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Volumn 12, Issue JUN, 2018, Pages

Linking glycation and glycosylation with inflammation and mitochondrial dysfunction in Parkinson's disease

Author keywords

Aging; Glycation; Glycosylation; Inflammation; Mitochondrial dysfunction; Parkinson's disease

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; ALPHA SYNUCLEIN; GLYOXALASE; METHYLGLYOXAL; PARKIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PTEN INDUCED PUTATIVE KINASE 1; UNCLASSIFIED DRUG;

EID: 85048250230     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2018.00381     Document Type: Review
Times cited : (60)

References (213)
  • 1
    • 84928009282 scopus 로고    scopus 로고
    • Neuroprotective effects of vildagliptin in rat rotenone Parkinson's disease model: role of RAGE-NFκB and Nrf2-antioxidant signaling pathways
    • Abdelsalam, R. M., and Safar, M. M. (2015). Neuroprotective effects of vildagliptin in rat rotenone Parkinson's disease model: role of RAGE-NFκB and Nrf2-antioxidant signaling pathways. J. Neurochem. 133, 700-707. doi: 10.1111/jnc.13087
    • (2015) J. Neurochem , vol.133 , pp. 700-707
    • Abdelsalam, R.M.1    Safar, M.M.2
  • 2
    • 84881251018 scopus 로고    scopus 로고
    • Molecular strategies to prevent, inhibit, and degrade advanced glycoxidation and advanced lipoxidation end products
    • Aldini, G., Vistoli, G., Stefek, M., Chondrogianni, N., Grune, T., Sereikaite, J., et al. (2013). Molecular strategies to prevent, inhibit, and degrade advanced glycoxidation and advanced lipoxidation end products. Free Radic. Res. 47(Suppl. 1), 93-137. doi: 10.3109/10715762.2013.792926
    • (2013) Free Radic. Res , vol.47 , pp. 93-137
    • Aldini, G.1    Vistoli, G.2    Stefek, M.3    Chondrogianni, N.4    Grune, T.5    Sereikaite, J.6
  • 3
    • 77955703092 scopus 로고    scopus 로고
    • RAGE: a multi-ligand receptor unveiling novel insights in health and disease
    • Alexiou, P., Chatzopoulou, M., Pegklidou, K., and Demopoulos, V. J. (2010). RAGE: a multi-ligand receptor unveiling novel insights in health and disease. Curr. Med. Chem. 17, 2232-2252. doi: 10.2174/092986710791331086
    • (2010) Curr. Med. Chem , vol.17 , pp. 2232-2252
    • Alexiou, P.1    Chatzopoulou, M.2    Pegklidou, K.3    Demopoulos, V.J.4
  • 4
    • 84860811239 scopus 로고    scopus 로고
    • Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets
    • Alfaro, J. F., Gong, C. X., Monroe, M. E., Aldrich, J. T., Clauss, T. R., Purvine, S. O., et al. (2012). Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proc. Natl. Acad. Sci. U.S.A. 109, 7280-7285. doi: 10.1073/pnas.1200425109
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 7280-7285
    • Alfaro, J.F.1    Gong, C.X.2    Monroe, M.E.3    Aldrich, J.T.4    Clauss, T.R.5    Purvine, S.O.6
  • 5
    • 84907482268 scopus 로고    scopus 로고
    • The proinflammatory RAGE/NF-kappaB pathway is involved in neuronal damage and reactive gliosis in a model of sleep apnea by intermittent hypoxia
    • Angelo, M. F., Aguirre, A., Aviles Reyes, R. X., Villarreal, A., Lukin, J., Melendez, M., et al. (2014). The proinflammatory RAGE/NF-kappaB pathway is involved in neuronal damage and reactive gliosis in a model of sleep apnea by intermittent hypoxia. PLoS One 9:e107901. doi: 10.1371/journal.pone.0107901
    • (2014) PLoS One , vol.9
    • Angelo, M.F.1    Aguirre, A.2    Aviles Reyes, R.X.3    Villarreal, A.4    Lukin, J.5    Melendez, M.6
  • 6
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H., and Sharon, N. (1999). On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473, 4-8. doi: 10.1016/S0304-4165(99)00165-8
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 8
    • 0034659178 scopus 로고    scopus 로고
    • Glycoxidation and lipoxidation in atherogenesis
    • Baynes, J. W., and Thorpe, S. R. (2000). Glycoxidation and lipoxidation in atherogenesis. Free Radic. Biol. Med. 28, 1708-1716. doi: 10.1016/S0891-5849(00)00228-8
    • (2000) Free Radic. Biol. Med , vol.28 , pp. 1708-1716
    • Baynes, J.W.1    Thorpe, S.R.2
  • 9
    • 56149114786 scopus 로고    scopus 로고
    • Diabetes in patients with idiopathic Parkinson's disease
    • Becker, C., Brobert, G. P., Johansson, S., Jick, S. S., and Meier, C. R. (2008). Diabetes in patients with idiopathic Parkinson's disease. Diabetes Care 31, 1808-1812. doi: 10.2337/dc08-0479
    • (2008) Diabetes Care , vol.31 , pp. 1808-1812
    • Becker, C.1    Brobert, G.P.2    Johansson, S.3    Jick, S.S.4    Meier, C.R.5
  • 11
    • 85027917509 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • Bose, A., and Beal, M. F. (2016). Mitochondrial dysfunction in Parkinson's disease. J. Neurochem. 139(Suppl. 1), 216-231. doi: 10.1111/jnc.13731
    • (2016) J. Neurochem , vol.139 , pp. 216-231
    • Bose, A.1    Beal, M.F.2
  • 12
    • 82155166363 scopus 로고    scopus 로고
    • High-fat diet exacerbates MPTP-induced dopaminergic degeneration in mice
    • Bousquet, M., St-Amour, I., Vandal, M., Julien, P., Cicchetti, F., and Calon, F. (2012). High-fat diet exacerbates MPTP-induced dopaminergic degeneration in mice. Neurobiol. Dis. 45, 529-538. doi: 10.1016/j.nbd.2011.09.009
    • (2012) Neurobiol. Dis , vol.45 , pp. 529-538
    • Bousquet, M.1    St-Amour, I.2    Vandal, M.3    Julien, P.4    Cicchetti, F.5    Calon, F.6
  • 13
    • 84861427711 scopus 로고    scopus 로고
    • Multiple proteins with essential mitochondrial functions have glycosylated isoforms
    • Burnham-Marusich, A. R., and Berninsone, P. M. (2012). Multiple proteins with essential mitochondrial functions have glycosylated isoforms. Mitochondrion 12, 423-427. doi: 10.1016/j.mito.2012.04.004
    • (2012) Mitochondrion , vol.12 , pp. 423-427
    • Burnham-Marusich, A.R.1    Berninsone, P.M.2
  • 14
    • 77957347060 scopus 로고    scopus 로고
    • Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro
    • Burre, J., Sharma, M., Tsetsenis, T., Buchman, V., Etherton, M. R., and Sudhof, T. C. (2010). Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 329, 1663-1667. doi: 10.1126/science.1195227
    • (2010) Science , vol.329 , pp. 1663-1667
    • Burre, J.1    Sharma, M.2    Tsetsenis, T.3    Buchman, V.4    Etherton, M.R.5    Sudhof, T.C.6
  • 15
    • 84873294436 scopus 로고    scopus 로고
    • The phagocytic capacity and immunological potency of human dendritic cells is improved by a2, 6-sialic acid deficiency
    • Cabral, M. G., Silva, Z., Ligeiro, D., Seixas, E., Crespo, H., Carrascal, M. A., et al. (2013). The phagocytic capacity and immunological potency of human dendritic cells is improved by a2, 6-sialic acid deficiency. Immunology 138, 235-245. doi: 10.1111/imm.12025
    • (2013) Immunology , vol.138 , pp. 235-245
    • Cabral, M.G.1    Silva, Z.2    Ligeiro, D.3    Seixas, E.4    Crespo, H.5    Carrascal, M.A.6
  • 16
    • 84868089556 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease
    • Castro-Caldas, M., Carvalho, A. N., Rodrigues, E., Henderson, C. J., Wolf, C. R., Rodrigues, C. M. P., et al. (2012). Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease. Mol. Neurobiol. 46, 475-486. doi: 10.1007/s12035-012-8295-4
    • (2012) Mol. Neurobiol , vol.46 , pp. 475-486
    • Castro-Caldas, M.1    Carvalho, A.N.2    Rodrigues, E.3    Henderson, C.J.4    Wolf, C.R.5    Rodrigues, C.M.P.6
  • 17
    • 84898783826 scopus 로고    scopus 로고
    • MHC-I expression renders catecholaminergic neurons susceptible to T-cell-mediated degeneration
    • Cebrián, C., Zucca, F. A., Mauri, P., Steinbeck, J. A., Studer, L., Scherzer, C. R., et al. (2014). MHC-I expression renders catecholaminergic neurons susceptible to T-cell-mediated degeneration. Nat. Commun. 5:3633. doi: 10.1038/ncomms4633
    • (2014) Nat. Commun , vol.5 , pp. 3633
    • Cebrián, C.1    Zucca, F.A.2    Mauri, P.3    Steinbeck, J.A.4    Studer, L.5    Scherzer, C.R.6
  • 18
    • 84863625218 scopus 로고    scopus 로고
    • Clinical features of Parkinson disease when onset of diabetes came first: a case-control study
    • Cereda, E., Barichella, M., Cassani, E., Caccialanza, R., and Pezzoli, G. (2012). Clinical features of Parkinson disease when onset of diabetes came first: a case-control study. Neurology 78, 1507-1511. doi: 10.1212/WNL.0b013e3182553cc9
    • (2012) Neurology , vol.78 , pp. 1507-1511
    • Cereda, E.1    Barichella, M.2    Cassani, E.3    Caccialanza, R.4    Pezzoli, G.5
  • 19
    • 85014096266 scopus 로고    scopus 로고
    • Post translational modification of Parkin
    • Chakraborty, J., Basso, V., and Ziviani, E. (2017). Post translational modification of Parkin. Biol. Direct 12:6. doi: 10.1186/s13062-017-0176-3
    • (2017) Biol. Direct , vol.12 , pp. 6
    • Chakraborty, J.1    Basso, V.2    Ziviani, E.3
  • 20
    • 0032584607 scopus 로고    scopus 로고
    • Identification of a glycoprotein from rat liver mitochondrial inner membrane and demonstration of its origin in the endoplasmic reticulum
    • Chandra, N. C., Spiro, M. J., and Spiro, R. G. (1998). Identification of a glycoprotein from rat liver mitochondrial inner membrane and demonstration of its origin in the endoplasmic reticulum. J. Biol. Chem. 273, 19715-19721. doi: 10.1074/jbc.273.31.19715
    • (1998) J. Biol. Chem , vol.273 , pp. 19715-19721
    • Chandra, N.C.1    Spiro, M.J.2    Spiro, R.G.3
  • 21
    • 32544432029 scopus 로고    scopus 로고
    • Non-motor symptoms of Parkinson's disease: diagnosis and management
    • Chaudhuri, K. R., Healy, D. G., and Schapira, A. H. (2006). Non-motor symptoms of Parkinson's disease: diagnosis and management. Lancet Neurol. 5, 235-245. doi: 10.1016/S1474-4422(06)70373-8
    • (2006) Lancet Neurol , vol.5 , pp. 235-245
    • Chaudhuri, K.R.1    Healy, D.G.2    Schapira, A.H.3
  • 22
    • 84983650290 scopus 로고    scopus 로고
    • The biomarkers of immune dysregulation and inflammation response in Parkinson disease
    • Chen, L., Mo, M., Li, G., Cen, L., Wei, L., Xiao, Y., et al. (2016). The biomarkers of immune dysregulation and inflammation response in Parkinson disease. Transl. Neurodegener. 5:16. doi: 10.1186/s40035-016-0063-3
    • (2016) Transl. Neurodegener , vol.5 , pp. 16
    • Chen, L.1    Mo, M.2    Li, G.3    Cen, L.4    Wei, L.5    Xiao, Y.6
  • 23
    • 68849129707 scopus 로고    scopus 로고
    • RAGE regulates BACE1 and Aß generation via NFAT1 activation in Alzheimer's disease animal model
    • Cho, H. J., Son, S. M., Jin, S. M., Hong, H. S., Shin, D. H., Kim, S. J., et al. (2009). RAGE regulates BACE1 and Aß generation via NFAT1 activation in Alzheimer's disease animal model. FASEB J. 23, 2639-2649. doi: 10.1096/fj.08-126383
    • (2009) FASEB J , vol.23 , pp. 2639-2649
    • Cho, H.J.1    Son, S.M.2    Jin, S.M.3    Hong, H.S.4    Shin, D.H.5    Kim, S.J.6
  • 24
    • 79955052386 scopus 로고    scopus 로고
    • Diversity in the regulation of autophagy and mitophagy: lessons from Parkinson's disease
    • Chu, C. T. (2011). Diversity in the regulation of autophagy and mitophagy: lessons from Parkinson's disease. Parkinson Dis. 2011:789431. doi: 10.4061/2011/789431
    • (2011) Parkinson Dis , vol.2011
    • Chu, C.T.1
  • 25
    • 0035116226 scopus 로고    scopus 로고
    • Dopaminergic cell death induced by MPP+, oxidant and specific neurotoxicants shares the common molecular mechanism
    • Chun, H. S., Gibson, G. E., DeGiorgio, L. A., Zhang, H., Kidd, V. J., and Son, J. H. (2001). Dopaminergic cell death induced by MPP+, oxidant and specific neurotoxicants shares the common molecular mechanism. J. Neurochem. 76, 1010-1021. doi: 10.1046/j.1471-4159.2001.00096.x
    • (2001) J. Neurochem , vol.76 , pp. 1010-1021
    • Chun, H.S.1    Gibson, G.E.2    DeGiorgio, L.A.3    Zhang, H.4    Kidd, V.J.5    Son, J.H.6
  • 26
    • 85018401049 scopus 로고    scopus 로고
    • Protein quality control by molecular chaperones in neurodegeneration
    • Ciechanover, A., and Kwon, Y. T. (2017). Protein quality control by molecular chaperones in neurodegeneration. Front. Neurosci. 11:185. doi: 10.3389/fnins.2017.00185
    • (2017) Front. Neurosci , vol.11 , pp. 185
    • Ciechanover, A.1    Kwon, Y.T.2
  • 27
    • 0026598930 scopus 로고
    • Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: evidence for free radical involvement
    • Cleeter, M. W. J., Cooper, J. M., and Schapira, A. H. V. (1992). Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: evidence for free radical involvement. J. Neurochem. 58, 786-789. doi: 10.1111/j.1471-4159.1992.tb09789.x
    • (1992) J. Neurochem , vol.58 , pp. 786-789
    • Cleeter, M.W.J.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 28
    • 33750052885 scopus 로고    scopus 로고
    • DJ-1, a cancer-and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2
    • Clements, C. M., McNally, R. S., Conti, B. J., Mak, T. W., and Ting, J. P. (2006). DJ-1, a cancer-and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. U.S.A. 103, 15091-15096. doi: 10.1073/pnas.0607260103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 15091-15096
    • Clements, C.M.1    McNally, R.S.2    Conti, B.J.3    Mak, T.W.4    Ting, J.P.5
  • 29
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T. Jr. (2000). Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U.S.A. 97, 571-576. doi: 10.1073/pnas.97.2.571
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 30
    • 84988692340 scopus 로고    scopus 로고
    • ER stress induced by tunicamycin triggers a-synuclein oligomerization, dopaminergic neurons death and locomotor impairment: a new model of Parkinson's disease
    • Cóppola-Segovia, V., Cavarsan, C., Maia, F. G., Ferraz, A. C., Nakao, L. S., Lima, M. M., et al. (2017). ER stress induced by tunicamycin triggers a-synuclein oligomerization, dopaminergic neurons death and locomotor impairment: a new model of Parkinson's disease. Mol. Neurobiol. 54, 5798-5806. doi: 10.1007/s12035-016-0114-x
    • (2017) Mol. Neurobiol , vol.54 , pp. 5798-5806
    • Cóppola-Segovia, V.1    Cavarsan, C.2    Maia, F.G.3    Ferraz, A.C.4    Nakao, L.S.5    Lima, M.M.6
  • 31
    • 84892173112 scopus 로고    scopus 로고
    • Dendritic cells: a spot on sialic acid
    • Crespo, H. J., Lau, J. T., and Videira, P. A. (2013). Dendritic cells: a spot on sialic acid. Front. Immunol. 4:491. doi: 10.3389/fimmu.2013.00491
    • (2013) Front. Immunol , vol.4 , pp. 491
    • Crespo, H.J.1    Lau, J.T.2    Videira, P.A.3
  • 33
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: mechanisms and models
    • Dauer, W., and Przedborski, S. (2003). Parkinson's disease: mechanisms and models. Neuron 39, 889-909. doi: 10.1016/S0896-6273(03)00568-3
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 34
    • 0037240325 scopus 로고    scopus 로고
    • Rare genetic mutations shed light on the pathogenesis of Parkinson disease
    • Dawson, T. M., and Dawson, V. L. (2003). Rare genetic mutations shed light on the pathogenesis of Parkinson disease. J. Clin. Invest. 111, 145-151. doi: 10.1172/JCI200317575
    • (2003) J. Clin. Invest , vol.111 , pp. 145-151
    • Dawson, T.M.1    Dawson, V.L.2
  • 35
    • 77953424577 scopus 로고    scopus 로고
    • The role of parkin in familial and sporadic Parkinson's disease
    • Dawson, T. M., and Dawson, V. L. (2010). The role of parkin in familial and sporadic Parkinson's disease. Mov. Disord. 25(Suppl. 1), 32-39. doi: 10.1002/mds.22798
    • (2010) Mov. Disord , vol.25 , pp. 32-39
    • Dawson, T.M.1    Dawson, V.L.2
  • 36
    • 84859723641 scopus 로고    scopus 로고
    • A multimodal RAGE-specific inhibitor reduces amyloid beta-mediated brain disorder in a mouse model of Alzheimer disease
    • Deane, R., Singh, I., Sagare, A. P., Bell, R. D., Ross, N. T., LaRue, B., et al. (2012). A multimodal RAGE-specific inhibitor reduces amyloid beta-mediated brain disorder in a mouse model of Alzheimer disease. J. Clin. Invest. 122, 1377-1392. doi: 10.1172/JCI58642
    • (2012) J. Clin. Invest , vol.122 , pp. 1377-1392
    • Deane, R.1    Singh, I.2    Sagare, A.P.3    Bell, R.D.4    Ross, N.T.5    LaRue, B.6
  • 37
    • 84863423974 scopus 로고    scopus 로고
    • Occurrence and distribution of salsolinol-like compound, 1-acetyl-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline (ADTIQ) in parkinsonian brains
    • Deng, Y., Zhang, Y., Li, Y., Xiao, S., Song, D., Qing, H., et al. (2012). Occurrence and distribution of salsolinol-like compound, 1-acetyl-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline (ADTIQ) in parkinsonian brains. J. Neural Transm. 119, 435-441. doi: 10.1007/s00702-011-0724-4
    • (2012) J. Neural Transm , vol.119 , pp. 435-441
    • Deng, Y.1    Zhang, Y.2    Li, Y.3    Xiao, S.4    Song, D.5    Qing, H.6
  • 38
    • 84881427177 scopus 로고    scopus 로고
    • Parkinson disease: from pathology to molecular disease mechanisms
    • Dexter, D. T., and Jenner, P. (2013). Parkinson disease: from pathology to molecular disease mechanisms. Free Radic. Biol. Med. 62, 132-144. doi: 10.1016/j.freeradbiomed.2013.01.018
    • (2013) Free Radic. Biol. Med , vol.62 , pp. 132-144
    • Dexter, D.T.1    Jenner, P.2
  • 39
    • 26944494920 scopus 로고    scopus 로고
    • Evaluation of RAGE isoforms, ligands, and signaling in the brain
    • Ding, Q., and Keller, J. N. (2005). Evaluation of RAGE isoforms, ligands, and signaling in the brain. Biochim. Biophys. Acta 1746, 18-27. doi: 10.1016/j.bbamcr.2005.08.006
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 18-27
    • Ding, Q.1    Keller, J.N.2
  • 40
    • 0034995073 scopus 로고    scopus 로고
    • S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato, R. (2001). S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33, 637-668. doi: 10.1016/S1357-2725(01)00046-2
    • (2001) Int. J. Biochem. Cell Biol , vol.33 , pp. 637-668
    • Donato, R.1
  • 41
    • 56149110407 scopus 로고    scopus 로고
    • Prospective cohort study of type 2 diabetes and the risk of Parkinson's disease
    • Driver, J. A., Smith, A., Buring, J. E., Gaziano, J. M., Kurth, T., and Logroscino, G. (2008). Prospective cohort study of type 2 diabetes and the risk of Parkinson's disease. Diabetes Care 31, 2003-2005. doi: 10.2337/dc08-0688
    • (2008) Diabetes Care , vol.31 , pp. 2003-2005
    • Driver, J.A.1    Smith, A.2    Buring, J.E.3    Gaziano, J.M.4    Kurth, T.5    Logroscino, G.6
  • 42
    • 27744510124 scopus 로고    scopus 로고
    • Circulating levels of soluble receptor for advanced glycation end products in Alzheimer disease and vascular dementia
    • Emanuele, E., D'Angelo, A., Tomaino, C., Binetti, G., Ghidoni, R., Politi, P., et al. (2005). Circulating levels of soluble receptor for advanced glycation end products in Alzheimer disease and vascular dementia. Arch. Neurol. 62, 1734-1736. doi: 10.1001/archneur.62.11.1734
    • (2005) Arch. Neurol , vol.62 , pp. 1734-1736
    • Emanuele, E.1    D'Angelo, A.2    Tomaino, C.3    Binetti, G.4    Ghidoni, R.5    Politi, P.6
  • 43
    • 84867450111 scopus 로고    scopus 로고
    • HMGB1 in development and diseases of the central nervous system
    • Fang, P., Schachner, M., and Shen, Y. (2012). HMGB1 in development and diseases of the central nervous system. Mol. Neurobiol. 45, 499-506. doi: 10.1007/s12035-012-8264-y
    • (2012) Mol. Neurobiol , vol.45 , pp. 499-506
    • Fang, P.1    Schachner, M.2    Shen, Y.3
  • 44
    • 77951176737 scopus 로고    scopus 로고
    • Extending human life span-from yeast to humans
    • Fontana, L., Partridge, L., and Longo, V. D. (2010). Extending human life span-from yeast to humans. Science 328, 321-326. doi: 10.1126/science.1172539
    • (2010) Science , vol.328 , pp. 321-326
    • Fontana, L.1    Partridge, L.2    Longo, V.D.3
  • 45
    • 78751502344 scopus 로고    scopus 로고
    • HMGB1 acts on microglia Mac1 to mediate chronic neuroinflammation that drives progressive neurodegeneration
    • Gao, H. M., Zhou, H., Zhang, F., Wilson, B. C., Kam, W., and Hong, J. S. (2011). HMGB1 acts on microglia Mac1 to mediate chronic neuroinflammation that drives progressive neurodegeneration. J. Neurosci. 31, 1081-1092. doi: 10.1523/JNEUROSCI.3732-10.2011
    • (2011) J. Neurosci , vol.31 , pp. 1081-1092
    • Gao, H.M.1    Zhou, H.2    Zhang, F.3    Wilson, B.C.4    Kam, W.5    Hong, J.S.6
  • 46
    • 84890841031 scopus 로고    scopus 로고
    • Association of RAGE gene polymorphisms with sporadic Parkinson's disease in Chinese Han population
    • Gao, J., Teng, J., Liu, H., Han, X., Chen, B., and Xie, A. (2014). Association of RAGE gene polymorphisms with sporadic Parkinson's disease in Chinese Han population. Neurosci. Lett. 559, 158-162. doi: 10.1016/j.neulet.2013.11.038
    • (2014) Neurosci. Lett , vol.559 , pp. 158-162
    • Gao, J.1    Teng, J.2    Liu, H.3    Han, X.4    Chen, B.5    Xie, A.6
  • 47
    • 36249019041 scopus 로고    scopus 로고
    • Prospective study of dietary pattern and risk of Parkinson disease
    • Gao, X., Chen, H., Fung, T. T., Logroscino, G., Schwarzschild, M. A., Hu, F. B., et al. (2007). Prospective study of dietary pattern and risk of Parkinson disease. Am. J. Clin. Nutr. 86, 1486-1494. doi: 10.1093/ajcn/86.5.1486
    • (2007) Am. J. Clin. Nutr , vol.86 , pp. 1486-1494
    • Gao, X.1    Chen, H.2    Fung, T.T.3    Logroscino, G.4    Schwarzschild, M.A.5    Hu, F.B.6
  • 48
    • 85027843681 scopus 로고    scopus 로고
    • Targeted inhibition of RAGE in substantia nigra of rats blocks 6-OHDA-induced dopaminergic denervation
    • Gasparotto, J., Ribeiro, C. T., Bortolin, R. C., Somensi, N., Rabelo, T. K., Kunzler, A., et al. (2017). Targeted inhibition of RAGE in substantia nigra of rats blocks 6-OHDA-induced dopaminergic denervation. Sci. Rep. 7:8795. doi: 10.1038/s41598-017-09257-3
    • (2017) Sci. Rep , vol.7 , pp. 8795
    • Gasparotto, J.1    Ribeiro, C.T.2    Bortolin, R.C.3    Somensi, N.4    Rabelo, T.K.5    Kunzler, A.6
  • 49
    • 84930655540 scopus 로고    scopus 로고
    • A comprehensive glycome profiling of Huntington's disease transgenic mice
    • Gizaw, S. T., Koda, T., Amano, M., Kamimura, K., Ohashi, T., Hinou, H., et al. (2015). A comprehensive glycome profiling of Huntington's disease transgenic mice. Biochim. Biophys. Acta 1850, 1704-1718. doi: 10.1016/j.bbagen.2015.04.006
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 1704-1718
    • Gizaw, S.T.1    Koda, T.2    Amano, M.3    Kamimura, K.4    Ohashi, T.5    Hinou, H.6
  • 50
    • 84962826217 scopus 로고    scopus 로고
    • Glycoblotting method allows for rapid and efficient glycome profiling of human Alzheimer's disease brain, serum and cerebrospinal fluid towards potential biomarker discovery
    • Gizaw, S. T., Ohashi, T., Tanaka, M., Hinou, H., and Nishimura, S. (2016). Glycoblotting method allows for rapid and efficient glycome profiling of human Alzheimer's disease brain, serum and cerebrospinal fluid towards potential biomarker discovery. Biochim. Biophys. Acta 1860, 1716-1727. doi: 10.1016/j.bbagen.2016.03.009
    • (2016) Biochim. Biophys. Acta , vol.1860 , pp. 1716-1727
    • Gizaw, S.T.1    Ohashi, T.2    Tanaka, M.3    Hinou, H.4    Nishimura, S.5
  • 51
    • 84885468645 scopus 로고    scopus 로고
    • Recent advances in a-synuclein functions, advanced glycation, and toxicity: implications for Parkinson's disease
    • Guerrero, E., Vasudevaraju, P., Hegde, M. L., Britton, G. B., and Rao, K. S. (2013). Recent advances in a-synuclein functions, advanced glycation, and toxicity: implications for Parkinson's disease. Mol. Neurobiol. 47, 525-536. doi: 10.1007/s12035-012-8328-z
    • (2013) Mol. Neurobiol , vol.47 , pp. 525-536
    • Guerrero, E.1    Vasudevaraju, P.2    Hegde, M.L.3    Britton, G.B.4    Rao, K.S.5
  • 52
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., and Roepstorff, P. (2004). A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J. Proteome Res. 3, 556-566. doi: 10.1021/pr034112b
    • (2004) J. Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 53
    • 18144406539 scopus 로고    scopus 로고
    • Oxidative stress and inflammation in Parkinson's disease: is there a causal link?
    • Hald, A., and Lotharius, J. (2005). Oxidative stress and inflammation in Parkinson's disease: is there a causal link? Exp. Neurol. 193, 279-290. doi: 10.1016/j.expneurol.2005.01.013
    • (2005) Exp. Neurol , vol.193 , pp. 279-290
    • Hald, A.1    Lotharius, J.2
  • 54
    • 79951499176 scopus 로고    scopus 로고
    • Glia: initiators and progressors of pathology in Parkinson's disease
    • Halliday, G. M., and Stevens, C. H. (2011). Glia: initiators and progressors of pathology in Parkinson's disease. Mov. Disord. 26, 6-17. doi: 10.1002/mds.23455
    • (2011) Mov. Disord , vol.26 , pp. 6-17
    • Halliday, G.M.1    Stevens, C.H.2
  • 55
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger, R. S., and Lowe, J. B. (2004). Role of glycosylation in development. Annu. Rev. Biochem. 73, 491-537. doi: 10.1146/annurev.biochem.73.011303.074043
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 56
    • 0035964192 scopus 로고    scopus 로고
    • Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment
    • Hastrup, H., Karlin, A., and Javitch, J. A. (2001). Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment. Proc. Natl. Acad. Sci. U.S.A. 98, 10055-10060. doi: 10.1073/pnas.181344298
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 10055-10060
    • Hastrup, H.1    Karlin, A.2    Javitch, J.A.3
  • 57
    • 84893858712 scopus 로고    scopus 로고
    • Serum N-glycan alteration associated with renal cell carcinoma detected by high-throughput glycan analysis
    • Hatakeyama, S., Amano, M., Tobisawa, Y., Yoneyama, T., Tsuchiya, N., Habuchi, T., et al. (2014). Serum N-glycan alteration associated with renal cell carcinoma detected by high-throughput glycan analysis. J. Urol. 191, 805-813. doi: 10.1016/j.juro.2013.10.052
    • (2014) J. Urol , vol.191 , pp. 805-813
    • Hatakeyama, S.1    Amano, M.2    Tobisawa, Y.3    Yoneyama, T.4    Tsuchiya, N.5    Habuchi, T.6
  • 58
    • 0142091435 scopus 로고    scopus 로고
    • Time-course of the expression of inflammatory cytokines and matrix metalloproteinases in the striatum and mesencephalon of mice injected with 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine, a dopaminergic neurotoxin
    • Hebert, G., Arsaut, J., Dantzer, R., and Demotes-Mainard, J. (2003). Time-course of the expression of inflammatory cytokines and matrix metalloproteinases in the striatum and mesencephalon of mice injected with 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine, a dopaminergic neurotoxin. Neurosci. Lett. 349, 191-195. doi: 10.1016/S0304-3940(03)00832-2
    • (2003) Neurosci. Lett , vol.349 , pp. 191-195
    • Hebert, G.1    Arsaut, J.2    Dantzer, R.3    Demotes-Mainard, J.4
  • 60
    • 84873427263 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease
    • Hirsch, E. C., Jenner, P., and Przedborski, S. (2013). Pathogenesis of Parkinson's disease. Mov. Disord. 28, 24-30. doi: 10.1002/mds.25032
    • (2013) Mov. Disord , vol.28 , pp. 24-30
    • Hirsch, E.C.1    Jenner, P.2    Przedborski, S.3
  • 61
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides
    • Hofmann, M. A., Drury, S., Fu, C., Qu, W., Taguchi, A., Lu, Y., et al. (1999). RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97, 889-901. doi: 10.1016/S0092-8674(00)80801-6
    • (1999) Cell , vol.97 , pp. 889-901
    • Hofmann, M.A.1    Drury, S.2    Fu, C.3    Qu, W.4    Taguchi, A.5    Lu, Y.6
  • 62
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz, W. A., and O'Malley, K. L. (2003). Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J. Biol. Chem. 278, 19367-19377. doi: 10.1074/jbc. M211821200
    • (2003) J. Biol. Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 64
    • 58649095123 scopus 로고    scopus 로고
    • Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose
    • Hu, Y., Suarez, J., Fricovsky, E., Wang, H., Scott, B. T., Trauger, S. A., et al. (2009). Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J. Biol. Chem. 284, 547-555. doi: 10.1074/jbc. M808518200
    • (2009) J. Biol. Chem , vol.284 , pp. 547-555
    • Hu, Y.1    Suarez, J.2    Fricovsky, E.3    Wang, H.4    Scott, B.T.5    Trauger, S.A.6
  • 65
    • 0037064124 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation
    • Huttunen, H. J., Kuja-Panula, J., and Rauvala, H. (2002). Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation. J. Biol. Chem. 277, 38635-38646. doi: 10.1074/jbc. M202515200
    • (2002) J. Biol. Chem , vol.277 , pp. 38635-38646
    • Huttunen, H.J.1    Kuja-Panula, J.2    Rauvala, H.3
  • 66
    • 84924331603 scopus 로고    scopus 로고
    • Serum tri-and tetra-antennary N-glycan is a potential predictive biomarker for castration-resistant prostate cancer
    • Ishibashi, Y., Tobisawa, Y., Hatakeyama, S., Ohashi, T., Tanaka, M., Narita, S., et al. (2014). Serum tri-and tetra-antennary N-glycan is a potential predictive biomarker for castration-resistant prostate cancer. Prostate 74, 1521-1529. doi: 10.1002/pros.22869
    • (2014) Prostate , vol.74 , pp. 1521-1529
    • Ishibashi, Y.1    Tobisawa, Y.2    Hatakeyama, S.3    Ohashi, T.4    Tanaka, M.5    Narita, S.6
  • 67
    • 41149163183 scopus 로고    scopus 로고
    • Parkinson's disease: clinical features and diagnosis
    • Jankovic, J. (2008). Parkinson's disease: clinical features and diagnosis. J. Neurol. Neurosurg. Psychiatry 79, 368-376. doi: 10.1136/jnnp.2007.131045
    • (2008) J. Neurol. Neurosurg. Psychiatry , vol.79 , pp. 368-376
    • Jankovic, J.1
  • 68
    • 11144232015 scopus 로고    scopus 로고
    • Parkin increases dopamine uptake by enhancing the cell surface expression of dopamine transporter
    • Jiang, H., Jiang, Q., and Feng, J. (2004). Parkin increases dopamine uptake by enhancing the cell surface expression of dopamine transporter. J. Biol. Chem. 279, 54380-54386. doi: 10.1074/jbc. M409282200
    • (2004) J. Biol. Chem , vol.279 , pp. 54380-54386
    • Jiang, H.1    Jiang, Q.2    Feng, J.3
  • 69
    • 85010285616 scopus 로고    scopus 로고
    • Adult conditional knockout of PGC-1a leads to loss of dopamine neurons
    • Jiang, H., Kang, S. U., Zhang, S., Karuppagounder, S., Xu, J., Lee, Y. K., et al. (2016). Adult conditional knockout of PGC-1a leads to loss of dopamine neurons. eNeuro 3:ENEURO.0183-16.2016. doi: 10.1523/ENEURO.0183-16.2016
    • (2016) eNeuro , vol.3
    • Jiang, H.1    Kang, S.U.2    Zhang, S.3    Karuppagounder, S.4    Xu, J.5    Lee, Y.K.6
  • 70
    • 79959567198 scopus 로고    scopus 로고
    • Alternative splicing of RAGE: roles in biology and disease
    • Kalea, A. Z., Schmidt, A. M., and Hudson, B. I. (2011). Alternative splicing of RAGE: roles in biology and disease. Front. Biosci. 16, 2756-2770. doi: 10.2741/3884
    • (2011) Front. Biosci , vol.16 , pp. 2756-2770
    • Kalea, A.Z.1    Schmidt, A.M.2    Hudson, B.I.3
  • 71
    • 33645796173 scopus 로고    scopus 로고
    • Strategy for simulation of CID spectra of N-linked oligosaccharides toward glycomics
    • Kameyama, A., Nakaya, S., Ito, H., Kikuchi, N., Angata, T., Nakamura, M., et al. (2006). Strategy for simulation of CID spectra of N-linked oligosaccharides toward glycomics. J. Proteome Res. 5, 808-814. doi: 10.1021/pr0503937
    • (2006) J. Proteome Res , vol.5 , pp. 808-814
    • Kameyama, A.1    Nakaya, S.2    Ito, H.3    Kikuchi, N.4    Angata, T.5    Nakamura, M.6
  • 72
    • 84879101848 scopus 로고    scopus 로고
    • Identification of novel serum biomarkers of hepatocellular carcinoma using glycomic analysis
    • Kamiyama, T., Yokoo, H., Furukawa, J. I., Kurogochi, M., Togashi, T., Miura, N., et al. (2013). Identification of novel serum biomarkers of hepatocellular carcinoma using glycomic analysis. Hepatology 57, 2314-2325. doi: 10.1002/hep.26262
    • (2013) Hepatology , vol.57 , pp. 2314-2325
    • Kamiyama, T.1    Yokoo, H.2    Furukawa, J.I.3    Kurogochi, M.4    Togashi, T.5    Miura, N.6
  • 73
    • 84898757532 scopus 로고    scopus 로고
    • The role of innate and adaptive immunity in Parkinson's disease
    • Kannarkat, G. T., Boss, J. M., and Tansey, M. G. (2013). The role of innate and adaptive immunity in Parkinson's disease. J. Parkinsons Dis. 3, 493-514. doi: 10.3233/JPD-130250
    • (2013) J. Parkinsons Dis , vol.3 , pp. 493-514
    • Kannarkat, G.T.1    Boss, J.M.2    Tansey, M.G.3
  • 74
    • 79955066685 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • Keane, P. C., Kurzawa, M., Blain, P. G., and Morris, C. M. (2011). Mitochondrial dysfunction in Parkinson's disease. Parkinsons Dis. 2011:716871. doi: 10.4061/2011/716871
    • (2011) Parkinsons Dis , vol.2011
    • Keane, P.C.1    Kurzawa, M.2    Blain, P.G.3    Morris, C.M.4
  • 75
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney, P. M., Xie, J., Capaldi, R. A., and Bennett, J. P. (2006). Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 26, 5256-5264. doi: 10.1523/JNEUROSCI.0984-06.2006
    • (2006) J. Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett, J.P.4
  • 76
    • 80052615268 scopus 로고    scopus 로고
    • Extracellular HMGB1 released by NMDA treatment confers neuronal apoptosis via RAGE-p38 MAPK/ERK signaling pathway
    • Kim, S. W., Lim, C. M., Kim, J. B., Shin, J. H., Lee, S., Lee, M., et al. (2011). Extracellular HMGB1 released by NMDA treatment confers neuronal apoptosis via RAGE-p38 MAPK/ERK signaling pathway. Neurotoxicol. Res. 20, 159-169. doi: 10.1007/s12640-010-9231-x
    • (2011) Neurotoxicol. Res , vol.20 , pp. 159-169
    • Kim, S.W.1    Lim, C.M.2    Kim, J.B.3    Shin, J.H.4    Lee, S.5    Lee, M.6
  • 77
    • 0033615356 scopus 로고    scopus 로고
    • Nepsilon-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression
    • Kislinger, T., Fu, C., Huber, B., Qu, W., Taguchi, A., Du Yan, S., et al. (1999). Nepsilon-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J. Biol. Chem. 274, 31740-31749. doi: 10.1074/jbc.274.44.31740
    • (1999) J. Biol. Chem , vol.274 , pp. 31740-31749
    • Kislinger, T.1    Fu, C.2    Huber, B.3    Qu, W.4    Taguchi, A.5    Du Yan, S.6
  • 78
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., et al. (1998). Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605-608. doi: 10.1038/33416
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5    Minoshima, S.6
  • 81
    • 33646482095 scopus 로고    scopus 로고
    • Age-dependent changes of glyoxalase expression in human brain
    • Kuhla, B., Boeck, K., Luth, H. J., Schmidt, A., Weigle, B., Schmitz, M., et al. (2006). Age-dependent changes of glyoxalase expression in human brain. Neurobiol. Aging 27, 815-822. doi: 10.1016/j.neurobiolaging.2005.04.006
    • (2006) Neurobiol. Aging , vol.27 , pp. 815-822
    • Kuhla, B.1    Boeck, K.2    Luth, H.J.3    Schmidt, A.4    Weigle, B.5    Schmitz, M.6
  • 82
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • Kung, L. A., Tao, S. C., Qian, J., Smith, M. G., Snyder, M., and Zhu, H. (2009). Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes. Mol. Syst. Biol. 5:308. doi: 10.1038/msb.2009.64
    • (2009) Mol. Syst. Biol , vol.5 , pp. 308
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5    Zhu, H.6
  • 83
    • 79951581055 scopus 로고    scopus 로고
    • Alpha-synuclein deficiency leads to increased glyoxalase I expression and glycation stress
    • Kurz, A., Rabbani, N., Walter, M., Bonin, M., Thornalley, P., Auburger, G., et al. (2011). Alpha-synuclein deficiency leads to increased glyoxalase I expression and glycation stress. Cell. Mol. Life Sci. 68, 721-733. doi: 10.1007/s00018-010-0483-7
    • (2011) Cell. Mol. Life Sci , vol.68 , pp. 721-733
    • Kurz, A.1    Rabbani, N.2    Walter, M.3    Bonin, M.4    Thornalley, P.5    Auburger, G.6
  • 84
    • 84864021706 scopus 로고    scopus 로고
    • Human DJ-1 and its homologs are novel glyoxalases
    • Lee, J. Y., Song, J., Kwon, K., Jang, S., Kim, C., Baek, K., et al. (2012). Human DJ-1 and its homologs are novel glyoxalases. Hum. Mol. Genet. 21, 3215-3225. doi: 10.1093/hmg/dds155
    • (2012) Hum. Mol. Genet , vol.21 , pp. 3215-3225
    • Lee, J.Y.1    Song, J.2    Kwon, K.3    Jang, S.4    Kim, C.5    Baek, K.6
  • 85
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alpha synuclein: new targets for drug discovery
    • Lee, V. M., and Trojanowski, J. Q. (2006). Mechanisms of Parkinson's disease linked to pathological alpha synuclein: new targets for drug discovery. Neuron 52, 33-38. doi: 10.1016/j.neuron.2006.09.026
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 86
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • Leroy, E., Boyer, R., Auburger, G., Leube, B., Ulm, G., Mezey, E., et al. (1998). The ubiquitin pathway in Parkinson's disease. Nature 395, 451-452. doi: 10.1038/26652
    • (1998) Nature , vol.395 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3    Leube, B.4    Ulm, G.5    Mezey, E.6
  • 87
    • 0024336499 scopus 로고
    • Distribution of glycosyltransferase activities in different compartments of mitochondria
    • Levrat, C., Louisot, P., and Morelis, R. (1989). Distribution of glycosyltransferase activities in different compartments of mitochondria. Biochem. Int. 18, 813-823
    • (1989) Biochem. Int , vol.18 , pp. 813-823
    • Levrat, C.1    Louisot, P.2    Morelis, R.3
  • 88
    • 84862780458 scopus 로고    scopus 로고
    • Advanced glycation end products and neurodegenerative diseases: mechanisms and perspective
    • Li, J., Liu, D., Sun, L., Lu, Y., and Zhang, Z. (2012). Advanced glycation end products and neurodegenerative diseases: mechanisms and perspective. J. Neurol. Sci. 317, 1-5. doi: 10.1016/j.jns.2012.02.018
    • (2012) J. Neurol. Sci , vol.317 , pp. 1-5
    • Li, J.1    Liu, D.2    Sun, L.3    Lu, Y.4    Zhang, Z.5
  • 89
    • 2442637536 scopus 로고    scopus 로고
    • The role of N-glycosylation in function and surface trafficking of the human dopamine transporter
    • Li, L. B., Chen, N., Ramamoorthy, S., Chi, L., Cui, X. N., Wang, L. C., et al. (2004). The role of N-glycosylation in function and surface trafficking of the human dopamine transporter. J. Biol. Chem. 279, 21012-21020. doi: 10.1074/jbc. M311972200
    • (2004) J. Biol. Chem , vol.279 , pp. 21012-21020
    • Li, L.B.1    Chen, N.2    Ramamoorthy, S.3    Chi, L.4    Cui, X.N.5    Wang, L.C.6
  • 90
    • 84862764594 scopus 로고    scopus 로고
    • Microglial carbohydrate-binding receptors for neural repair
    • Linnartz, B., Bodea, L. G., and Neumann, H. (2012). Microglial carbohydrate-binding receptors for neural repair. Cell Tissue Res. 349, 215-227. doi: 10.1007/s00441-012-1342-7
    • (2012) Cell Tissue Res , vol.349 , pp. 215-227
    • Linnartz, B.1    Bodea, L.G.2    Neumann, H.3
  • 91
    • 84905500579 scopus 로고    scopus 로고
    • Siglec functions of microglia
    • Linnartz-Gerlach, B., Kopatz, J., and Neumann, H. (2014). Siglec functions of microglia. Glycobiology 24, 794-799. doi: 10.1093/glycob/cwu044
    • (2014) Glycobiology , vol.24 , pp. 794-799
    • Linnartz-Gerlach, B.1    Kopatz, J.2    Neumann, H.3
  • 92
    • 0016318795 scopus 로고
    • Glucose intolerance in Parkinson's disease
    • Lipman, I. J., Boykin, M. E., and Flora, R. E. (1974). Glucose intolerance in Parkinson's disease. J. Chronic Dis. 27, 573-579. doi: 10.1016/0021-9681(74)90031-9
    • (1974) J. Chronic Dis , vol.27 , pp. 573-579
    • Lipman, I.J.1    Boykin, M.E.2    Flora, R.E.3
  • 93
    • 84871606902 scopus 로고    scopus 로고
    • Therapeutic effects of rapamycin on MPTP-induced Parkinsonism in mice
    • Liu, K., Shi, N., Sun, Y., Zhang, T., and Sun, X. (2013). Therapeutic effects of rapamycin on MPTP-induced Parkinsonism in mice. Neurochem. Res. 38, 201-207. doi: 10.1007/s11064-012-0909-8
    • (2013) Neurochem. Res , vol.38 , pp. 201-207
    • Liu, K.1    Shi, N.2    Sun, Y.3    Zhang, T.4    Sun, X.5
  • 94
    • 84936871460 scopus 로고    scopus 로고
    • Structural and functional features of central nervous system lymphatic vessels
    • Louveau, A., Smirnov, I., Keyes, T. J., Eccles, J. D., Rouhani, S. J., Peske, J. D., et al. (2015). Structural and functional features of central nervous system lymphatic vessels. Nature 523, 337-341. doi: 10.1038/nature14432
    • (2015) Nature , vol.523 , pp. 337-341
    • Louveau, A.1    Smirnov, I.2    Keyes, T.J.3    Eccles, J.D.4    Rouhani, S.J.5    Peske, J.D.6
  • 95
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to Mammalian glycan function
    • Lowe, J. B., and Marth, J. D. (2003). A genetic approach to Mammalian glycan function. Annu. Rev. Biochem. 72, 643-691. doi: 10.1146/annurev.biochem.72.121801.161809
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 96
    • 84908160592 scopus 로고    scopus 로고
    • Diabetes and risk of Parkinson's disease: an updated meta-analysis of case control studies
    • Lu, L., Fu, D. L., Li, H. Q., Liu, A. J., Li, J. H., and Zheng, G. Q. (2014). Diabetes and risk of Parkinson's disease: an updated meta-analysis of case control studies. PLoS One 9:e85781. doi: 10.1371/journal.pone.0085781
    • (2014) PLoS One , vol.9
    • Lu, L.1    Fu, D.L.2    Li, H.Q.3    Liu, A.J.4    Li, J.H.5    Zheng, G.Q.6
  • 97
    • 84930081694 scopus 로고    scopus 로고
    • Effects of discontinuing a high-fat diet on mitochondrial proteins and 6-hydroxydopamine-induced dopamine depletion in rats
    • Ma, D., Shuler, J. M., Raider, K. D., Rogers, R. S., Wheatley, J. L., Geiger, P. C., et al. (2015). Effects of discontinuing a high-fat diet on mitochondrial proteins and 6-hydroxydopamine-induced dopamine depletion in rats. Brain Res. 1613, 49-58. doi: 10.1016/j.brainres.2015.03.053
    • (2015) Brain Res , vol.1613 , pp. 49-58
    • Ma, D.1    Shuler, J.M.2    Raider, K.D.3    Rogers, R.S.4    Wheatley, J.L.5    Geiger, P.C.6
  • 98
    • 84945131551 scopus 로고    scopus 로고
    • O-GlcNAc modification blocks the aggregation and toxicity of the protein a-synuclein associated with Parkinson's disease
    • Marotta, N. P., Lin, Y. H., Lewis, Y. E., Ambroso, M. R., Zaro, B. W., Roth, M. T., et al. (2015). O-GlcNAc modification blocks the aggregation and toxicity of the protein a-synuclein associated with Parkinson's disease. Nat. Chem. 7, 913-920. doi: 10.1038/nchem.2361
    • (2015) Nat. Chem , vol.7 , pp. 913-920
    • Marotta, N.P.1    Lin, Y.H.2    Lewis, Y.E.3    Ambroso, M.R.4    Zaro, B.W.5    Roth, M.T.6
  • 99
    • 84952985625 scopus 로고    scopus 로고
    • Evidence for a role of adaptive immune response in the disease pathogenesis of the MPTP mouse model of Parkinson's disease
    • Martin, H. L., Santoro, M., Mustafa, S., Riedel, G., Forrester, J. V., and Teismann, P. (2016). Evidence for a role of adaptive immune response in the disease pathogenesis of the MPTP mouse model of Parkinson's disease. Glia 64, 386-395. doi: 10.1002/glia.22935
    • (2016) Glia , vol.64 , pp. 386-395
    • Martin, H.L.1    Santoro, M.2    Mustafa, S.3    Riedel, G.4    Forrester, J.V.5    Teismann, P.6
  • 100
    • 79960361814 scopus 로고    scopus 로고
    • Recent advances in the genetics of Parkinson's disease
    • Martin, I., Dawson, V. L., and Dawson, T. M. (2011). Recent advances in the genetics of Parkinson's disease. Annu. Rev. Genomics Hum. Genet. 12, 301-325. doi: 10.1146/annurev-genom-082410-101440
    • (2011) Annu. Rev. Genomics Hum. Genet , vol.12 , pp. 301-325
    • Martin, I.1    Dawson, V.L.2    Dawson, T.M.3
  • 101
    • 33847022701 scopus 로고    scopus 로고
    • GM1 specifically interacts with a-synuclein and inhibits fibrillation
    • Martinez, Z., Zhu, M., Han, S., and Fink, A. L. (2007). GM1 specifically interacts with a-synuclein and inhibits fibrillation. Biochemistry 46, 1868-1877. doi: 10.1021/bi061749a
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 102
    • 84978437500 scopus 로고    scopus 로고
    • Parkinson's disease-related proteins PINK1 and parkin repress mitochondrial antigen presentation
    • Matheoud, D., Sugiura, A., Bellemare-Pelletier, A., Laplante, A., Rondeau, C., Chemali, M., et al. (2016). Parkinson's disease-related proteins PINK1 and parkin repress mitochondrial antigen presentation. Cell 166, 314-327. doi: 10.1016/j.cell.2016.05.039
    • (2016) Cell , vol.166 , pp. 314-327
    • Matheoud, D.1    Sugiura, A.2    Bellemare-Pelletier, A.3    Laplante, A.4    Rondeau, C.5    Chemali, M.6
  • 103
    • 79954435887 scopus 로고    scopus 로고
    • TNF: a key neuroinflammatory mediator of neurotoxicity and neurodegeneration in models of Parkinson's disease
    • McCoy, M. K., Ruhn, K. A., Blesch, A., and Tansey, M. G. (2011). TNF: a key neuroinflammatory mediator of neurotoxicity and neurodegeneration in models of Parkinson's disease. Adv. Exp. Med. Biol. 691, 539-540. doi: 10.1007/978-1-4419-6612-4_56
    • (2011) Adv. Exp. Med. Biol , vol.691 , pp. 539-540
    • McCoy, M.K.1    Ruhn, K.A.2    Blesch, A.3    Tansey, M.G.4
  • 104
    • 47349104402 scopus 로고    scopus 로고
    • Glial reactions in Parkinson's disease
    • McGeer, P. L., and McGeer, E. G. (2008). Glial reactions in Parkinson's disease. Mov. Disord. 23, 474-483. doi: 10.1002/mds.21751
    • (2008) Mov. Disord , vol.23 , pp. 474-483
    • McGeer, P.L.1    McGeer, E.G.2
  • 105
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K. S., and Jenner, P. (2001). Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297, 191-194. doi: 10.1016/S0304-3940(00)01701-8
    • (2001) Neurosci. Lett , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 106
    • 84929903016 scopus 로고    scopus 로고
    • Compromised autophagy and neurodegenerative diseases
    • Menzies, F. M., Fleming, A., and Rubinsztein, D. C. (2015). Compromised autophagy and neurodegenerative diseases. Nat. Rev. Neurosci. 16, 345-357. doi: 10.1038/nrn3961
    • (2015) Nat. Rev. Neurosci , vol.16 , pp. 345-357
    • Menzies, F.M.1    Fleming, A.2    Rubinsztein, D.C.3
  • 107
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinson's disease
    • Mercado, G., Valdés, P., and Hetz, C. (2013). An ERcentric view of Parkinson's disease. Trends Mol. Med. 19, 165-175. doi: 10.1016/j.molmed.2012.12.005
    • (2013) Trends Mol. Med , vol.19 , pp. 165-175
    • Mercado, G.1    Valdés, P.2    Hetz, C.3
  • 108
    • 84940462626 scopus 로고    scopus 로고
    • The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal
    • Mihoub, M., Abdallah, J., Gontero, B., Dairou, J., and Richarme, G. (2015). The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463, 1305-1310. doi: 10.1016/j.bbrc.2015.06.111
    • (2015) Biochem. Biophys. Res. Commun , vol.463 , pp. 1305-1310
    • Mihoub, M.1    Abdallah, J.2    Gontero, B.3    Dairou, J.4    Richarme, G.5
  • 109
    • 0024330311 scopus 로고
    • Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease
    • Mizuno, Y., Ohta, S., Tanaka, M., Takamiya, S., Suzuki, K., Sato, T., et al. (1989). Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease. Biochem. Biophys. Res. Commun. 163, 1450-1455. doi: 10.1016/0006-291X(89)91141-8
    • (1989) Biochem. Biophys. Res. Commun , vol.163 , pp. 1450-1455
    • Mizuno, Y.1    Ohta, S.2    Tanaka, M.3    Takamiya, S.4    Suzuki, K.5    Sato, T.6
  • 110
    • 0028171374 scopus 로고
    • Interleukin-1 beta, interleukin-6, epidermal growth factor and transforming growth factor-alpha are elevated in the brain from parkinsonian patients
    • Mogi, M., Harada, M., Kondo, T., Riederer, P., Inagaki, H., Minami, M., et al. (1994). Interleukin-1 beta, interleukin-6, epidermal growth factor and transforming growth factor-alpha are elevated in the brain from parkinsonian patients. Neurosci. Lett. 180, 147-150. doi: 10.1016/0304-3940(94)90508-8
    • (1994) Neurosci. Lett , vol.180 , pp. 147-150
    • Mogi, M.1    Harada, M.2    Kondo, T.3    Riederer, P.4    Inagaki, H.5    Minami, M.6
  • 111
    • 20744435383 scopus 로고    scopus 로고
    • Molecular pathophysiology of Parkinson's disease
    • Moore, D. J., West, A. B., Dawson, V. L., and Dawson, T. M. (2005). Molecular pathophysiology of Parkinson's disease. Annu. Rev. Neurosci. 28, 57-87. doi: 10.1146/annurev.neuro.28.061604.135718
    • (2005) Annu. Rev. Neurosci , vol.28 , pp. 57-87
    • Moore, D.J.1    West, A.B.2    Dawson, V.L.3    Dawson, T.M.4
  • 112
    • 84880172298 scopus 로고    scopus 로고
    • Cellular and molecular mediators of neuroinflammation in the pathogenesis of Parkinson's disease
    • More, S. V., Kumar, H., Kim, I. S., Song, S. Y., and Choi, D. K. (2013). Cellular and molecular mediators of neuroinflammation in the pathogenesis of Parkinson's disease. Med. Inflamm. 2013:952375. doi: 10.1155/2013/952375
    • (2013) Med. Inflamm , vol.2013
    • More, S.V.1    Kumar, H.2    Kim, I.S.3    Song, S.Y.4    Choi, D.K.5
  • 113
    • 85020310862 scopus 로고    scopus 로고
    • Nrf2 activation by tauroursodeoxycholic acid in experimental models of Parkinson's disease
    • Moreira, S., Fonseca, I., Nunes, M. J., Rosa, A., Lemos, L., Rodrigues, E., et al. (2017). Nrf2 activation by tauroursodeoxycholic acid in experimental models of Parkinson's disease. Exp. Neurol. 295, 77-87. doi: 10.1016/j.expneurol.2017.05.009
    • (2017) Exp. Neurol , vol.295 , pp. 77-87
    • Moreira, S.1    Fonseca, I.2    Nunes, M.J.3    Rosa, A.4    Lemos, L.5    Rodrigues, E.6
  • 115
    • 0034468706 scopus 로고    scopus 로고
    • Crosslinking of alpha synuclein by advanced glycation end products-an early pathophysiological step in Lewy body formation?
    • Münch, G., Lüth, H. J., Wong, A., Arendt, T., Hirsch, E., Ravid, R., et al. (2000). Crosslinking of alpha synuclein by advanced glycation end products-an early pathophysiological step in Lewy body formation? J. Chem. Neuroanat. 20, 253-257. doi: 10.1016/S0891-0618(00)00096-X
    • (2000) J. Chem. Neuroanat , vol.20 , pp. 253-257
    • Münch, G.1    Lüth, H.J.2    Wong, A.3    Arendt, T.4    Hirsch, E.5    Ravid, R.6
  • 116
    • 85018933386 scopus 로고    scopus 로고
    • NSAIDs ameliorate cognitive and motor impairment in a model of parkinsonism induced by chlorpromazine
    • Naeem, S., Ikram, R., Khan, S. S., and Rao, S. S. (2017). NSAIDs ameliorate cognitive and motor impairment in a model of parkinsonism induced by chlorpromazine. Pak. J. Pharm. Sci. 30, 801-808
    • (2017) Pak. J. Pharm. Sci , vol.30 , pp. 801-808
    • Naeem, S.1    Ikram, R.2    Khan, S.S.3    Rao, S.S.4
  • 117
    • 0035377458 scopus 로고    scopus 로고
    • Post-translational modifications of proteins: acetylcholinesterase as a model system
    • Nalivaeva, N. N., and Turner, A. J. (2001). Post-translational modifications of proteins: acetylcholinesterase as a model system. Proteomics 1, 735-747. doi: 10.1002/1615-9861(200106)1:6<735::AID-PROT735>3.0.CO;2-8
    • (2001) Proteomics , vol.1 , pp. 735-747
    • Nalivaeva, N.N.1    Turner, A.J.2
  • 118
    • 0026659883 scopus 로고
    • Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins
    • Neeper, M., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y. C., et al. (1992). Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J. Biol. Chem. 267, 14998-15004
    • (1992) J. Biol. Chem , vol.267 , pp. 14998-15004
    • Neeper, M.1    Schmidt, A.M.2    Brett, J.3    Yan, S.D.4    Wang, F.5    Pan, Y.C.6
  • 119
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani, V. M., Lu, W., Berge, V., Nakamura, K., Onoa, B., Lee, M. K., et al. (2010). Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65, 66-79. doi: 10.1016/j.neuron.2009.12.023
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6
  • 120
    • 0036715414 scopus 로고    scopus 로고
    • Apoptotic molecules and MPTP-induced cell death
    • Nicotra, A., and Parvez, S. H. (2002). Apoptotic molecules and MPTP-induced cell death. Neurotoxicol. Teratol. 24, 599-605. doi: 10.1016/S0892-0362(02)00213-1
    • (2002) Neurotoxicol. Teratol , vol.24 , pp. 599-605
    • Nicotra, A.1    Parvez, S.H.2
  • 121
    • 79960311716 scopus 로고    scopus 로고
    • Toward automated glycan analysis
    • Nishimura, S.-I. (2011). Toward automated glycan analysis. Adv. Carbohydr. Chem. Biochem. 65, 219-271. doi: 10.1016/B978-0-12-385520-6.00005-4
    • (2011) Adv. Carbohydr. Chem. Biochem , vol.65 , pp. 219-271
    • Nishimura, S.-I.1
  • 122
    • 84885038677 scopus 로고    scopus 로고
    • Clinical utility of high-throughput glycome analysis in patients with pancreatic cancer
    • Nouso, K., Amano, M., Miyahara, K., Ito, M. I., Morimoto, Y., Kato, H., et al. (2013). Clinical utility of high-throughput glycome analysis in patients with pancreatic cancer. J. Gastroenterol. 48, 1171-1179. doi: 10.1007/s00535-012-0732-7
    • (2013) J. Gastroenterol , vol.48 , pp. 1171-1179
    • Nouso, K.1    Amano, M.2    Miyahara, K.3    Ito, M.I.4    Morimoto, Y.5    Kato, H.6
  • 123
    • 77954104112 scopus 로고    scopus 로고
    • Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
    • Nuytemans, K., Theuns, J., Cruts, M., and Van Broeckhoven, C. (2010). Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update. Hum. Mutat. 31, 763-780. doi: 10.1002/humu.21277
    • (2010) Hum. Mutat , vol.31 , pp. 763-780
    • Nuytemans, K.1    Theuns, J.2    Cruts, M.3    Van Broeckhoven, C.4
  • 124
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo, K., and Marth, J. D. (2006). Glycosylation in cellular mechanisms of health and disease. Cell 126, 855-867. doi: 10.1016/j.cell.2006.08.019
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 126
    • 79955657305 scopus 로고    scopus 로고
    • Role of advanced glycation on aggregation and DNA binding properties of alpha-synuclein
    • Padmaraju, V., Bhaskar, J. J., Prasada Rao, U. J., Salimath, P. V., and Rao, K. S. (2011). Role of advanced glycation on aggregation and DNA binding properties of alpha-synuclein. J. Alzheimers Dis. 24, 211-221. doi: 10.3233/JAD-2011-101965
    • (2011) J. Alzheimers Dis , vol.24 , pp. 211-221
    • Padmaraju, V.1    Bhaskar, J.J.2    Prasada Rao, U.J.3    Salimath, P.V.4    Rao, K.S.5
  • 127
    • 84928181637 scopus 로고    scopus 로고
    • Disease associated mutations of TREM2 alter the processing of N-linked oligosaccharides in the golgi apparatus
    • Park, J. S., Ji, I. J., An, H. J., Kang, M. J., Kang, S. W., Kim, D. H., et al. (2015). Disease associated mutations of TREM2 alter the processing of N-linked oligosaccharides in the golgi apparatus. Traffic 16, 510-518. doi: 10.1111/tra.12264
    • (2015) Traffic , vol.16 , pp. 510-518
    • Park, J.S.1    Ji, I.J.2    An, H.J.3    Kang, M.J.4    Kang, S.W.5    Kim, D.H.6
  • 128
    • 33847681800 scopus 로고    scopus 로고
    • Temporal mRNA profiles of inflammatory mediators in the murine 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyrimidine model of Parkinson's disease
    • Pattarini, R., Smeyne, R. J., and Morgan, J. I. (2007). Temporal mRNA profiles of inflammatory mediators in the murine 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyrimidine model of Parkinson's disease. Neuroscience 145, 654-668. doi: 10.1016/j.neuroscience.2006.12.030
    • (2007) Neuroscience , vol.145 , pp. 654-668
    • Pattarini, R.1    Smeyne, R.J.2    Morgan, J.I.3
  • 129
    • 84903975888 scopus 로고    scopus 로고
    • Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
    • Pekkurnaz, G., Trinidad, J. C., Wang, X., Kong, D., and Schwarz, T. L. (2014). Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase. Cell 158, 54-68. doi: 10.1016/j.cell.2014.06.007
    • (2014) Cell , vol.158 , pp. 54-68
    • Pekkurnaz, G.1    Trinidad, J.C.2    Wang, X.3    Kong, D.4    Schwarz, T.L.5
  • 131
    • 85009727735 scopus 로고    scopus 로고
    • Evidence against a role for the Parkinsonism-associated protein DJ-1 in methylglyoxal detoxification
    • Pfaff, D. H., Fleming, T., Nawroth, P., and Teleman, A. A. (2017). Evidence against a role for the Parkinsonism-associated protein DJ-1 in methylglyoxal detoxification. J. Biol. Chem. 292, 685-690. doi: 10.1074/jbc. M116.743823
    • (2017) J. Biol. Chem , vol.292 , pp. 685-690
    • Pfaff, D.H.1    Fleming, T.2    Nawroth, P.3    Teleman, A.A.4
  • 133
    • 10244222286 scopus 로고    scopus 로고
    • MPTP as a mitochondrial neurotoxin model of Parkinson's disease
    • Przedborski, S., Tieu, K., Perier, C., and Vila, M. (2004). MPTP as a mitochondrial neurotoxin model of Parkinson's disease. J. Bioenerg. Biomembr. 36, 375-379. doi: 10.1023/B:JOBB.0000041771.66775.d5
    • (2004) J. Bioenerg. Biomembr , vol.36 , pp. 375-379
    • Przedborski, S.1    Tieu, K.2    Perier, C.3    Vila, M.4
  • 134
    • 53849092368 scopus 로고    scopus 로고
    • Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress
    • Rabbani, N., and Thornalley, P. J. (2008). Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress. Biochem. Soc. Trans. 36(Pt 5), 1045-1050. doi: 10.1042/BST0361045
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 1045-1050
    • Rabbani, N.1    Thornalley, P.J.2
  • 135
    • 84862688640 scopus 로고    scopus 로고
    • Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
    • Rabbani, N., and Thornalley, P. J. (2012). Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino Acids 42, 1133-1142. doi: 10.1007/s00726-010-0783-0
    • (2012) Amino Acids , vol.42 , pp. 1133-1142
    • Rabbani, N.1    Thornalley, P.J.2
  • 136
    • 84879113935 scopus 로고    scopus 로고
    • TREM2 in neurodegeneration: evidence for association of the p. R47H variant with frontotemporal dementia and Parkinson's disease
    • Rayaprolu, S., Mullen, B., Baker, M., Lynch, T., Finger, E., Seeley, W. W., et al. (2013). TREM2 in neurodegeneration: evidence for association of the p. R47H variant with frontotemporal dementia and Parkinson's disease. Mol. Neurodegener. 8:19. doi: 10.1186/1750-1326-8-19
    • (2013) Mol. Neurodegener , vol.8 , pp. 19
    • Rayaprolu, S.1    Mullen, B.2    Baker, M.3    Lynch, T.4    Finger, E.5    Seeley, W.W.6
  • 137
    • 84904968146 scopus 로고    scopus 로고
    • PINK-1 deficiency sustains cell proliferation by reprogramming glucose metabolism through HIF1
    • Requejo-Aguilar, R., Lopez-Fabuel, I., Fernandez, E., Martins, L. M., Almeida, A., and Bolaños, J. P. (2014). PINK-1 deficiency sustains cell proliferation by reprogramming glucose metabolism through HIF1. Nat. Commun. 24:4514. doi: 10.1038/ncomms5514
    • (2014) Nat. Commun , vol.24 , pp. 4514
    • Requejo-Aguilar, R.1    Lopez-Fabuel, I.2    Fernandez, E.3    Martins, L.M.4    Almeida, A.5    Bolaños, J.P.6
  • 139
    • 84922264295 scopus 로고    scopus 로고
    • Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal-and glyoxal-glycated cysteine, arginine, and lysine residues
    • Richarme, G., Mihoub, M., Dairou, J., Bui, L. C., Leger, T., and Lamouri, A. (2015). Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal-and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290, 1885-1897. doi: 10.1074/jbc. M114.597815
    • (2015) J. Biol. Chem , vol.290 , pp. 1885-1897
    • Richarme, G.1    Mihoub, M.2    Dairou, J.3    Bui, L.C.4    Leger, T.5    Lamouri, A.6
  • 140
    • 85045271175 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid improves motor symptoms in a mouse model of Parkinson's disease
    • [Epub ahead of print]
    • Rosa, A. I., Duarte-Silva, S., Silva-Fernandes, A., Nunes, M. J., Carvalho, A. N., Rodrigues, E., et al. (2018). Tauroursodeoxycholic acid improves motor symptoms in a mouse model of Parkinson's disease. Mol. Neurobiol. doi: 10.1007/s12035-018-1062-4 [Epub ahead of print]
    • (2018) Mol. Neurobiol
    • Rosa, A.I.1    Duarte-Silva, S.2    Silva-Fernandes, A.3    Nunes, M.J.4    Carvalho, A.N.5    Rodrigues, E.6
  • 141
    • 85021192126 scopus 로고    scopus 로고
    • Novel insights into the antioxidant role of tauroursodeoxycholic acid in experimental models of Parkinson's disease
    • Rosa, A. I., Fonseca, I., Nunes, M. J., Moreira, S., Rodrigues, E., Carvalho, A. N., et al. (2017). Novel insights into the antioxidant role of tauroursodeoxycholic acid in experimental models of Parkinson's disease. Biochim. Biophys. Acta 1863, 2171-2181. doi: 10.1016/j.bbadis.2017.06.004
    • (2017) Biochim. Biophys. Acta , vol.1863 , pp. 2171-2181
    • Rosa, A.I.1    Fonseca, I.2    Nunes, M.J.3    Moreira, S.4    Rodrigues, E.5    Carvalho, A.N.6
  • 142
    • 22344442393 scopus 로고    scopus 로고
    • Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation
    • Rosca, M. G., Mustata, T. G., Kinter, M. T., Ozdemir, A. M., Kern, T. S., Szweda, L. I., et al. (2005). Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation. Am. J. Physiol. Renal Physiol. 289, F420-F430. doi: 10.1152/ajprenal.00415.2004
    • (2005) Am. J. Physiol. Renal Physiol , vol.289 , pp. F420-F430
    • Rosca, M.G.1    Mustata, T.G.2    Kinter, M.T.3    Ozdemir, A.M.4    Kern, T.S.5    Szweda, L.I.6
  • 143
    • 84918804167 scopus 로고    scopus 로고
    • Diet induced obesity accelerates the onset of terminal phenotypes in alpha-synuclein transgenic mice
    • Rotermund, C., Truckenmuller, F. M., Schell, H., and Kahle, P. J. (2014). Diet induced obesity accelerates the onset of terminal phenotypes in alpha-synuclein transgenic mice. J. Neurochem. 31, 848-858. doi: 10.1111/jnc.12813
    • (2014) J. Neurochem , vol.31 , pp. 848-858
    • Rotermund, C.1    Truckenmuller, F.M.2    Schell, H.3    Kahle, P.J.4
  • 144
    • 85017294045 scopus 로고    scopus 로고
    • The N-glycosylation of immunoglobulin G as a novel biomarker of Parkinson's disease
    • Russell, A. C., Šimurina, M., Garcia, M. T., Novokmet, M., Wang, Y., Rudan, I., et al. (2017). The N-glycosylation of immunoglobulin G as a novel biomarker of Parkinson's disease. Glycobiology 27, 501-510. doi: 10.1093/glycob/cwx022
    • (2017) Glycobiology , vol.27 , pp. 501-510
    • Russell, A.C.1    Šimurina, M.2    Garcia, M.T.3    Novokmet, M.4    Wang, Y.5    Rudan, I.6
  • 145
    • 84907663355 scopus 로고    scopus 로고
    • The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach
    • Salahuddin, P., Rabbani, G., and Khan, R. H. (2014). The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach. Cell. Mol. Biol. Lett. 19, 407-437. doi: 10.2478/s11658-014-0205-5
    • (2014) Cell. Mol. Biol. Lett , vol.19 , pp. 407-437
    • Salahuddin, P.1    Rabbani, G.2    Khan, R.H.3
  • 146
    • 0027561888 scopus 로고
    • The relationship between diabetes mellitus and Parkinson's disease
    • Sandyk, R. (1993). The relationship between diabetes mellitus and Parkinson's disease. Int. J. Neurosci. 69, 125-130. doi: 10.3109/00207459309003322
    • (1993) Int. J. Neurosci , vol.69 , pp. 125-130
    • Sandyk, R.1
  • 147
    • 84955566351 scopus 로고    scopus 로고
    • Current challenges towards the development of a blood test for Parkinson's disease
    • Santiago, J. A., and Potashkin, J. A. (2014). Current challenges towards the development of a blood test for Parkinson's disease. Diagnostics 4, 153-164. doi: 10.3390/diagnostics4040153
    • (2014) Diagnostics , vol.4 , pp. 153-164
    • Santiago, J.A.1    Potashkin, J.A.2
  • 148
    • 84962520475 scopus 로고    scopus 로고
    • In-vivo evidence that high mobility group box 1 exerts deleterious effects in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine model and Parkinson's disease which can be attenuated by glycyrrhizin
    • Santoro, M., Maetzler, W., Stathakos, P., Martin, H. L., Hobert, M. A., Rattay, T. W., et al. (2016). In-vivo evidence that high mobility group box 1 exerts deleterious effects in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine model and Parkinson's disease which can be attenuated by glycyrrhizin. Neurobiol. Dis. 91, 59-68. doi: 10.1016/j.nbd.2016.02.018
    • (2016) Neurobiol. Dis , vol.91 , pp. 59-68
    • Santoro, M.1    Maetzler, W.2    Stathakos, P.3    Martin, H.L.4    Hobert, M.A.5    Rattay, T.W.6
  • 149
    • 84947798703 scopus 로고    scopus 로고
    • Anti-high mobility group box 1 antibody exerts neuroprotection in a rat model of Parkinson's disease
    • Sasaki, T., Liu, K., Agari, T., Yasuhara, T., Morimoto, J., Okazaki, M., et al. (2016). Anti-high mobility group box 1 antibody exerts neuroprotection in a rat model of Parkinson's disease. Exp. Neurol. 275, 220-231. doi: 10.1016/j.expneurol.2015.11.003
    • (2016) Exp. Neurol , vol.275 , pp. 220-231
    • Sasaki, T.1    Liu, K.2    Agari, T.3    Yasuhara, T.4    Morimoto, J.5    Okazaki, M.6
  • 150
    • 84870168829 scopus 로고    scopus 로고
    • S100B is increased in Parkinson's disease and ablation protects against MPTP induced toxicity through the RAGE and TNF-alpha pathway
    • Sathe, K., Maetzler, W., Lang, J. D., Mounsey, R. B., Fleckenstein, C., Martin, H. L., et al. (2012). S100B is increased in Parkinson's disease and ablation protects against MPTP induced toxicity through the RAGE and TNF-alpha pathway. Brain 135(Pt 11), 3336-3347. doi: 10.1093/brain/aws250
    • (2012) Brain , vol.135 , pp. 3336-3347
    • Sathe, K.1    Maetzler, W.2    Lang, J.D.3    Mounsey, R.B.4    Fleckenstein, C.5    Martin, H.L.6
  • 152
    • 0027960333 scopus 로고
    • Mitochondrial function and neurotoxicity
    • Schapira, A. H. (1994). Mitochondrial function and neurotoxicity. Curr. Opin. Neurol. 7, 531-534. doi: 10.1097/00019052-199412000-00010
    • (1994) Curr. Opin. Neurol , vol.7 , pp. 531-534
    • Schapira, A.H.1
  • 153
    • 84857969901 scopus 로고    scopus 로고
    • Targeting mitochondria for neuroprotection in Parkinson's disease
    • Schapira, A. H. (2012). Targeting mitochondria for neuroprotection in Parkinson's disease. Antioxid. Redox Signal. 16, 965-973. doi: 10.1089/ars.2011.4419
    • (2012) Antioxid. Redox Signal , vol.16 , pp. 965-973
    • Schapira, A.H.1
  • 154
  • 155
    • 0028981784 scopus 로고
    • GM1 ganglioside rescues substantia nigra pars compacta neurons and increases dopamine synthesis in residual nigrostriatal dopaminergic neurons in MPTP-treated mice
    • Schneider, J. S., Kean, A., and DiStefano, L. (1995). GM1 ganglioside rescues substantia nigra pars compacta neurons and increases dopamine synthesis in residual nigrostriatal dopaminergic neurons in MPTP-treated mice. J. Neurosci. Res. 42, 117-123. doi: 10.1002/jnr.490420113
    • (1995) J. Neurosci. Res , vol.42 , pp. 117-123
    • Schneider, J.S.1    Kean, A.2    DiStefano, L.3
  • 156
    • 0039267710 scopus 로고
    • Progression and prognosis in Parkinson's disease
    • Schwab, R. S. (1960). Progression and prognosis in Parkinson's disease. J. Nerv. Ment. Dis. 130, 556-566. doi: 10.1097/00005053-196006000-00017
    • (1960) J. Nerv. Ment. Dis , vol.130 , pp. 556-566
    • Schwab, R.S.1
  • 157
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease
    • Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., et al. (2001). Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293, 263-269. doi: 10.1126/science.1060627
    • (2001) Science , vol.293 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6
  • 158
    • 79952303794 scopus 로고    scopus 로고
    • PARIS (ZNF746) repression of PGC-1a contributes to neurodegeneration in Parkinson's disease
    • Shin, J. H., Ko, H. S., Kang, H., Lee, Y., Lee, Y. I., Pletinkova, O., et al. (2011). PARIS (ZNF746) repression of PGC-1a 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
  • 159
    • 85014489244 scopus 로고    scopus 로고
    • Sialic acid removal from dendritic cells improves antigen cross-presentation and boosts anti-tumor immune responses
    • Silva, M., Silva, Z., Marques, G., Ferro, T., Gonçalves, M., Monteiro, M., et al. (2016). Sialic acid removal from dendritic cells improves antigen cross-presentation and boosts anti-tumor immune responses. Oncotarget 7, 41053-41066. doi: 10.18632/oncotarget.9419
    • (2016) Oncotarget , vol.7 , pp. 41053-41066
    • Silva, M.1    Silva, Z.2    Marques, G.3    Ferro, T.4    Gonçalves, M.5    Monteiro, M.6
  • 160
    • 28244466782 scopus 로고    scopus 로고
    • CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism
    • Silva, R. M., Ries, V., Oo, T. F., Yarygina, O., Jackson, V., Ryu, E. J., et al. (2005). CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism. J. Neurochem. 95, 974-986. doi: 10.1111/j.1471-4159.2005.03428.x
    • (2005) J. Neurochem , vol.95 , pp. 974-986
    • Silva, R.M.1    Ries, V.2    Oo, T.F.3    Yarygina, O.4    Jackson, V.5    Ryu, E.J.6
  • 161
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri, L., Caputo, V., Bellacchio, E., Atorino, L., Dallapiccola, B., Valenteet, E. M., et al. (2005). Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum. Mol. Genet. 14, 3477-3492. doi: 10.1093/hmg/ddi377
    • (2005) Hum. Mol. Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3    Atorino, L.4    Dallapiccola, B.5    Valenteet, E.M.6
  • 162
    • 33644842309 scopus 로고    scopus 로고
    • Altered glycosylation of acetylcholinesterase in Creutzfeldt-Jakob disease
    • Silveyra, M. X., Cuadrado-Corrales, N., Marcos, A., Barquero, M. S., Rábano, A., Calero, M., et al. (2006). Altered glycosylation of acetylcholinesterase in Creutzfeldt-Jakob disease. J. Neurochem. 96, 97-104. doi: 10.1111/j.1471-4159.2005.03514.x
    • (2006) J. Neurochem , vol.96 , pp. 97-104
    • Silveyra, M.X.1    Cuadrado-Corrales, N.2    Marcos, A.3    Barquero, M.S.4    Rábano, A.5    Calero, M.6
  • 163
    • 84893826232 scopus 로고    scopus 로고
    • Formation of a salsolinol-like compound, the neurotoxin, 1-acetyl-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline, in a cellular model of hyperglycemia and a rat model of diabetes
    • Song, D. W., Xin, N., Xie, B. J., Li, Y. J., Meng, L. Y., Li, H. M., et al. (2014). Formation of a salsolinol-like compound, the neurotoxin, 1-acetyl-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline, in a cellular model of hyperglycemia and a rat model of diabetes. Int. J. Mol. Med. 33, 736-742. doi: 10.3892/ijmm.2013.1604
    • (2014) Int. J. Mol. Med , vol.33 , pp. 736-742
    • Song, D.W.1    Xin, N.2    Xie, B.J.3    Li, Y.J.4    Meng, L.Y.5    Li, H.M.6
  • 164
    • 84874322054 scopus 로고    scopus 로고
    • Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with parkinson disease in mammalian cells and drosophila
    • Song, S., Jang, S., Park, J., Bang, S., Choi, S., Kwon, K. Y., et al. (2013). Characterization of PINK1 (PTEN-induced putative kinase 1) mutations associated with parkinson disease in mammalian cells and drosophila. J. Biol. Chem. 288, 5660-5672. doi: 10.1074/jbc. M112.430801
    • (2013) J. Biol. Chem , vol.288 , pp. 5660-5672
    • Song, S.1    Jang, S.2    Park, J.3    Bang, S.4    Choi, S.5    Kwon, K.Y.6
  • 165
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R. G. (2002). Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12, 43R-56R. doi: 10.1093/glycob/12.4.43R
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 166
    • 2442496280 scopus 로고    scopus 로고
    • Induction of gp130-related cytokines and activation of JAK2/STAT3 pathway in astrocytes precedes up-regulation of glial fibrillary acidic protein in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine model of neurodegeneration: key signaling pathway for astrogliosis in vivo?
    • Sriram, K., Benkovic, S. A., Hebert, M. A., Miller, D. B., and O'Callaghan, J. P. (2004). Induction of gp130-related cytokines and activation of JAK2/STAT3 pathway in astrocytes precedes up-regulation of glial fibrillary acidic protein in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine model of neurodegeneration: key signaling pathway for astrogliosis in vivo? J. Biol. Chem. 279, 19936-19947. doi: 10.1074/jbc. M309304200
    • (2004) J. Biol. Chem , vol.279 , pp. 19936-19947
    • Sriram, K.1    Benkovic, S.A.2    Hebert, M.A.3    Miller, D.B.4    O'Callaghan, J.P.5
  • 167
    • 67649839223 scopus 로고    scopus 로고
    • 'N-Glycans, '
    • eds A. Varki, R. Cummings, and J. Esko (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Stanley, P., Schachter, H., Taniguchi, N., et al. (2009). "N-Glycans, "in Essentials of Glycobiology, 2nd Edn, eds A. Varki, R. Cummings, and J. Esko (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • (2009) Essentials of Glycobiology, 2nd Edn
    • Stanley, P.1    Schachter, H.2    Taniguchi, N.3
  • 168
    • 7944227203 scopus 로고    scopus 로고
    • Dopamine transporter: involvement in selective dopaminergic neurotoxicity and degeneration
    • Storch, A., Ludolph, A. C., and Schwarz, J. (2004). Dopamine transporter: involvement in selective dopaminergic neurotoxicity and degeneration. J. Neural Transm. 111, 1267-1286. doi: 10.1007/s00702-004-0203-2
    • (2004) J. Neural Transm , vol.111 , pp. 1267-1286
    • Storch, A.1    Ludolph, A.C.2    Schwarz, J.3
  • 169
    • 84909996967 scopus 로고    scopus 로고
    • Alpha synuclein is transported into and out of the brain by the blood-brain barrier
    • Sui, Y. T., Bullock, K. M., Erickson, M. A., Zhang, J., and Banks, W. A. (2014). Alpha synuclein is transported into and out of the brain by the blood-brain barrier. Peptides 62, 197-202. doi: 10.1016/j.peptides.2014.09.018
    • (2014) Peptides , vol.62 , pp. 197-202
    • Sui, Y.T.1    Bullock, K.M.2    Erickson, M.A.3    Zhang, J.4    Banks, W.A.5
  • 170
    • 85042640362 scopus 로고    scopus 로고
    • Blood-brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders
    • Sweeney, M. D., Sagare, A. P., and Zlokovic, B. V. (2018). Blood-brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders. Nat. Rev. Neurol. 14, 133-150. doi: 10.1038/nrneurol.2017.188
    • (2018) Nat. Rev. Neurol , vol.14 , pp. 133-150
    • Sweeney, M.D.1    Sagare, A.P.2    Zlokovic, B.V.3
  • 171
    • 84862288751 scopus 로고    scopus 로고
    • Microglial amyloid-ß 1-40 phagocytosis dysfunction is caused by high-mobility group box protein-1: implications for the pathological progression of Alzheimer's disease
    • Takata, K., Takada, T., Ito, A., Asai, M., Tawa, M., Saito, Y., et al. (2012). Microglial amyloid-ß 1-40 phagocytosis dysfunction is caused by high-mobility group box protein-1: implications for the pathological progression of Alzheimer's disease. Int. J. Alzheimers Dis. 2012:685739. doi: 10.1155/2012/685739
    • (2012) Int. J. Alzheimers Dis , vol.2012
    • Takata, K.1    Takada, T.2    Ito, A.3    Asai, M.4    Tawa, M.5    Saito, Y.6
  • 172
    • 0034682796 scopus 로고    scopus 로고
    • The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-alpha through nuclear factor kappa B, and by 17beta-estradiol through Sp-1 in human vascular endothelial cells
    • Tanaka, N., Yonekura, H., Yamagishi, S., Fujimori, H., Yamamoto, Y., and Yamamoto, H. (2000). The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-alpha through nuclear factor kappa B, and by 17beta-estradiol through Sp-1 in human vascular endothelial cells. J. Biol. Chem. 275, 25781-25790. doi: 10.1074/jbc. M001235200
    • (2000) J. Biol. Chem , vol.275 , pp. 25781-25790
    • Tanaka, N.1    Yonekura, H.2    Yamagishi, S.3    Fujimori, H.4    Yamamoto, Y.5    Yamamoto, H.6
  • 173
    • 84958106930 scopus 로고    scopus 로고
    • Differential roles of M1 and M2 microglia in neurodegenerative diseases
    • Tang, Y., and Le, W. (2016). Differential roles of M1 and M2 microglia in neurodegenerative diseases. Mol. Neurobiol. 53, 1181-1194. doi: 10.1007/s12035-014-9070-5
    • (2016) Mol. Neurobiol , vol.53 , pp. 1181-1194
    • Tang, Y.1    Le, W.2
  • 174
    • 84864379214 scopus 로고    scopus 로고
    • Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity
    • Teismann, P., Sathe, K., Bierhaus, A., Leng, L., Martin, H. L., Bucala, R., et al. (2012). Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity. Neurobiol. Aging 33, 2478-2490. doi: 10.1016/j.neurobiolaging.2011.12.006
    • (2012) Neurobiol. Aging , vol.33 , pp. 2478-2490
    • Teismann, P.1    Sathe, K.2    Bierhaus, A.3    Leng, L.4    Martin, H.L.5    Bucala, R.6
  • 175
    • 84986915900 scopus 로고    scopus 로고
    • Anti-Inflammatory modulation of microglia via CD163-targeted glucocorticoids protects dopaminergic neurons in the 6-OHDA Parkinson's disease model
    • Tentillier, N., Etzerodt, A., Olesen, M. N., Rizalar, F. S., Jacobsen, J., Bender, D., et al. (2016). Anti-Inflammatory modulation of microglia via CD163-targeted glucocorticoids protects dopaminergic neurons in the 6-OHDA Parkinson's disease model. J. Neurosci. 36, 9375-9390. doi: 10.1523/JNEUROSCI.1636-16.2016
    • (2016) J. Neurosci , vol.36 , pp. 9375-9390
    • Tentillier, N.1    Etzerodt, A.2    Olesen, M.N.3    Rizalar, F.S.4    Jacobsen, J.5    Bender, D.6
  • 176
    • 37349004102 scopus 로고    scopus 로고
    • Parkinson's disease
    • Thomas, B., and Beal, M. F. (2007). Parkinson's disease. Hum. Mol. Genet. 16, 183-194. doi: 10.1093/hmg/ddm159
    • (2007) Hum. Mol. Genet , vol.16 , pp. 183-194
    • Thomas, B.1    Beal, M.F.2
  • 177
    • 0027454552 scopus 로고
    • The glyoxalase system in health and disease
    • Thornalley, P. J. (1993). The glyoxalase system in health and disease. Mol. Aspects Med. 14, 287-371. doi: 10.1016/0098-2997(93)90002-U
    • (1993) Mol. Aspects Med , vol.14 , pp. 287-371
    • Thornalley, P.J.1
  • 178
    • 84920609361 scopus 로고    scopus 로고
    • Receptor for AGEs (RAGE) as mediator of NF-kB pathway activation in neuroinflammation and oxidative stress
    • Tóbon-Velasco, J. C., Cuevas, E., and Torres-Ramos, M. A. (2014). Receptor for AGEs (RAGE) as mediator of NF-kB pathway activation in neuroinflammation and oxidative stress. CNS Neurol. Disord. Drug Targets 13, 1615-1626. doi: 10.2174/1871527313666140806144831
    • (2014) CNS Neurol. Disord. Drug Targets , vol.13 , pp. 1615-1626
    • Tóbon-Velasco, J.C.1    Cuevas, E.2    Torres-Ramos, M.A.3
  • 179
    • 0037462827 scopus 로고    scopus 로고
    • Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter
    • Torres, G. E., Carneiro, A., Seamans, K., Fiorentini, C., Sweeney, A., Yao, W. D., et al. (2003). Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter. J. Biol. Chem. 278, 2731-2739. doi: 10.1074/jbc. M201926200
    • (2003) J. Biol. Chem , vol.278 , pp. 2731-2739
    • Torres, G.E.1    Carneiro, A.2    Seamans, K.3    Fiorentini, C.4    Sweeney, A.5    Yao, W.D.6
  • 180
    • 85028329332 scopus 로고    scopus 로고
    • Distinct metabolomic signature in cerebrospinal fluid in early Parkinson's disease
    • Trezzi, J. P., Galozzi, S., Jaeger, C., Barkovits, K., Brockmann, K., Maetzler, W., et al. (2017). Distinct metabolomic signature in cerebrospinal fluid in early Parkinson's disease. Mov. Disord. 32, 1401-1408. doi: 10.1002/mds.27132
    • (2017) Mov. Disord , vol.32 , pp. 1401-1408
    • Trezzi, J.P.1    Galozzi, S.2    Jaeger, C.3    Barkovits, K.4    Brockmann, K.5    Maetzler, W.6
  • 181
    • 84940094379 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum stress in Parkinson's disease
    • Tsujii, S., Ishisaka, M., and Hara, H. (2015). Modulation of endoplasmic reticulum stress in Parkinson's disease. Eur. J. Pharmacol. 765, 154-156. doi: 10.1016/j.ejphar.2015.08.033
    • (2015) Eur. J. Pharmacol , vol.765 , pp. 154-156
    • Tsujii, S.1    Ishisaka, M.2    Hara, H.3
  • 182
    • 85011299976 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • Tysnes, O. B., and Storstein, A. (2017). Epidemiology of Parkinson's disease. J. Neural Transm. 124, 901-905. doi: 10.1007/s00702-017-1686-y
    • (2017) J. Neural Transm , vol.124 , pp. 901-905
    • Tysnes, O.B.1    Storstein, A.2
  • 183
    • 84855830535 scopus 로고    scopus 로고
    • Glycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics)
    • Uchiki, T., Weikel, K. A., Jiao, W., Shang, F., Caceres, A., Pawlak, D., et al. (2012). Glycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics). Aging Cell 11, 1-13. doi: 10.1111/j.1474-9726.2011.00752.x
    • (2012) Aging Cell , vol.11 , pp. 1-13
    • Uchiki, T.1    Weikel, K.A.2    Jiao, W.3    Shang, F.4    Caceres, A.5    Pawlak, D.6
  • 184
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich, P., and Cerami, A. (2001). Protein glycation, diabetes, and aging. Recent Prog. Horm. Res. 56, 1-21. doi: 10.1210/rp.56.1.1
    • (2001) Recent Prog. Horm. Res , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 185
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk, Y., and Rabinovich, G. A. (2008). Protein-glycan interactions in the control of innate and adaptive immune responses. Nat. Immunol. 9, 593-601. doi: 10.1038/ni.f.203
    • (2008) Nat. Immunol , vol.9 , pp. 593-601
    • van Kooyk, Y.1    Rabinovich, G.A.2
  • 186
    • 84981172818 scopus 로고    scopus 로고
    • Regulation of striatal astrocytic receptor for advanced glycation end-products variants in an early stage of experimental Parkinson's disease
    • Viana, S. D., Valero, J., Rodrigues-Santos, P., Couceiro, P., Silva, A. M., Carvalho, F., et al. (2016). Regulation of striatal astrocytic receptor for advanced glycation end-products variants in an early stage of experimental Parkinson's disease. J. Neurochem. 138, 598-609. doi: 10.1111/jnc.13682
    • (2016) J. Neurochem , vol.138 , pp. 598-609
    • Viana, S.D.1    Valero, J.2    Rodrigues-Santos, P.3    Couceiro, P.4    Silva, A.M.5    Carvalho, F.6
  • 187
    • 84959455993 scopus 로고    scopus 로고
    • Glycation in Parkinson's disease and Alzheimer's disease
    • Vicente Miranda, H., El-Agnaf, O. M., and Outeiro, T. F. (2016). Glycation in Parkinson's disease and Alzheimer's disease. Mov. Disord. 31, 782-790. doi: 10.1002/mds.26566
    • (2016) Mov. Disord , vol.31 , pp. 782-790
    • Vicente Miranda, H.1    El-Agnaf, O.M.2    Outeiro, T.F.3
  • 188
    • 85019609948 scopus 로고    scopus 로고
    • Glycation potentiates a-synuclein-associated neurodegeneration in synucleinopathies
    • Vicente Miranda, H., Szego, éM., Oliveira, L. M., Breda, C., Darendelioglu, E., de Oliveira, R. M., et al. (2017). Glycation potentiates a-synuclein-associated neurodegeneration in synucleinopathies. Brain 140, 1399-1419. doi: 10.1093/brain/awx056
    • (2017) Brain , vol.140 , pp. 1399-1419
    • Vicente Miranda, H.1    Szego, É.M.2    Oliveira, L.M.3    Breda, C.4    Darendelioglu, E.5    de Oliveira, R.M.6
  • 189
    • 40949126559 scopus 로고    scopus 로고
    • Surface alpha 2-3-and alpha 2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis
    • Videira, P. A., Amado, I. F., Crespo, H. J., Algueró, M. C., Dall'Olio, F., Cabral, M. G., et al. (2008). Surface alpha 2-3-and alpha 2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis. Glycoconj. J. 25, 259-268. doi: 10.1007/s10719-007-9092-6
    • (2008) Glycoconj. J , vol.25 , pp. 259-268
    • Videira, P.A.1    Amado, I.F.2    Crespo, H.J.3    Algueró, M.C.4    Dall'Olio, F.5    Cabral, M.G.6
  • 190
    • 33645867671 scopus 로고    scopus 로고
    • Cyclooxygenase-2 mediates microglial activation and secondary dopaminergic cell death in the mouse MPTP model of Parkinson's disease
    • Vijitruth, R., Liu, M., Choi, D. Y., Nguyen, X. V., Hunter, R. L., and Bing, G. (2006). Cyclooxygenase-2 mediates microglial activation and secondary dopaminergic cell death in the mouse MPTP model of Parkinson's disease. J. Neuroinflammation 3:6
    • (2006) J. Neuroinflammation , vol.3 , pp. 6
    • Vijitruth, R.1    Liu, M.2    Choi, D.Y.3    Nguyen, X.V.4    Hunter, R.L.5    Bing, G.6
  • 191
    • 84859233375 scopus 로고    scopus 로고
    • Parkin-induced defects in neurophysiology and locomotion are generated by metabolic dysfunction and not oxidative stress
    • Vincent, A., Briggs, L., Chatwin, G. F. J., Emery, E., Tomlins, R., Oswald, M., et al. (2012). Parkin-induced defects in neurophysiology and locomotion are generated by metabolic dysfunction and not oxidative stress. Hum. Mol. Genet. 21, 1760-1769. doi: 10.1093/hmg/ddr609
    • (2012) Hum. Mol. Genet , vol.21 , pp. 1760-1769
    • Vincent, A.1    Briggs, L.2    Chatwin, G.F.J.3    Emery, E.4    Tomlins, R.5    Oswald, M.6
  • 192
    • 21644489744 scopus 로고    scopus 로고
    • Oxidative stress level in circulating neutrophils is linked to neurodegenerative diseases
    • Vitte, J., Michel, B. F., Bongrand, P., and Gastaut, J. L. (2004). Oxidative stress level in circulating neutrophils is linked to neurodegenerative diseases. J. Clin. Immunol. 24, 683-692. doi: 10.1007/s10875-004-6243-4
    • (2004) J. Clin. Immunol , vol.24 , pp. 683-692
    • Vitte, J.1    Michel, B.F.2    Bongrand, P.3    Gastaut, J.L.4
  • 193
    • 64249090462 scopus 로고    scopus 로고
    • Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells
    • Wang, H., Liu, J., and Wu, L. (2009). Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells. Biochem. Pharmacol. 77, 1709-1715. doi: 10.1016/j.bcp.2009.02.024
    • (2009) Biochem. Pharmacol , vol.77 , pp. 1709-1715
    • Wang, H.1    Liu, J.2    Wu, L.3
  • 194
    • 84991396164 scopus 로고    scopus 로고
    • A novel Parkinson's disease drug candidate with potent anti-neuroinflammatory effects through the Src signaling pathway
    • Wang, Y. D., Bao, X. Q., Xu, S., Yu, W. W., Cao, S. N., Hu, J. P., et al. (2016). A novel Parkinson's disease drug candidate with potent anti-neuroinflammatory effects through the Src signaling pathway. J. Med. Chem. 59, 9062-9079. doi: 10.1021/acs.jmedchem.6b00976
    • (2016) J. Med. Chem , vol.59 , pp. 9062-9079
    • Wang, Y.D.1    Bao, X.Q.2    Xu, S.3    Yu, W.W.4    Cao, S.N.5    Hu, J.P.6
  • 195
    • 84961199092 scopus 로고    scopus 로고
    • O-GlcNAcase deficiency suppresses skeletal myogenesis and insulin sensitivity in mice through the modulation of mitochondrial homeostasis
    • Wang, X., Feng, Z., Wang, X., Yang, L., Han, S., Cao, K., et al. (2016). O-GlcNAcase deficiency suppresses skeletal myogenesis and insulin sensitivity in mice through the modulation of mitochondrial homeostasis. Diabetologia 59, 1287-1296. doi: 10.1007/s00125-016-3919-2
    • (2016) Diabetologia , vol.59 , pp. 1287-1296
    • Wang, X.1    Feng, Z.2    Wang, X.3    Yang, L.4    Han, S.5    Cao, K.6
  • 196
    • 85024847491 scopus 로고    scopus 로고
    • O-GlcNAc regulation of autophagy and a-synuclein homeostasis; implications for Parkinson's disease
    • Wani, W. Y., Ouyang, X., Benavides, G. A., Redmann, M., Cofield, S. S., Shacka, J. J., et al. (2017). O-GlcNAc regulation of autophagy and a-synuclein homeostasis; implications for Parkinson's disease. Mol. Brain 10:32. doi: 10.1186/s13041-017-0311-1
    • (2017) Mol. Brain , vol.10 , pp. 32
    • Wani, W.Y.1    Ouyang, X.2    Benavides, G.A.3    Redmann, M.4    Cofield, S.S.5    Shacka, J.J.6
  • 197
    • 1542285483 scopus 로고    scopus 로고
    • Genetics of parkin-linked disease
    • West, A. B., and Maidment, N. T. (2004). Genetics of parkin-linked disease. Hum. Genet. 114, 327-336. doi: 10.1007/s00439-003-1074-6
    • (2004) Hum. Genet , vol.114 , pp. 327-336
    • West, A.B.1    Maidment, N.T.2
  • 198
    • 85024384526 scopus 로고    scopus 로고
    • Genome-wide pleiotropy between Parkinson disease and autoimmune diseases
    • Witoelar, A., Jansen, I. E., Wang, Y., Desikan, R. S., Gibbs, J. R., Blauwendraat, C., et al. (2017). Genome-wide pleiotropy between Parkinson disease and autoimmune diseases. JAMA Neurol. 74, 780-792. doi: 10.1001/jamaneurol.2017.0469
    • (2017) JAMA Neurol , vol.74 , pp. 780-792
    • Witoelar, A.1    Jansen, I.E.2    Wang, Y.3    Desikan, R.S.4    Gibbs, J.R.5    Blauwendraat, C.6
  • 199
    • 85027948203 scopus 로고    scopus 로고
    • Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's disease
    • Wong, A. S., Lee, R. H., Cheung, A. Y., Yeung, P. K., Chung, S. K., Cheung, Z. H., et al. (2011). Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's disease. Nat. Cell Biol. 13, 568-579. doi: 10.1038/ncb2217
    • (2011) Nat. Cell Biol , vol.13 , pp. 568-579
    • Wong, A.S.1    Lee, R.H.2    Cheung, A.Y.3    Yeung, P.K.4    Chung, S.K.5    Cheung, Z.H.6
  • 200
    • 0036522967 scopus 로고    scopus 로고
    • Blockade of microglial activation is neuroprotective in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine mouse model of Parkinson disease
    • Wu, D. C., Jackson-Lewis, V., Vila, M., Tieu, K., Teismann, P., Vadseth, C., et al. (2002). Blockade of microglial activation is neuroprotective in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine mouse model of Parkinson disease. J. Neurosci. 22, 1763-1771. doi: 10.1523/JNEUROSCI.22-05-01763.2002
    • (2002) J. Neurosci , vol.22 , pp. 1763-1771
    • Wu, D.C.1    Jackson-Lewis, V.2    Vila, M.3    Tieu, K.4    Teismann, P.5    Vadseth, C.6
  • 201
    • 80755189053 scopus 로고    scopus 로고
    • Mice lacking major brain gangliosides develop parkinsonism
    • Wu, G., Lu, Z. H., Kulkarni, N., Amin, R., and Ledeen, R. W. (2011). Mice lacking major brain gangliosides develop parkinsonism. Neurochem. Res. 36, 1706-1714. doi: 10.1007/s11064-011-0437-y
    • (2011) Neurochem. Res , vol.36 , pp. 1706-1714
    • Wu, G.1    Lu, Z.H.2    Kulkarni, N.3    Amin, R.4    Ledeen, R.W.5
  • 202
    • 84875088471 scopus 로고    scopus 로고
    • Glycoform-selective prion formation in sporadic and familial forms of prion disease
    • Xiao, X., Yuan, J., Haïk, S., Cali, I., Zhan, Y., Moudjou, M., et al. (2013). Glycoform-selective prion formation in sporadic and familial forms of prion disease. PLoS One 8:e58786. doi: 10.1371/journal.pone.0058786
    • (2013) PLoS One , vol.8
    • Xiao, X.1    Yuan, J.2    Haïk, S.3    Cali, I.4    Zhan, Y.5    Moudjou, M.6
  • 203
    • 84931331883 scopus 로고    scopus 로고
    • A newly discovered neurotoxin ADTIQ associated with hyperglycemia and Parkinson's disease
    • Xie, B., Lin, F., Ullah, K., Peng, L., Ding, W., Dai, R., et al. (2015). A newly discovered neurotoxin ADTIQ associated with hyperglycemia and Parkinson's disease. Biochem. Biophys. Res. Commun. 459, 361-366. doi: 10.1016/j.bbrc.2015.02.069
    • (2015) Biochem. Biophys. Res. Commun , vol.459 , pp. 361-366
    • Xie, B.1    Lin, F.2    Ullah, K.3    Peng, L.4    Ding, W.5    Dai, R.6
  • 204
    • 84975230355 scopus 로고    scopus 로고
    • Plasma levels of soluble receptor for advanced glycation end products in Alzheimer's disease
    • Xu, X. Y., Deng, C. Q., Wang, J., Deng, X. J., Xiao, Q., Li, Y., et al. (2017). Plasma levels of soluble receptor for advanced glycation end products in Alzheimer's disease. Int. J. Neurosci. 127, 454-458. doi: 10.1080/00207454.2016.1193861
    • (2017) Int. J. Neurosci , vol.127 , pp. 454-458
    • Xu, X.Y.1    Deng, C.Q.2    Wang, J.3    Deng, X.J.4    Xiao, Q.5    Li, Y.6
  • 205
    • 77954889408 scopus 로고    scopus 로고
    • Advanced glycation end product (AGE)-receptor for AGE (RAGE) signaling and up-regulation of Egr-1 in hypoxic macrophages
    • Xu, Y., Toure, F., Qu, W., Lin, L., Song, F., Shen, X., et al. (2010). Advanced glycation end product (AGE)-receptor for AGE (RAGE) signaling and up-regulation of Egr-1 in hypoxic macrophages. J. Biol. Chem. 285, 23233-23240. doi: 10.1074/jbc. M110.117457
    • (2010) J. Biol. Chem , vol.285 , pp. 23233-23240
    • Xu, Y.1    Toure, F.2    Qu, W.3    Lin, L.4    Song, F.5    Shen, X.6
  • 206
    • 84858307371 scopus 로고    scopus 로고
    • Transcriptional control of glyoxalase 1 by Nrf2 provides a stress-responsive defence against dicarbonyl glycation
    • Xue, M., Rabbani, N., Momiji, H., Imbasi, P., Anwar, M. M., Kitteringham, N., et al. (2012). Transcriptional control of glyoxalase 1 by Nrf2 provides a stress-responsive defence against dicarbonyl glycation. Biochem. J. 443, 213-222. doi: 10.1042/BJ20111648
    • (2012) Biochem. J , vol.443 , pp. 213-222
    • Xue, M.1    Rabbani, N.2    Momiji, H.3    Imbasi, P.4    Anwar, M.M.5    Kitteringham, N.6
  • 207
    • 84945940465 scopus 로고    scopus 로고
    • Advanced glycation end products: a molecular target for vascular complications in diabetes
    • Yamagishi, S., Nakamura, N., Suematsu, M., Kaseda, K., and Matsui, T. (2015). Advanced glycation end products: a molecular target for vascular complications in diabetes. Mol. Med. 21(Suppl. 1), S32-S40. doi: 10.2119/molmed.2015.00067
    • (2015) Mol. Med , vol.21 , pp. S32-S40
    • Yamagishi, S.1    Nakamura, N.2    Suematsu, M.3    Kaseda, K.4    Matsui, T.5
  • 208
    • 77649186801 scopus 로고    scopus 로고
    • Soluble RAGE: therapy and biomarker in unraveling the RAGE axis in chronic disease and aging
    • Yan, S. F., Ramasamy, R., and Schmidt, A. M. (2010). Soluble RAGE: therapy and biomarker in unraveling the RAGE axis in chronic disease and aging. Biochem. Pharmacol. 79, 1379-1386. doi: 10.1016/j.bcp.2010.01.013
    • (2010) Biochem. Pharmacol , vol.79 , pp. 1379-1386
    • Yan, S.F.1    Ramasamy, R.2    Schmidt, A.M.3
  • 209
    • 0026544129 scopus 로고
    • Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease
    • Yoshino, H., Nakagawa-Hattori, Y., Kondo, T., and Mizuno, Y. (1992). Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease. J. Neural Transm. Park. Dis. Dement. Sect. 4, 27-34. doi: 10.1007/BF02257619
    • (1992) J. Neural Transm. Park. Dis. Dement. Sect , vol.4 , pp. 27-34
    • Yoshino, H.1    Nakagawa-Hattori, Y.2    Kondo, T.3    Mizuno, Y.4
  • 210
    • 84902186248 scopus 로고    scopus 로고
    • Aging leads to elevation of O-GlcNAcylation and disruption of mitochondrial homeostasis in retina
    • Zhao, L., Feng, Z., Zou, X., Cao, K., Xu, J., and Liu, J. (2014). Aging leads to elevation of O-GlcNAcylation and disruption of mitochondrial homeostasis in retina. Oxid. Med. Cell. Longev. 2014:425705. doi: 10.1155/2014/425705
    • (2014) Oxid. Med. Cell. Longev , vol.2014
    • Zhao, L.1    Feng, Z.2    Zou, X.3    Cao, K.4    Xu, J.5    Liu, J.6
  • 211
    • 77958072667 scopus 로고    scopus 로고
    • PGC-1a, a potential therapeutic target for early intervention in Parkinson's disease
    • Zheng, B., Liao, Z., Locascio, J. J., Lesniak, K. A., Roderick, S. S., Watt, M. L., et al. (2010). PGC-1a, a potential therapeutic target for early intervention in Parkinson's disease. Sci. Transl. Med. 2:52ra73. doi: 10.1126/scitranslmed.3001059
    • (2010) Sci. Transl. Med , vol.2
    • Zheng, B.1    Liao, Z.2    Locascio, J.J.3    Lesniak, K.A.4    Roderick, S.S.5    Watt, M.L.6
  • 212
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • Zhu, J. H., Horbinski, C., Guo, F., Watkins, S., Uchiyama, Y., and Chu, C. T. (2007). Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am. J. Pathol. 170, 75-86. doi: 10.2353/ajpath.2007.060524
    • (2007) Am. J. Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6
  • 213
    • 85084753062 scopus 로고    scopus 로고
    • The range and nature of non-motor symptoms in drug-naive Parkinson's disease patients: a state-of-the-art systematic review
    • Zis, P., Erro, R., Walton, C. C., Sauerbier, A., and Chaudhuri, K. R. (2015). The range and nature of non-motor symptoms in drug-naive Parkinson's disease patients: a state-of-the-art systematic review. NPJ Parkinsons Dis. 1:15013. doi: 10.1038/npjparkd.2015.13
    • (2015) NPJ Parkinsons Dis , vol.1 , pp. 15013
    • Zis, P.1    Erro, R.2    Walton, C.C.3    Sauerbier, A.4    Chaudhuri, K.R.5


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