamm, S.3
  • 43
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • 10.1126/science.1077209 12446870 10.1126/science.1077209 1:CAS:528:DC%2BD3sXhs1Gkuw%3D%3D
    • Bonifati V, Rizzu P, van Baren MJ et al (2003) Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299:256-259. doi: 10.1126/science.1077209
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    Van Baren, M.J.3
  • 44
    • 77958479016 scopus 로고    scopus 로고
    • Dissecting the role of the mitochondrial chaperone mortalin in Parkinson's disease: Functional impact of disease-related variants on mitochondrial homeostasis
    • 10.1093/hmg/ddq370 20817635 10.1093/hmg/ddq370 1:CAS:528: DC%2BC3cXhtlaktrvI
    • Burbulla LF, Schelling C, Kato H et al (2010) Dissecting the role of the mitochondrial chaperone mortalin in Parkinson's disease: functional impact of disease-related variants on mitochondrial homeostasis. Hum Mol Genet 19:4437-4452. doi: 10.1093/hmg/ddq370
    • (2010) Hum Mol Genet , vol.19 , pp. 4437-4452
    • Burbulla, L.F.1    Schelling, C.2    Kato, H.3
  • 45
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein
    • 10.1111/j.1471-4159.2012.07809.x 22639965 10.1111/j.1471-4159.2012.07809. x 1:CAS:528:DC%2BC38XhtFeis7fL
    • Niu J, Yu M, Wang C, Xu Z (2012) Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein. J Neurochem 122:650-658. doi: 10.1111/j.1471-4159.2012.07809.x
    • (2012) J Neurochem , vol.122 , pp. 650-658
    • Niu, J.1    Yu, M.2    Wang, C.3    Xu, Z.4
  • 46
    • 84859259002 scopus 로고    scopus 로고
    • LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
    • 10.1093/hmg/dds003 22228096 10.1093/hmg/dds003 1:CAS:528: DC%2BC38XkvVeqsL4%3D
    • Wang X, Yan MH, Fujioka H, Liu J, Wilson-Delfosse A, Chen SG, Perry G, Casadesus G, Zhu X (2012) LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1. Hum Mol Genet 21:1931-1944. doi: 10.1093/hmg/dds003
    • (2012) Hum Mol Genet , vol.21 , pp. 1931-1944
    • Wang, X.1    Yan, M.H.2    Fujioka, H.3    Liu, J.4    Wilson-Delfosse, A.5    Chen, S.G.6    Perry, G.7    Casadesus, G.8    Zhu, X.9
  • 47
    • 84872691988 scopus 로고    scopus 로고
    • Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons
    • 10.1016/j.ajpath.2012.10.027 23231918 10.1016/j.ajpath.2012.10.027 1:CAS:528:DC%2BC3sXhtFGqtLw%3D
    • Cherra SJ 3rd, Steer E, Gusdon AM, Kiselyov K, Chu CT (2013) Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons. Am J Pathol 182:474-484. doi: 10.1016/j.ajpath.2012.10.027
    • (2013) Am J Pathol , vol.182 , pp. 474-484
    • Cherra III, S.J.1    Steer, E.2    Gusdon, A.M.3    Kiselyov, K.4    Chu, C.T.5
  • 48
    • 0027724036 scopus 로고
    • Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes
    • 10.1006/jtbi.1993.1210 8114509 10.1006/jtbi.1993.1210 1:CAS:528:DyaK2cXht1KrtrY%3D
    • Allen JF (1993) Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes. J Theor Biol 165:609-631. doi: 10.1006/jtbi.1993.1210
    • (1993) J Theor Biol , vol.165 , pp. 609-631
    • Allen, J.F.1
  • 49
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • 15068799 10.1016/S1097-2765(04)00179-0 1:CAS:528:DC%2BD2cXjvVaqsbs%3D
    • Butow RA, Avadhani NG (2004) Mitochondrial signaling: the retrograde response. Mol Cell 14:1-15
    • (2004) Mol Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 50
    • 84861983560 scopus 로고    scopus 로고
    • Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency
    • 10.1126/science.1218632 22582012 10.1126/science.1218632 1:CAS:528:DC%2BC38XnvFektr4%3D
    • Vos M, Esposito G, Edirisinghe JN et al (2012) Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency. Science 336:1306-1310. doi: 10.1126/science.1218632
    • (2012) Science , vol.336 , pp. 1306-1310
    • Vos, M.1    Esposito, G.2    Edirisinghe, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.