메뉴 건너뛰기




Volumn 92, Issue 1, 2014, Pages 31-42

An emerging role of PARK2 in cancer

Author keywords

Deletion; Metabolism; Mitophagy; Mutation; PARK2; Tumor suppressor

Indexed keywords

MESSENGER RNA; PARKIN; PROTEIN TYROSINE KINASE;

EID: 84891888589     PISSN: 09462716     EISSN: 14321440     Source Type: Journal    
DOI: 10.1007/s00109-013-1107-0     Document Type: Review
Times cited : (90)

References (130)
  • 2
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • 1:CAS:528:DC%2BC3MXlsVGltrw%3D 3444301 21532592 10.1038/nature09966
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474:105-108
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 7
    • 84867233572 scopus 로고    scopus 로고
    • Lack of association between cancer history and PARKIN genotype: A family based study in PARKIN/Parkinson's families
    • 1:CAS:528:DC%2BC38Xht1Ciur3M 3465486 22927236 10.1002/gcc.21995
    • Alcalay RN, Clark LN, Marder KS, Bradley WE (2012) Lack of association between cancer history and PARKIN genotype: a family based study in PARKIN/Parkinson's families. Genes Chromosomes Cancer 51:1109-1113
    • (2012) Genes Chromosomes Cancer , vol.51 , pp. 1109-1113
    • Alcalay, R.N.1    Clark, L.N.2    Marder, K.S.3    Bradley, W.E.4
  • 8
    • 84875909195 scopus 로고    scopus 로고
    • Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation
    • 1:CAS:528:DC%2BC3sXnsV2msrs%3D 23470638 10.4161/cc.24215
    • Sun XD, Liu M, Hao JH, Li DW, Luo YG, Wang XC, Yang YF, Li F, Shui WQ, Chen Q et al (2013) Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation. Cell Cycle 12:1133-1141
    • (2013) Cell Cycle , vol.12 , pp. 1133-1141
    • Sun, X.D.1    Liu, M.2    Hao, J.H.3    Li, D.W.4    Luo, Y.G.5    Wang, X.C.6    Yang, Y.F.7    Li, F.8    Shui, W.Q.9    Chen, Q.10
  • 9
    • 77956517757 scopus 로고    scopus 로고
    • Parkin enhances the expression of cyclin-dependent kinase 6 and negatively regulates the proliferation of breast cancer cells
    • 1:CAS:528:DC%2BC3cXhtFCns7jI 20630868 10.1074/jbc.M110.108241
    • Tay SP, Yeo CW, Chai C, Chua PJ, Tan HM, Ang AX, Yip DL, Sung JX, Tan PH, Bay BH et al (2010) Parkin enhances the expression of cyclin-dependent kinase 6 and negatively regulates the proliferation of breast cancer cells. J Biol Chem 285:29231-29238
    • (2010) J Biol Chem , vol.285 , pp. 29231-29238
    • Tay, S.P.1    Yeo, C.W.2    Chai, C.3    Chua, P.J.4    Tan, H.M.5    Ang, A.X.6    Yip, D.L.7    Sung, J.X.8    Tan, P.H.9    Bay, B.H.10
  • 12
    • 73349125417 scopus 로고    scopus 로고
    • Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies
    • 1:CAS:528:DC%2BD1MXhsVylsb%2FN 19946270 10.1038/ng.491
    • Veeriah S, Taylor BS, Meng S, Fang F, Yilmaz E, Vivanco I, Janakiraman M, Schultz N, Hanrahan AJ, Pao W et al (2010) Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies. Nat Genet 42:77-82
    • (2010) Nat Genet , vol.42 , pp. 77-82
    • Veeriah, S.1    Taylor, B.S.2    Meng, S.3    Fang, F.4    Yilmaz, E.5    Vivanco, I.6    Janakiraman, M.7    Schultz, N.8    Hanrahan, A.J.9    Pao, W.10
  • 17
    • 80053635472 scopus 로고    scopus 로고
    • Parkin, a p53 target gene, mediates the role of p53 in glucose metabolism and the Warburg effect
    • 1:CAS:528:DC%2BC3MXht1Kmtb%2FI 3182683 21930938 10.1073/pnas.1113884108
    • Zhang C, Lin M, Wu R, Wang X, Yang B, Levine AJ, Hu W, Feng Z (2011) Parkin, a p53 target gene, mediates the role of p53 in glucose metabolism and the Warburg effect. Proc Natl Acad Sci U S A 108:16259-16264
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16259-16264
    • Zhang, C.1    Lin, M.2    Wu, R.3    Wang, X.4    Yang, B.5    Levine, A.J.6    Hu, W.7    Feng, Z.8
  • 18
    • 79954417075 scopus 로고    scopus 로고
    • Parkin is transcriptionally regulated by ATF4: Evidence for an interconnection between mitochondrial stress and ER stress
    • 1:CAS:528:DC%2BC3MXksFWju78%3D 21113145 10.1038/cdd.2010.142
    • Bouman L, Schlierf A, Lutz AK, Shan J, Deinlein A, Kast J, Galehdar Z, Palmisano V, Patenge N, Berg D et al (2011) Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress. Cell Death Differ 18:769-782
    • (2011) Cell Death Differ , vol.18 , pp. 769-782
    • Bouman, L.1    Schlierf, A.2    Lutz, A.K.3    Shan, J.4    Deinlein, A.5    Kast, J.6    Galehdar, Z.7    Palmisano, V.8    Patenge, N.9    Berg, D.10
  • 20
    • 34247132171 scopus 로고    scopus 로고
    • Cell type-specific upregulation of parkin in response to ER stress
    • DOI 10.1089/ars.2006.1522
    • Wang HQ, Imai Y, Kataoka A, Takahashi R (2007) Cell type-specific upregulation of parkin in response to ER stress. Antioxid Redox Signal 9:533-542 (Pubitemid 46598251)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.5 , pp. 533-541
    • Wang, H.-Q.1    Imai, Y.2    Kataoka, A.3    Takahashi, R.4
  • 25
    • 33748486517 scopus 로고    scopus 로고
    • AceView: A comprehensive cDNA-supported gene and transcripts annotation
    • 10.1186/gb-2006-7-s1-s12 11-14
    • Thierry-Mieg D, Thierry-Mieg J (2006) AceView: a comprehensive cDNA-supported gene and transcripts annotation. Genome Biol 7(Suppl 1):S12 11-14
    • (2006) Genome Biol , vol.7 , Issue.SUPPL 1 , pp. 12
    • Thierry-Mieg, D.1    Thierry-Mieg, J.2
  • 26
    • 0037016687 scopus 로고    scopus 로고
    • Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain
    • DOI 10.1074/jbc.M109806200
    • Fallon L, Moreau F, Croft BG, Labib N, Gu WJ, Fon EA (2002) Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. J Biol Chem 277:486-491 (Pubitemid 34952083)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 486-491
    • Fallon, L.1    Moreau, F.2    Croft, B.G.3    Labib, N.4    Gu, W.-J.5    Fon, E.A.6
  • 30
    • 79960649509 scopus 로고    scopus 로고
    • Autoregulation of parkin activity through its ubiquitin-like domain
    • 1:CAS:528:DC%2BC3MXnvVektb0%3D 21694720 10.1038/emboj.2011.204
    • Chaugule VK, Burchell L, Barber KR, Sidhu A, Leslie SJ, Shaw GS, Walden H (2011) Autoregulation of parkin activity through its ubiquitin-like domain. Embo J 30:2853-2867
    • (2011) Embo J , vol.30 , pp. 2853-2867
    • Chaugule, V.K.1    Burchell, L.2    Barber, K.R.3    Sidhu, A.4    Leslie, S.J.5    Shaw, G.S.6    Walden, H.7
  • 31
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
    • 1:CAS:528:DC%2BC3sXhs1KqtLw%3D 23319602 10.1083/jcb.201210111
    • Lazarou M, Narendra DP, Jin SM, Tekle E, Banerjee S, Youle RJ (2013) PINK1 drives parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J Cell Biol 200:163-172
    • (2013) J Cell Biol , vol.200 , pp. 163-172
    • Lazarou, M.1    Narendra, D.P.2    Jin, S.M.3    Tekle, E.4    Banerjee, S.5    Youle, R.J.6
  • 33
    • 78650881155 scopus 로고    scopus 로고
    • Novel regulation of parkin function through c-Abl-mediated tyrosine phosphorylation: Implications for Parkinson's disease
    • 1:CAS:528:DC%2BC3MXls1yhug%3D%3D 3039694 21209200 10.1523/JNEUROSCI.1833- 10.2011
    • Imam SZ, Zhou Q, Yamamoto A, Valente AJ, Ali SF, Bains M, Roberts JL, Kahle PJ, Clark RA, Li S (2011) Novel regulation of parkin function through c-Abl-mediated tyrosine phosphorylation: implications for Parkinson's disease. J Neurosci 31:157-163
    • (2011) J Neurosci , vol.31 , pp. 157-163
    • Imam, S.Z.1    Zhou, Q.2    Yamamoto, A.3    Valente, A.J.4    Ali, S.F.5    Bains, M.6    Roberts, J.L.7    Kahle, P.J.8    Clark, R.A.9    Li, S.10
  • 34
    • 34250344611 scopus 로고    scopus 로고
    • Phosphorylation of Parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation
    • DOI 10.1074/jbc.M608243200
    • Avraham E, Rott R, Liani E, Szargel R, Engelender S (2007) Phosphorylation of parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation. J Biol Chem 282:12842-12850 (Pubitemid 47100582)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12842-12850
    • Avraham, E.1    Rott, R.2    Liani, E.3    Szargel, R.4    Engelender, S.5
  • 37
    • 72149095496 scopus 로고    scopus 로고
    • SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination
    • 1:CAS:528:DC%2BC3cXhslaqs70%3D 20064468 10.1016/j.molcel.2009.11.021
    • Trempe JF, Chen CX, Grenier K, Camacho EM, Kozlov G, McPherson PS, Gehring K, Fon EA (2009) SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination. Mol Cell 36:1034-1047
    • (2009) Mol Cell , vol.36 , pp. 1034-1047
    • Trempe, J.F.1    Chen, C.X.2    Grenier, K.3    Camacho, E.M.4    Kozlov, G.5    McPherson, P.S.6    Gehring, K.7    Fon, E.A.8
  • 38
    • 84865656962 scopus 로고    scopus 로고
    • Regulation of parkin E3 ubiquitin ligase activity
    • 1:CAS:528:DC%2BC38Xht1Gku7nJ 22527713 10.1007/s00018-012-0978-5
    • Walden H, Martinez-Torres RJ (2012) Regulation of parkin E3 ubiquitin ligase activity. Cell Mol Life Sci 69:3053-3067
    • (2012) Cell Mol Life Sci , vol.69 , pp. 3053-3067
    • Walden, H.1    Martinez-Torres, R.J.2
  • 41
    • 45849149191 scopus 로고    scopus 로고
    • Loss of heterozygosity and copy number abnormality in clear cell renal cell carcinoma discovered by high-density Affymetrix 10K single nucleotide polymorphism mapping array
    • DOI 10.1593/neo.08160
    • Toma MI, Grosser M, Herr A, Aust DE, Meye A, Hoefling C, Fuessel S, Wuttig D, Wirth MP, Baretton GB (2008) Loss of heterozygosity and copy number abnormality in clear cell renal cell carcinoma discovered by high-density affymetrix 10K single nucleotide polymorphism mapping array. Neoplasia 10:634-642 (Pubitemid 351883879)
    • (2008) Neoplasia , vol.10 , Issue.7 , pp. 634-642
    • Toma, M.I.1    Grosser, M.2    Herr, A.3    Aust, D.E.4    Meye, A.5    Hoefling, C.6    Fuessel, S.7    Wuttig, D.8    Wirth, M.P.9    Baretton, G.B.10
  • 42
    • 77956402130 scopus 로고    scopus 로고
    • Genome-wide catalogue of chromosomal aberrations in Barrett's esophagus and esophageal adenocarcinoma: A high-density single nucleotide polymorphism array analysis
    • 1:CAS:528:DC%2BC3cXht1Gju7%2FL 10.1158/1940-6207.CAPR-09-0265
    • Gu JA, Ajani JA, Hawk ET, Ye YQ, Lee JH, Bhutani MS, Hofstetter WL, Swisher SG, Wang KK, Wu XF (2010) Genome-wide catalogue of chromosomal aberrations in Barrett's esophagus and esophageal adenocarcinoma: a high-density single nucleotide polymorphism array analysis. Cancer Prev Res 3:1176-1186
    • (2010) Cancer Prev Res , vol.3 , pp. 1176-1186
    • Gu, J.A.1    Ajani, J.A.2    Hawk, E.T.3    Ye, Y.Q.4    Lee, J.H.5    Bhutani, M.S.6    Hofstetter, W.L.7    Swisher, S.G.8    Wang, K.K.9    Wu, X.F.10
  • 43
    • 66349133436 scopus 로고    scopus 로고
    • High-resolution genomic copy number profiling of glioblastoma multiforme by single nucleotide polymorphism DNA microarray
    • 1:CAS:528:DC%2BD1MXmtFCisLk%3D 19435819 10.1158/1541-7786.MCR-08-0270
    • Yin D, Ogawa S, Kawamata N, Tunici P, Finocchiaro G, Eoli M, Ruckert C, Huynh T, Liu GT, Kato M et al (2009) High-resolution genomic copy number profiling of glioblastoma multiforme by single nucleotide polymorphism DNA microarray. Mol Cancer Res 7:665-677
    • (2009) Mol Cancer Res , vol.7 , pp. 665-677
    • Yin, D.1    Ogawa, S.2    Kawamata, N.3    Tunici, P.4    Finocchiaro, G.5    Eoli, M.6    Ruckert, C.7    Huynh, T.8    Liu, G.T.9    Kato, M.10
  • 44
    • 84858000213 scopus 로고    scopus 로고
    • Contribution of germline mutations to PARK2 gene inactivation in lung adenocarcinoma
    • 1:CAS:528:DC%2BC38XhvVSgtrc%3D 22302706 10.1002/gcc.21933
    • Iwakawa R, Okayama H, Kohno T, Sato-Otsubo A, Ogawa S, Yokota J (2012) Contribution of germline mutations to PARK2 gene inactivation in lung adenocarcinoma. Genes Chromosomes Cancer 51:462-472
    • (2012) Genes Chromosomes Cancer , vol.51 , pp. 462-472
    • Iwakawa, R.1    Okayama, H.2    Kohno, T.3    Sato-Otsubo, A.4    Ogawa, S.5    Yokota, J.6
  • 45
    • 84862777035 scopus 로고    scopus 로고
    • A comprehensive survey of genomic alterations in gastric cancer reveals systematic patterns of molecular exclusivity and co-occurrence among distinct therapeutic targets
    • 1:CAS:528:DC%2BC38Xps1Kiu7g%3D 3322587 22315472 10.1136/gutjnl-2011- 301839
    • Deng N, Goh LK, Wang H, Das K, Tao J, Tan IB, Zhang S, Lee M, Wu J, Lim KH et al (2012) A comprehensive survey of genomic alterations in gastric cancer reveals systematic patterns of molecular exclusivity and co-occurrence among distinct therapeutic targets. Gut 61:673-684
    • (2012) Gut , vol.61 , pp. 673-684
    • Deng, N.1    Goh, L.K.2    Wang, H.3    Das, K.4    Tao, J.5    Tan, I.B.6    Zhang, S.7    Lee, M.8    Wu, J.9    Lim, K.H.10
  • 47
    • 33645215136 scopus 로고    scopus 로고
    • Abnormal methylation of the common PARK2 and PACRG promoter is associated with downregulation of gene expression in acute lymphoblastic leukemia and chronic myeloid leukemia
    • 1:CAS:528:DC%2BD28Xjt1Gqtbc%3D 16287063 10.1002/ijc.21584
    • Agirre X, Roman-Gomez J, Vazquez I, Jimenez-Velasco A, Garate L, Montiel-Duarte C, Artieda P, Cordeu L, Lahortiga I, Calasanz MJ et al (2006) Abnormal methylation of the common PARK2 and PACRG promoter is associated with downregulation of gene expression in acute lymphoblastic leukemia and chronic myeloid leukemia. Int J Cancer 118:1945-1953
    • (2006) Int J Cancer , vol.118 , pp. 1945-1953
    • Agirre, X.1    Roman-Gomez, J.2    Vazquez, I.3    Jimenez-Velasco, A.4    Garate, L.5    Montiel-Duarte, C.6    Artieda, P.7    Cordeu, L.8    Lahortiga, I.9    Calasanz, M.J.10
  • 48
    • 84872401497 scopus 로고    scopus 로고
    • PARK2 and PACRG are commonly downregulated in clear-cell renal cell carcinoma and are associated with aggressive disease and poor clinical outcome
    • 1:CAS:528:DC%2BC38Xhs1ShtrrO 23125027 10.1002/gcc.22026
    • Toma MI, Wuttig D, Kaiser S, Herr A, Weber T, Zastrow S, Koch R, Meinhardt M, Baretton GB, Wirth MP et al (2013) PARK2 and PACRG are commonly downregulated in clear-cell renal cell carcinoma and are associated with aggressive disease and poor clinical outcome. Genes Chromosomes Cancer 52:265-273
    • (2013) Genes Chromosomes Cancer , vol.52 , pp. 265-273
    • Toma, M.I.1    Wuttig, D.2    Kaiser, S.3    Herr, A.4    Weber, T.5    Zastrow, S.6    Koch, R.7    Meinhardt, M.8    Baretton, G.B.9    Wirth, M.P.10
  • 49
    • 0344441899 scopus 로고    scopus 로고
    • Alterations in the common fragile site gene Parkin in ovarian and other cancers
    • DOI 10.1038/sj.onc.1207072
    • Denison SR, Wang F, Becker NA, Schule B, Kock N, Phillips LA, Klein C, Smith DI (2003) Alterations in the common fragile site gene parkin in ovarian and other cancers. Oncogene 22:8370-8378 (Pubitemid 37485529)
    • (2003) Oncogene , vol.22 , Issue.51 , pp. 8370-8378
    • Denison, S.R.1    Wang, F.2    Becker, N.A.3    Schule, B.4    Kock, N.5    Phillips, L.A.6    Klein, C.7    Smith, D.I.8
  • 51
    • 66749185308 scopus 로고    scopus 로고
    • Parkin regulates paclitaxel sensitivity in breast cancer via a microtubule-dependent mechanism
    • 1:CAS:528:DC%2BD1MXls1Ort7s%3D 19214989 10.1002/path.2512
    • Wang HX, Liu BB, Zhang C, Peng GY, Liu M, Li DW, Gu F, Chen Q, Dong JT, Fu L et al (2009) Parkin regulates paclitaxel sensitivity in breast cancer via a microtubule-dependent mechanism. Journal of Pathology 218:76-85
    • (2009) Journal of Pathology , vol.218 , pp. 76-85
    • Wang, H.X.1    Liu, B.B.2    Zhang, C.3    Peng, G.Y.4    Liu, M.5    Li, D.W.6    Gu, F.7    Chen, Q.8    Dong, J.T.9    Fu, L.10
  • 52
    • 0042522482 scopus 로고    scopus 로고
    • Characterization of FRA6E and its potential role in autosomal recessive juvenile parkinsonism and ovarian cancer
    • DOI 10.1002/gcc.10236
    • Denison SR, Callahan G, Becker NA, Phillips LA, Smith DI (2003) Characterization of FRA6E and its potential role in autosomal recessive juvenile parkinsonism and ovarian cancer. Gene Chromosome Canc 38:40-52 (Pubitemid 36994883)
    • (2003) Genes Chromosomes and Cancer , vol.38 , Issue.1 , pp. 40-52
    • Denison, S.R.1    Callahan, G.2    Becker, N.A.3    Phillips, L.A.4    Smith, D.I.5
  • 59
    • 34249946941 scopus 로고    scopus 로고
    • Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage
    • DOI 10.1093/hmg/ddm083
    • Stichel CC, Zhu XR, Bader V, Linnartz B, Schmidt S, Lubbert H (2007) Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage. Hum Mol Genet 16:2377-2393 (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
  • 62
    • 84876151446 scopus 로고    scopus 로고
    • Parkinsonism due to mutations in PINK1, parkin, and DJ-1 and oxidative stress and mitochondrial pathways
    • 22951446 10.1101/cshperspect.a009415 1:CAS:528:DC%2BC3sXntlemt7w%3D
    • Cookson MR (2012) Parkinsonism due to mutations in PINK1, parkin, and DJ-1 and oxidative stress and mitochondrial pathways. Cold Spring Harb Perspect Med 2:a009415
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. 009415
    • Cookson, M.R.1
  • 63
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and parkin: Links to parkinsonism
    • doi: 10.1101/cshperspect.a011338
    • Narendra D, Walker JE, Youle R (2012) Mitochondrial quality control mediated by PINK1 and parkin: links to parkinsonism. Cold Spring Harb Perspect Biol. doi: 10.1101/cshperspect.a011338
    • (2012) Cold Spring Harb Perspect Biol
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 64
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • 1:CAS:528:DC%2BC38XhvVWqtLnI 22743996 10.1038/cdd.2012.81
    • Ashrafi G, Schwarz TL (2013) The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ 20:31-42
    • (2013) Cell Death Differ , vol.20 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 68
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • DOI 10.1074/jbc.M500843200
    • Yang F, Jiang Q, Zhao J, Ren Y, Sutton MD, Feng J (2005) Parkin stabilizes microtubules through strong binding mediated by three independent domains. J Biol Chem 280:17154-17162 (Pubitemid 41389181)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3    Ren, Y.4    Sutton, M.D.5    Feng, J.6
  • 69
    • 63649093151 scopus 로고    scopus 로고
    • Parkin protects dopaminergic neurons against microtubule-depolymerizing toxins by attenuating microtubule-associated protein kinase activation
    • 1:CAS:528:DC%2BD1MXht1OqsrY%3D 19074146 10.1074/jbc.M806245200
    • Ren Y, Jiang H, Yang F, Nakaso K, Feng J (2009) Parkin protects dopaminergic neurons against microtubule-depolymerizing toxins by attenuating microtubule-associated protein kinase activation. J Biol Chem 284:4009-4017
    • (2009) J Biol Chem , vol.284 , pp. 4009-4017
    • Ren, Y.1    Jiang, H.2    Yang, F.3    Nakaso, K.4    Feng, J.5
  • 70
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to α/β tubulin and increases their ubiquitination and degradation
    • Ren Y, Zhao J, Feng J (2003) Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J Neurosci 23:3316-3324 (Pubitemid 36531973)
    • (2003) Journal of Neuroscience , vol.23 , Issue.8 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 72
    • 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 JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD, Chin LS (2007) Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 178:1025-1038 (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
  • 73
    • 82755184126 scopus 로고    scopus 로고
    • Regulation of cell migration by dynamic microtubules
    • 1:CAS:528:DC%2BC3MXhsFygtLbN 3256984 22001384 10.1016/j.semcdb.2011.09. 017
    • Kaverina I, Straube A (2011) Regulation of cell migration by dynamic microtubules. Semin Cell Dev Biol 22:968-974
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 968-974
    • Kaverina, I.1    Straube, A.2
  • 74
    • 13244269913 scopus 로고    scopus 로고
    • Regulation of microtubules in cell migration
    • DOI 10.1016/j.tcb.2004.12.006, PII S0962892404003381
    • Watanabe T, Noritake J, Kaibuchi K (2005) Regulation of microtubules in cell migration. Trends Cell Biol 15:76-83 (Pubitemid 40188217)
    • (2005) Trends in Cell Biology , vol.15 , Issue.2 , pp. 76-83
    • Watanabe, T.1    Noritake, J.2    Kaibuchi, K.3
  • 75
    • 0037422010 scopus 로고    scopus 로고
    • Parkin Is a Component of an SCF-like Ubiquitin Ligase Complex and Protects Postmitotic Neurons from Kainate Excitotoxicity
    • DOI 10.1016/S0896-6273(03)00084-9
    • Staropoli JF, McDermott C, Martinat C, Schulman B, Demireva E, Abeliovich A (2003) Parkin is a component of an SCF-like ubipuitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37:735-749 (Pubitemid 36288547)
    • (2003) Neuron , vol.37 , Issue.5 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 76
    • 58149393853 scopus 로고    scopus 로고
    • Direct binding with histone deacetylase 6 mediates the reversible recruitment of parkin to the centrosome
    • 1:CAS:528:DC%2BD1cXhsVKgsbnJ 2680492 19036992 10.1523/JNEUROSCI.2860-08. 2008
    • Jiang Q, Ren Y, Feng J (2008) Direct binding with histone deacetylase 6 mediates the reversible recruitment of parkin to the centrosome. J Neurosci 28:12993-13002
    • (2008) J Neurosci , vol.28 , pp. 12993-13002
    • Jiang, Q.1    Ren, Y.2    Feng, J.3
  • 77
    • 0142074728 scopus 로고    scopus 로고
    • Parkin is recruited to the centrosome in response to inhibition of proteasomes
    • DOI 10.1242/jcs.00700
    • Zhao J, Ren Y, Jiang Q, Feng J (2003) Parkin is recruited to the centrosome in response to inhibition of proteasomes. J Cell Sci 116:4011-4019 (Pubitemid 37279315)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 4011-4019
    • Zhao, J.1    Ren, Y.2    Jiang, Q.3    Feng, J.4
  • 78
    • 84862816740 scopus 로고    scopus 로고
    • The C-terminus of PARK2 is required for its self-interaction, solubility and role in the spindle assembly checkpoint
    • 1:CAS:528:DC%2BC38Xjt1yhur8%3D 22200450 10.1016/j.bbadis.2011.12.007
    • Chen Y, Fang ST, Yeh PC, Yang HH, Chen SY, Chang CJ, Zhai WJ, Chen YC, Juang YL (2012) The C-terminus of PARK2 is required for its self-interaction, solubility and role in the spindle assembly checkpoint. Biochim Biophys Acta 1822:573-580
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 573-580
    • Chen, Y.1    Fang, S.T.2    Yeh, P.C.3    Yang, H.H.4    Chen, S.Y.5    Chang, C.J.6    Zhai, W.J.7    Chen, Y.C.8    Juang, Y.L.9
  • 79
    • 58149096751 scopus 로고    scopus 로고
    • Parkin regulates Eg5 expression by Hsp70 ubiquitination-dependent inactivation of c-Jun NH2-terminal kinase
    • 1:CAS:528:DC%2BD1cXhsVylsrnE 18845538 10.1074/jbc.M806860200
    • Liu M, Aneja R, Sun X, Xie S, Wang H, Wu X, Dong JT, Li M, Joshi HC, Zhou J (2008) Parkin regulates Eg5 expression by Hsp70 ubiquitination-dependent inactivation of c-Jun NH2-terminal kinase. J Biol Chem 283:35783-35788
    • (2008) J Biol Chem , vol.283 , pp. 35783-35788
    • Liu, M.1    Aneja, R.2    Sun, X.3    Xie, S.4    Wang, H.5    Wu, X.6    Dong, J.T.7    Li, M.8    Joshi, H.C.9    Zhou, J.10
  • 82
    • 79952303794 scopus 로고    scopus 로고
    • PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson's disease
    • 1:CAS:528:DC%2BC3MXjsFeqtrc%3D 3063894 21376232 10.1016/j.cell.2011.02. 010
    • 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
    • (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
  • 83
    • 77955398958 scopus 로고    scopus 로고
    • Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells
    • 1:CAS:528:DC%2BC3cXovVartrs%3D 2900690 20547844 10.1073/pnas.0914569107
    • Suen DF, Narendra DP, Tanaka A, Manfredi G, Youle RJ (2010) Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells. Proc Natl Acad Sci U S A 107:11835-11840
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11835-11840
    • Suen, D.F.1    Narendra, D.P.2    Tanaka, A.3    Manfredi, G.4    Youle, R.J.5
  • 84
    • 33746466098 scopus 로고    scopus 로고
    • Mitochondrial mutations in cancer
    • DOI 10.1038/sj.onc.1209607, PII 1209607
    • Brandon M, Baldi P, Wallace DC (2006) Mitochondrial mutations in cancer. Oncogene 25:4647-4662 (Pubitemid 44187615)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4647-4662
    • Brandon, M.1    Baldi, P.2    Wallace, D.C.3
  • 85
    • 33746891176 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in human cancer
    • DOI 10.1038/sj.onc.1209604, PII 1209604
    • Chatterjee A, Mambo E, Sidransky D (2006) Mitochondrial DNA mutations in human cancer. Oncogene 25:4663-4674 (Pubitemid 44187616)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4663-4674
    • Chatterjee, A.1    Mambo, E.2    Sidransky, D.3
  • 86
    • 28444490412 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in cancer
    • DOI 10.1371/journal.pmed.0020401, e401
    • Zanssen S, Schon EA (2005) Mitochondrial DNA mutations in cancer. PLoS Med 2:e401 (Pubitemid 41735771)
    • (2005) PLoS Medicine , vol.2 , Issue.11 , pp. 1082-1084
    • Zanssen, S.1    Schon, E.A.2
  • 87
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for parkin recruitment to damaged mitochondria
    • 3432468 22910362 10.1038/ncomms2016 1:CAS:528:DC%2BC38XhsleitLfL
    • Okatsu K, Oka T, Iguchi M, Imamura K, Kosako H, Tani N, Kimura M, Go E, Koyano F, Funayama M et al (2012) PINK1 autophosphorylation upon membrane potential dissipation is essential for parkin recruitment to damaged mitochondria. Nat Commun 3:1016
    • (2012) Nat Commun , vol.3 , pp. 1016
    • Okatsu, K.1    Oka, T.2    Iguchi, M.3    Imamura, K.4    Kosako, H.5    Tani, N.6    Kimura, M.7    Go, E.8    Koyano, F.9    Funayama, M.10
  • 89
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase parkin
    • 1:CAS:528:DC%2BC38Xit12htL4%3D 3288275 22280891 10.1016/j.devcel.2011.12. 014
    • Lazarou M, Jin SM, Kane LA, Youle RJ (2012) Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase parkin. Dev Cell 22:320-333
    • (2012) Dev Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 90
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated by mitochondrial membrane potential depolarization and stimulates parkin E3 ligase activity by phosphorylating Serine 65
    • 3376738 22724072 10.1098/rsob.120080 1:CAS:528:DC%2BC38XhtlSlsL3N
    • Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, Gourlay R, Burchell L, Walden H, Macartney TJ, Deak M et al (2012) PINK1 is activated by mitochondrial membrane potential depolarization and stimulates parkin E3 ligase activity by phosphorylating Serine 65. Open Biol 2:120080
    • (2012) Open Biol , vol.2 , pp. 120080
    • Kondapalli, C.1    Kazlauskaite, A.2    Zhang, N.3    Woodroof, H.I.4    Campbell, D.G.5    Gourlay, R.6    Burchell, L.7    Walden, H.8    Macartney, T.J.9    Deak, M.10
  • 91
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the parkin ubiquitin-like domain primes mitochondrial translocation of parkin and regulates mitophagy
    • 3525937 23256036 10.1038/srep01002 1:CAS:528:DC%2BC3sXhtFaqtrk%3D
    • Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, Sato S, Hattori N (2012) PINK1-mediated phosphorylation of the parkin ubiquitin-like domain primes mitochondrial translocation of parkin and regulates mitophagy. Sci Rep 2:1002
    • (2012) Sci Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 92
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • 1:CAS:528:DC%2BC3sXkvFOqs7k%3D 3641819 23503661 10.1038/nature12043
    • Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW (2013) Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 496:372-376
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3    Sowa, M.E.4    Huttlin, E.L.5    Gygi, S.P.6    Harper, J.W.7
  • 94
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • 1:CAS:528:DC%2BC3MXhsVKgsLbP 3261796 22078885 10.1016/j.cell.2011.10.018
    • 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
    • (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
  • 95
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • 1:CAS:528:DC%2BD1cXhsVOjtrjJ 19029340 10.1083/jcb.200809125
    • Narendra D, Tanaka A, Suen DF, Youle RJ (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. Journal of Cell Biology 183:795-803
    • (2008) Journal of Cell Biology , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 98
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is required for parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • 1:CAS:528:DC%2BC3cXhs1WltrjK 20890124 10.4161/auto.6.8.13426
    • Narendra D, Kane LA, Hauser DN, Fearnley IM, Youle RJ (2010) p62/SQSTM1 is required for parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6:1090-1106
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 99
    • 41149105722 scopus 로고    scopus 로고
    • Mitochondria in cancer cells: What is so special about them?
    • 1:CAS:528:DC%2BD1cXktlGksbg%3D 18296052 10.1016/j.tcb.2008.01.006
    • Gogvadze V, Orrenius S, Zhivotovsky B (2008) Mitochondria in cancer cells: what is so special about them? Trends Cell Biol 18:165-173
    • (2008) Trends Cell Biol , vol.18 , pp. 165-173
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 101
    • 70350689923 scopus 로고    scopus 로고
    • Parkin selectively alters the intrinsic threshold for mitochondrial cytochrome c release
    • 1:CAS:528:DC%2BD1MXhtlWhu7bJ 19679562 10.1093/hmg/ddp384
    • Berger AK, Cortese GP, Amodeo KD, Weihofen A, Letai A, LaVoie MJ (2009) Parkin selectively alters the intrinsic threshold for mitochondrial cytochrome c release. Hum Mol Genet 18:4317-4328
    • (2009) Hum Mol Genet , vol.18 , pp. 4317-4328
    • Berger, A.K.1    Cortese, G.P.2    Amodeo, K.D.3    Weihofen, A.4    Letai, A.5    Lavoie, M.J.6
  • 103
    • 84859962717 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax
    • 1:CAS:528:DC%2BC38Xmt1Omu7s%3D 3341078 22460798 10.1073/pnas.1113248109
    • Johnson BN, Berger AK, Cortese GP, LaVoie MJ (2012) The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax. Proc Natl Acad Sci U S A 109:6283-6288
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6283-6288
    • Johnson, B.N.1    Berger, A.K.2    Cortese, G.P.3    Lavoie, M.J.4
  • 104
    • 84883521293 scopus 로고    scopus 로고
    • Parkin-dependent degradation of the f-box protein fbw7beta promotes neuronal survival in response to oxidative stress by stabilizing mcl-1
    • 1:CAS:528:DC%2BC3sXhtl2jsrrN 23858059 10.1128/MCB.00535-13
    • Ekholm-Reed S, Goldberg MS, Schlossmacher MG, Reed SI (2013) Parkin-dependent degradation of the f-box protein fbw7beta promotes neuronal survival in response to oxidative stress by stabilizing mcl-1. Mol Cell Biol 33:3627-3643
    • (2013) Mol Cell Biol , vol.33 , pp. 3627-3643
    • Ekholm-Reed, S.1    Goldberg, M.S.2    Schlossmacher, M.G.3    Reed, S.I.4
  • 105
    • 78649653044 scopus 로고    scopus 로고
    • Parkin mono-ubiquitinates Bcl-2 and regulates autophagy
    • 1:CAS:528:DC%2BC3cXhsVOku7zJ 20889974 10.1074/jbc.M110.101469
    • Chen D, Gao F, Li B, Wang HF, Xu YX, Zhu CQ, Wang GH (2010) Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J Biol Chem 285:38214-38223
    • (2010) J Biol Chem , vol.285 , pp. 38214-38223
    • Chen, D.1    Gao, F.2    Li, B.3    Wang, H.F.4    Xu, Y.X.5    Zhu, C.Q.6    Wang, G.H.7
  • 108
    • 84871453443 scopus 로고    scopus 로고
    • Parkin induces apoptotic cell death in TNF-alpha-treated cervical cancer cells
    • 1:CAS:528:DC%2BC38XhsFyitLrI 23010174 10.5483/BMBRep.2012.45.9.104
    • Lee K, Lee MH, Kang YW, Rhee KJ, Kim TU, Kim YS (2012) Parkin induces apoptotic cell death in TNF-alpha-treated cervical cancer cells. BMB Rep 45:526-531
    • (2012) BMB Rep , vol.45 , pp. 526-531
    • Lee, K.1    Lee, M.H.2    Kang, Y.W.3    Rhee, K.J.4    Kim, T.U.5    Kim, Y.S.6
  • 109
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • 1:CAS:528:DC%2BC3MXjsFeqtrk%3D 21376230 10.1016/j.cell.2011.02.013
    • Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 110
    • 28844439032 scopus 로고    scopus 로고
    • Proteomic analysis of parkin knockout mice: Alterations in energy metabolism, protein handling and synaptic function
    • DOI 10.1111/j.1471-4159.2005.03442.x
    • Periquet M, Corti O, Jacquier S, Brice A (2005) Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J Neurochem 95:1259-1276 (Pubitemid 41779252)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.5 , pp. 1259-1276
    • Periquet, M.1    Corti, O.2    Jacquier, S.3    Brice, A.4
  • 112
    • 70349970658 scopus 로고    scopus 로고
    • Stable isotope labeling and label-free proteomics of Drosophila parkin null mutants
    • 1:CAS:528:DC%2BD1MXhtFehurnO 2766925 19705877 10.1021/pr9006238
    • Xun Z, Kaufman TC, Clemmer DE (2009) Stable isotope labeling and label-free proteomics of Drosophila parkin null mutants. J Proteome Res 8:4500-4510
    • (2009) J Proteome Res , vol.8 , pp. 4500-4510
    • Xun, Z.1    Kaufman, T.C.2    Clemmer, D.E.3
  • 113
    • 15544380902 scopus 로고    scopus 로고
    • Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
    • DOI 10.1093/hmg/ddi074
    • Greene JC, Whitworth AJ, Andrews LA, Parker TJ, Pallanck LJ (2005) Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis. Hum Mol Genet 14:799-811 (Pubitemid 40403276)
    • (2005) Human Molecular Genetics , vol.14 , Issue.6 , pp. 799-811
    • Greene, J.C.1    Whitworth, A.J.2    Andrews, L.A.3    Parker, T.J.4    Pallanck, L.J.5
  • 114
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • DOI 10.1242/dev.01095
    • Pesah Y, Pham T, Burgess H, Middlebrooks B, Verstreken P, Zhou Y, Harding M, Bellen H, Mardon G (2004) Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131:2183-2194 (Pubitemid 38702049)
    • (2004) Development , vol.131 , Issue.9 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5    Zhou, Y.6    Harding, M.7    Bellen, H.8    Mardon, G.9
  • 115
    • 77955594704 scopus 로고    scopus 로고
    • Extended lifespan of Drosophila parkin mutants through sequestration of redox-active metals and enhancement of anti-oxidative pathways
    • 1:CAS:528:DC%2BC3cXhtVGrt7rF 20483372 10.1016/j.nbd.2010.05.011
    • Saini N, Oelhafen S, Hua H, Georgiev O, Schaffner W, Bueler H (2010) Extended lifespan of Drosophila parkin mutants through sequestration of redox-active metals and enhancement of anti-oxidative pathways. Neurobiol Dis 40:82-92
    • (2010) Neurobiol Dis , vol.40 , pp. 82-92
    • Saini, N.1    Oelhafen, S.2    Hua, H.3    Georgiev, O.4    Schaffner, W.5    Bueler, H.6
  • 116
    • 45049084568 scopus 로고    scopus 로고
    • Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress
    • 1:CAS:528:DC%2BD1cXnt1Sksrw%3D 18541373 10.1016/j.neulet.2008.05.052
    • Yu F, Zhou J (2008) Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci Lett 440:4-8
    • (2008) Neurosci Lett , vol.440 , pp. 4-8
    • Yu, F.1    Zhou, J.2
  • 117
    • 0037047311 scopus 로고    scopus 로고
    • Effect of wild-type or mutant parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome
    • DOI 10.1074/jbc.M200666200
    • Hyun DH, Lee M, Hattori N, Kubo S, Mizuno Y, Halliwell B, Jenner P (2002) Effect of wild-type or mutant parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome. J Biol Chem 277:28572-28577 (Pubitemid 41079284)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.32 , pp. 28572-28577
    • Hyun, D.-H.1    Lee, M.2    Hattori, N.3    Kubo, S.-I.4    Mizuno, Y.5    Halliwell, B.6    Jenner, P.7
  • 121
    • 0344875488 scopus 로고    scopus 로고
    • Inactivation of parkin by oxidative stress and C-terminal truncations: A protective role of molecular chaperones
    • DOI 10.1074/jbc.M306769200
    • Winklhofer KF, Henn IH, Kay-Jackson PC, Heller U, Tatzelt J (2003) Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones. J Biol Chem 278:47199-47208 (Pubitemid 37452306)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47199-47208
    • Winklhofer, K.F.1    Henn, I.H.2    Kay-Jackson, P.C.3    Heller, U.4    Tatzelt, J.5
  • 122
    • 79956007514 scopus 로고    scopus 로고
    • Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregation
    • 1:CAS:528:DC%2BC3MXmvVKrtrk%3D 3120712 21595948 10.1186/1750-1326-6-34
    • Meng F, Yao D, Shi Y, Kabakoff J, Wu W, Reicher J, Ma Y, Moosmann B, Masliah E, Lipton SA et al (2011) Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregation. Mol Neurodegener 6:34
    • (2011) Mol Neurodegener , vol.6 , pp. 34
    • Meng, F.1    Yao, D.2    Shi, Y.3    Kabakoff, J.4    Wu, W.5    Reicher, J.6    Ma, Y.7    Moosmann, B.8    Masliah, E.9    Lipton, S.A.10
  • 126
    • 77955058151 scopus 로고    scopus 로고
    • Parkin suppresses c-Jun N-terminal kinase-induced cell death via transcriptional regulation in Drosophila
    • 1:CAS:528:DC%2BC3cXptFKrtb4%3D 20496123 10.1007/s10059-010-0068-1
    • Hwang S, Kim D, Choi G, An SW, Hong YK, Suh YS, Lee MJ, Cho KS (2010) Parkin suppresses c-Jun N-terminal kinase-induced cell death via transcriptional regulation in Drosophila. Mol Cells 29:575-580
    • (2010) Mol Cells , vol.29 , pp. 575-580
    • Hwang, S.1    Kim, D.2    Choi, G.3    An, S.W.4    Hong, Y.K.5    Suh, Y.S.6    Lee, M.J.7    Cho, K.S.8
  • 129
    • 79952035031 scopus 로고    scopus 로고
    • Parkin degrades estrogen-related receptors to limit the expression of monoamine oxidases
    • 1:CAS:528:DC%2BC3MXisFaguro%3D 21177257 10.1093/hmg/ddq550
    • Ren Y, Jiang H, Ma D, Nakaso K, Feng J (2011) Parkin degrades estrogen-related receptors to limit the expression of monoamine oxidases. Hum Mol Genet 20:1074-1083
    • (2011) Hum Mol Genet , vol.20 , pp. 1074-1083
    • Ren, Y.1    Jiang, H.2    Ma, D.3    Nakaso, K.4    Feng, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.