메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Protein clearance mechanisms of alpha-synuclein and amyloid-beta in Lewy body disorders

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN;

EID: 84869039156     PISSN: None     EISSN: 20900252     Source Type: Journal    
DOI: 10.1155/2012/391438     Document Type: Review
Times cited : (37)

References (134)
  • 1
    • 36949031267 scopus 로고    scopus 로고
    • α-Synucleinopathy models and human neuropathology: Similarities and differences
    • DOI 10.1007/s00401-007-0302-x
    • Kahle P. J., α -Synucleinopathy models and human neuropathology: similarities and differences. Acta Neuropathologica 2008 115 1 87 95 2-s2.0-36949031267 10.1007/s00401-007-0302-x (Pubitemid 350238669)
    • (2008) Acta Neuropathologica , vol.115 , Issue.1 , pp. 87-95
    • Kahle, P.J.1
  • 2
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: Insights from genetic studies
    • 2-s2.0-69149089036 10.1017/S1462399409001148
    • Gasser T., Molecular pathogenesis of Parkinson disease: insights from genetic studies. Expert Reviews in Molecular Medicine 2009 11, article e22 2-s2.0-69149089036 10.1017/S1462399409001148
    • (2009) Expert Reviews in Molecular Medicine , vol.1122
    • Gasser, T.1
  • 6
    • 0032937059 scopus 로고    scopus 로고
    • Diagnostic criteria for Parkinson disease
    • DOI 10.1001/archneur.56.1.33
    • Gelb D. J., Oliver E., Gilman S., Diagnostic criteria for Parkinson disease. Archives of Neurology 1999 56 1 33 39 2-s2.0-0032937059 10.1001/archneur.56.1.33 (Pubitemid 29046907)
    • (1999) Archives of Neurology , vol.56 , Issue.1 , pp. 33-39
    • Gelb, D.J.1    Oliver, E.2    Gilman, S.3
  • 10
    • 0018897531 scopus 로고
    • Parkinson disease, dementia, and Alzheimer disease: Clinicopathological correlations
    • Boller F., Mizutani T., Roessmann U., Gambetti P., Parkinson disease, dementia, and Alzheimer disease: clinicopathological correlations. Annals of Neurology 1980 7 4 329 335 2-s2.0-0018897531 (Pubitemid 10112826)
    • (1980) Annals of Neurology , vol.7 , Issue.4 , pp. 329-335
    • Boller, F.1    Mizutani, T.2    Roessmann, U.3    Gambetti, P.4
  • 11
    • 17644426053 scopus 로고    scopus 로고
    • Cognitive status correlates with neuropathologic stage in Parkinson disease
    • Braak H., Rüb U., Jansen Steur E. N. H., Del Tredici K., de Vos R. A. I., Cognitive status correlates with neuropathologic stage in Parkinson disease. Neurology 2005 64 8 1404 1410 2-s2.0-17644426053 (Pubitemid 40570509)
    • (2005) Neurology , vol.64 , Issue.8 , pp. 1404-1410
    • Braak, H.1    Rub, U.2    Jansen Steur, E.N.H.3    Del Tredici, K.4    De Vos, R.A.I.5
  • 12
    • 0027465936 scopus 로고
    • A clinicopathologic study of 100 cases of Parkinson's disease
    • Hughes A. J., Daniel S. E., Blankson S., Lees A. J., A clinicopathologic study of 100 cases of Parkinson's disease. Archives of Neurology 1993 50 2 140 148 2-s2.0-0027465936 (Pubitemid 23054795)
    • (1993) Archives of Neurology , vol.50 , Issue.2 , pp. 140-148
    • Hughes, A.J.1    Daniel, S.E.2    Blankson, S.3    Lees, A.J.4
  • 13
    • 71849104690 scopus 로고    scopus 로고
    • Progression of Parkinson's disease in the clinical phase: Potential markers
    • 2-s2.0-71849104690 10.1016/S1474-4422(09)70291-1
    • Maetzler W., Liepelt I., Berg D., Progression of Parkinson's disease in the clinical phase: potential markers. The Lancet Neurology 2009 8 12 1158 1171 2-s2.0-71849104690 10.1016/S1474-4422(09)70291-1
    • (2009) The Lancet Neurology , vol.8 , Issue.12 , pp. 1158-1171
    • Maetzler, W.1    Liepelt, I.2    Berg, D.3
  • 14
    • 33845709899 scopus 로고    scopus 로고
    • Differences in neuropathologic characteristics across the Lewy body dementia spectrum
    • DOI 10.1212/01.wnl.0000249130.63615.cc, PII 0000611420061212000009
    • Ballard C., Ziabreva I., Perry R., Larsen J. P., O'Brien J., McKeith I., Perry E., Aarsland D., Differences in neuropathologic characteristics across the Lewy body dementia spectrum. Neurology 2006 67 11 1931 1934 2-s2.0-33845709899 10.1212/01.wnl.0000249130.63615.cc (Pubitemid 44967366)
    • (2006) Neurology , vol.67 , Issue.11 , pp. 1931-1934
    • Ballard, C.1    Ziabreva, I.2    Perry, R.3    Larsen, J.P.4    O'Brien, J.5    McKeith, I.6    Perry, E.7    Aarsland, D.8
  • 15
    • 72849109343 scopus 로고    scopus 로고
    • Imaging amyloid in Parkinson's disease dementia and dementia with Lewy bodies with positron emission tomography
    • 2-s2.0-72849109343 10.1002/mds.22581
    • Brooks D. J., Imaging amyloid in Parkinson's disease dementia and dementia with Lewy bodies with positron emission tomography. Movement Disorders 2009 24 supplement 2 S742 S747 2-s2.0-72849109343 10.1002/mds.22581
    • (2009) Movement Disorders , vol.24 , Issue.SUPPLEMENT 2
    • Brooks, D.J.1
  • 17
    • 84857633703 scopus 로고    scopus 로고
    • Biomarker candidates of neurodegeneration in Parkinson's disease for the evaluation of disease-modifying therapeutics
    • 2-s2.0-79960183832 10.1007/s00702-011-0682-x
    • Gerlach M., Maetzler W., Broich K., Hampel H., Rems L., Reum T., Riederer P., Stöffler A., Streffer J., Berg D., Biomarker candidates of neurodegeneration in Parkinson's disease for the evaluation of disease-modifying therapeutics. Journal of Neural Transmission 2012 119 1 39 52 2-s2.0-79960183832 10.1007/s00702-011-0682-x
    • (2012) Journal of Neural Transmission , vol.119 , Issue.1 , pp. 39-52
    • Gerlach, M.1    Maetzler, W.2    Broich, K.3    Hampel, H.4    Rems, L.5    Reum, T.6    Riederer, P.7    Stöffler, A.8    Streffer, J.9    Berg, D.10
  • 18
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • DOI 10.1146/annurev.biochem.67.1.425
    • Hershko A., Ciechanover A., The ubiquitin system. Annual Review of Biochemistry 1998 67 425 479 2-s2.0-0031657807 10.1146/annurev.biochem.67.1.425 (Pubitemid 28411135)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 19
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • DOI 10.1146/annurev.med.50.1.57
    • Schwartz A. L., Ciechanover A., The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annual Review of Medicine 1999 50 57 74 2-s2.0-0033016291 10.1146/annurev.med.50.1.57 (Pubitemid 29117052)
    • (1999) Annual Review of Medicine , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 20
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • DOI 10.1016/S0896-6273(03)00606-8
    • Ciechanover A., Brundin P., The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003 40 2 427 446 2-s2.0-0141987860 10.1016/S0896-6273(03)00606-8 (Pubitemid 37244106)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 21
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • DOI 10.1016/j.tcb.2003.12.002
    • Cuervo A. M., Autophagy: in sickness and in health. Trends in Cell Biology 2004 14 2 70 77 2-s2.0-0442323561 10.1016/j.tcb.2003.12.002 (Pubitemid 38186640)
    • (2004) Trends in Cell Biology , vol.14 , Issue.2 , pp. 70-77
    • Cuervo, A.M.1
  • 22
    • 23344446037 scopus 로고    scopus 로고
    • Autophagy
    • 2-s2.0-23344446037
    • Klionsky D. J., Autophagy. Current Biology 2005 15 8 R282 R283 2-s2.0-23344446037
    • (2005) Current Biology , vol.15 , Issue.8
    • Klionsky, D.J.1
  • 23
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • DOI 10.1101/gad.1599207
    • Mizushima N., Autophagy: process and function. Genes and Development 2007 21 22 2861 2873 2-s2.0-36249025723 10.1101/gad.1599207 (Pubitemid 350133435)
    • (2007) Genes and Development , vol.21 , Issue.22 , pp. 2861-2873
    • Mizushima, N.1
  • 24
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: when the cleaning crew goes on strike
    • DOI 10.1016/S1474-4422(07)70076-5, PII S1474442207700765
    • Martinez-Vicente M., Cuervo A. M., Autophagy and neurodegeneration: when the cleaning crew goes on strike. The Lancet Neurology 2007 6 4 352 361 2-s2.0-33847652900 10.1016/S1474-4422(07)70076-5 (Pubitemid 46367949)
    • (2007) Lancet Neurology , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 25
    • 18144453796 scopus 로고    scopus 로고
    • Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer's disease
    • DOI 10.1006/exnr.1997.6738
    • Dewitt D. A., Perry G., Cohen M., Doller C., Silver J., Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer's disease. Experimental Neurology 1998 149 2 329 340 2-s2.0-18144453796 10.1006/exnr.1997.6738 (Pubitemid 28115071)
    • (1998) Experimental Neurology , vol.149 , Issue.2 , pp. 329-340
    • Dewitt, D.A.1    Perry, G.2    Cohen, M.3    Doller, C.4    Silver, J.5
  • 26
    • 77956955758 scopus 로고    scopus 로고
    • The role of microglia in amyloid clearance from the AD brain
    • 2-s2.0-77956955758 10.1007/s00702-010-0433-4
    • Lee C. Y. D., Landreth G. E., The role of microglia in amyloid clearance from the AD brain. Journal of Neural Transmission 2010 117 8 949 960 2-s2.0-77956955758 10.1007/s00702-010-0433-4
    • (2010) Journal of Neural Transmission , vol.117 , Issue.8 , pp. 949-960
    • Lee, C.Y.D.1    Landreth, G.E.2
  • 28
    • 77955604553 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal A β 42 uptake and lysosomal trafficking
    • 2-s2.0-77955604553 10.1371/journal.pone.0011884 e11884
    • Fuentealba R. A., Liu Q., Zhang J., Kanekiyo T., Hu X., Lee J. M., Ladu M. J., Bu G., Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal A β 42 uptake and lysosomal trafficking. PLoS ONE 2010 5 7 2-s2.0-77955604553 10.1371/journal.pone.0011884 e11884
    • (2010) PLoS ONE , vol.5 , Issue.7
    • Fuentealba, R.A.1    Liu, Q.2    Zhang, J.3    Kanekiyo, T.4    Hu, X.5    Lee, J.M.6    Ladu, M.J.7    Bu, G.8
  • 29
    • 42249115877 scopus 로고    scopus 로고
    • Neuroinflammation mediated by IL-1β increases susceptibility of dopamine neurons to degeneration in an animal model of Parkinson's disease
    • DOI 10.1186/1742-2094-5-8
    • Koprich J. B., Reske-Nielsen C., Mithal P., Isacson O., Neuroinflammation mediated by IL-1 β increases susceptibility of dopamine neurons to degeneration in an animal model of Parkinson's disease. Journal of Neuroinflammation 2008 5, article 8 2-s2.0-42249115877 10.1186/1742-2094-5-8 (Pubitemid 351546594)
    • (2008) Journal of Neuroinflammation , vol.5 , pp. 8
    • Koprich, J.B.1    Reske-Nielsen, C.2    Mithal, P.3    Isacson, O.4
  • 30
    • 78649745833 scopus 로고    scopus 로고
    • The toll-like receptor-3 agonist polyinosinic:polycytidylic acid triggers nigrostriatal dopaminergic degeneration
    • 2-s2.0-78649745833 10.1523/JNEUROSCI.2400-10.2010
    • Deleidi M., Hallett P. J., Koprich J. B., Chung C. Y., Isacson O., The toll-like receptor-3 agonist polyinosinic:polycytidylic acid triggers nigrostriatal dopaminergic degeneration. Journal of Neuroscience 2010 30 48 16091 16101 2-s2.0-78649745833 10.1523/JNEUROSCI.2400-10.2010
    • (2010) Journal of Neuroscience , vol.30 , Issue.48 , pp. 16091-16101
    • Deleidi, M.1    Hallett, P.J.2    Koprich, J.B.3    Chung, C.Y.4    Isacson, O.5
  • 32
    • 0036085702 scopus 로고    scopus 로고
    • Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals
    • DOI 10.1016/S0531-5565(02)00029-3, PII S0531556502000293
    • Weksler M. E., Relkin N., Turkenich R., LaRusse S., Zhou L., Szabo P., Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals. Experimental Gerontology 2002 37 7 943 948 2-s2.0-0036085702 10.1016/S0531-5565(02)00029-3 (Pubitemid 34665486)
    • (2002) Experimental Gerontology , vol.37 , Issue.7 , pp. 943-948
    • Weksler, M.E.1    Relkin, N.2    Turkenich, R.3    LaRusse, S.4    Zhou, L.5    Szabo, P.6
  • 34
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • DOI 10.1016/S0197-4580(02)00065-9, PII S0197458002000659
    • Braak H., Del Tredici K., Rüb U., de Vos R. A. I., Jansen Steur E. N. H., Braak E., Staging of brain pathology related to sporadic Parkinson's disease. Neurobiology of Aging 2003 24 2 197 211 2-s2.0-0037333666 10.1016/S0197-4580(02)00065-9 (Pubitemid 36007810)
    • (2003) Neurobiology of Aging , vol.24 , Issue.2 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rub, U.3    De Vos, R.A.I.4    Jansen Steur, E.N.H.5    Braak, E.6
  • 35
    • 84861706581 scopus 로고    scopus 로고
    • α -Synuclein overexpressing transgenic mice show internal organ pathology and autonomic deficits
    • 2-s2.0-84861706581 10.1016/j.nbd.2012.04.009
    • Hallett P. J., McLean J. R., Kartunen A., Langston J. W., Isacson O., α -Synuclein overexpressing transgenic mice show internal organ pathology and autonomic deficits. Neurobiology of Disease 2012 47 2 258 267 2-s2.0-84861706581 10.1016/j.nbd.2012.04.009
    • (2012) Neurobiology of Disease , vol.47 , Issue.2 , pp. 258-267
    • Hallett, P.J.1    McLean, J.R.2    Kartunen, A.3    Langston, J.W.4    Isacson, O.5
  • 36
    • 4644323707 scopus 로고    scopus 로고
    • Autonomic failure as the initial presentation of Parkinson disease and dementia with Lewy bodies
    • Kaufmann H., Nahm K., Purohit D., Wolfe D., Autonomic failure as the initial presentation of Parkinson disease and dementia with Lewy bodies. Neurology 2004 63 6 1093 1095 2-s2.0-4644323707 (Pubitemid 39287924)
    • (2004) Neurology , vol.63 , Issue.6 , pp. 1093-1095
    • Kaufmann, H.1    Nahm, K.2    Purohit, D.3    Wolfe, D.4
  • 37
    • 0041589248 scopus 로고    scopus 로고
    • α-synuclein Is Degraded by Both Autophagy and the Proteasome
    • DOI 10.1074/jbc.M300227200
    • Webb J. L., Ravikumar B., Atkins J., Skepper J. N., Rubinsztein D. C., α -Synuclein is degraded by both autophagy and the proteasome. The Journal of Biological Chemistry 2003 278 27 25009 25013 2-s2.0-0041589248 10.1074/jbc.M300227200 (Pubitemid 37548663)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3    Skepper, J.N.4    Rubinsztein, D.C.5
  • 38
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo A. M., Stafanis L., Fredenburg R., Lansbury P. T., Sulzer D., Impaired degradation of mutant α -synuclein by chaperone-mediated autophagy. Science 2004 305 5688 1292 1295 2-s2.0-4344659685 10.1126/science.1101738 (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 39
    • 0035976835 scopus 로고    scopus 로고
    • α-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • DOI 10.1016/S0014-5793(01)03115-5, PII S0014579301031155
    • Tofaris G. K., Layfield R., Spillantini M. G., α -Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Letters 2001 509 1 22 26 2-s2.0-0035976835 10.1016/S0014-5793(01)03115-5 (Pubitemid 33153074)
    • (2001) FEBS Letters , vol.509 , Issue.1 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 40
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in α -synuclein models of Parkinson's and Lewy body diseases
    • 2-s2.0-70350550208 10.1523/JNEUROSCI.4390-09.2009
    • Spencer B., Potkar R., Trejo M., Rockenstein E., Patrick C., Gindi R., Adame A., Wyss-Coray T., Masliah E., Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in α -synuclein models of Parkinson's and Lewy body diseases. Journal of Neuroscience 2009 29 43 13578 13588 2-s2.0-70350550208 10.1523/JNEUROSCI.4390-09.2009
    • (2009) Journal of Neuroscience , vol.29 , Issue.43 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 42
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L., Larsen K. E., Rideout H. J., Sulzer D., Greene L. A., Expression of A53T mutant but not wild-type α -synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. Journal of Neuroscience 2001 21 24 9549 9560 2-s2.0-0035894855 (Pubitemid 34184043)
    • (2001) Journal of Neuroscience , vol.21 , Issue.24 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 43
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant α-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • Tanaka Y., Engelender S., Igarashi S., Rao R. K., Wanner T., Tanzi R. E., Sawa A., Dawson V. L., Dawson T. M., Ross C. A., Inducible expression of mutant α -synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Human Molecular Genetics 2001 10 9 919 926 2-s2.0-0035870881 (Pubitemid 32401408)
    • (2001) Human Molecular Genetics , vol.10 , Issue.9 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6    Sawa, A.7    Dawson, V.L.8    Dawson, T.M.9    Ross, C.A.10
  • 44
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant α-Synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • DOI 10.1016/S0896-6273(02)01125-X
    • Petrucelli L., O'Farrell C., Lockhart P. J., Baptista M., Kehoe K., Vink L., Choi P., Wolozin B., Farrer M., Hardy J., Cookson M. R., Parkin protects against the toxicity associated with mutant α -synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 2002 36 6 1007 1019 2-s2.0-0037137702 10.1016/S0896-6273(02)01125-X (Pubitemid 36044504)
    • (2002) Neuron , vol.36 , Issue.6 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6    Choi, P.7    Wolozin, B.8    Farrer, M.9    Hardy, J.10    Cookson, M.R.11
  • 45
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric α-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
    • DOI 10.1074/jbc.M208641200
    • Snyder H., Mensah K., Theisler C., Lee J., Matouschek A., Wolozin B., Aggregated and monomeric α -synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function. The Journal of Biological Chemistry 2003 278 14 11753 11759 2-s2.0-0038413759 10.1074/jbc.M208641200 (Pubitemid 36800143)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 47
    • 79952451427 scopus 로고    scopus 로고
    • Mitophagy: The latest problem for Parkinson's disease
    • 2-s2.0-79952451427 10.1016/j.molmed.2010.11.002
    • Vives-Bauza C., Przedborski S., Mitophagy: the latest problem for Parkinson's disease. Trends in Molecular Medicine 2011 17 3 158 165 2-s2.0-79952451427 10.1016/j.molmed.2010.11.002
    • (2011) Trends in Molecular Medicine , vol.17 , Issue.3 , pp. 158-165
    • Vives-Bauza, C.1    Przedborski, S.2
  • 50
    • 79955701611 scopus 로고    scopus 로고
    • DJ-1 regulation of mitochondrial function and autophagy through oxidative stress
    • 2-s2.0-79955701611 10.4161/auto.7.5.14684
    • McCoy M. K., Cookson M. R., DJ-1 regulation of mitochondrial function and autophagy through oxidative stress. Autophagy 2011 7 5 531 532 2-s2.0-79955701611 10.4161/auto.7.5.14684
    • (2011) Autophagy , vol.7 , Issue.5 , pp. 531-532
    • McCoy, M.K.1    Cookson, M.R.2
  • 51
    • 77953090478 scopus 로고    scopus 로고
    • Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of α -synuclein, and apoptotic cell death in aged mice
    • 2-s2.0-77953090478 10.1073/pnas.1004676107
    • Tong Y., Yamaguchi H., Giaime E., Boyle S., Kopan R., Kelleher R. J., Shen J., Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of α -synuclein, and apoptotic cell death in aged mice. Proceedings of the National Academy of Sciences of the United States of America 2010 107 21 9879 9884 2-s2.0-77953090478 10.1073/pnas.1004676107
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , Issue.21 , pp. 9879-9884
    • Tong, Y.1    Yamaguchi, H.2    Giaime, E.3    Boyle, S.4    Kopan, R.5    Kelleher, R.J.6    Shen, J.7
  • 53
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and α -synuclein form a bidirectional pathogenic loop in synucleinopathies
    • 2-s2.0-79960009804 10.1016/j.cell.2011.06.001
    • Mazzulli J. R., Xu Y. H., Sun Y., Knight A. L., McLean P. J., Caldwell G. A., Sidransky E., Grabowski G. A., Krainc D., Gaucher disease glucocerebrosidase and α -synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 2011 146 1 37 52 2-s2.0-79960009804 10.1016/j.cell.2011.06.001
    • (2011) Cell , vol.146 , Issue.1 , pp. 37-52
    • Mazzulli, J.R.1    Xu, Y.H.2    Sun, Y.3    Knight, A.L.4    McLean, P.J.5    Caldwell, G.A.6    Sidransky, E.7    Grabowski, G.A.8    Krainc, D.9
  • 55
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of α-synuclein and its aggregates
    • DOI 10.1523/JNEUROSCI.0692-05.2005
    • Lee H. J., Patel S., Lee S. J., Intravesicular localization and exocytosis of α -synuclein and its aggregates. Journal of Neuroscience 2005 25 25 6016 6024 2-s2.0-21344456506 10.1523/JNEUROSCI.0692-05.2005 (Pubitemid 40911433)
    • (2005) Journal of Neuroscience , vol.25 , Issue.25 , pp. 6016-6024
    • Lee, H.-J.1    Patel, S.2    Lee, S.-J.3
  • 56
    • 85109083933 scopus 로고    scopus 로고
    • α -Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma
    • El-Agnaf O. M., Salem S. A., Paleologou K. E., Cooper L. J., Fullwood N. J., α -Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma. The FASEB Journal 2003 17 13 1945 1947
    • (2003) The FASEB Journal , vol.17 , Issue.13 , pp. 1945-1947
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Cooper, L.J.4    Fullwood, N.J.5
  • 57
    • 79951720856 scopus 로고    scopus 로고
    • α -Synuclein and tau concentrations in cerebrospinal fluid of patients presenting with parkinsonism: A cohort study
    • 2-s2.0-79951720856 10.1016/S1474-4422(11)70014-X
    • Mollenhauer B., Locascio J. J., Schulz-Schaeffer W., Sixel-Döring F., Trenkwalder C., Schlossmacher M. G., α -Synuclein and tau concentrations in cerebrospinal fluid of patients presenting with parkinsonism: a cohort study. The Lancet Neurology 2011 10 3 230 240 2-s2.0-79951720856 10.1016/S1474-4422(11)70014-X
    • (2011) The Lancet Neurology , vol.10 , Issue.3 , pp. 230-240
    • Mollenhauer, B.1    Locascio, J.J.2    Schulz-Schaeffer, W.3    Sixel-Döring, F.4    Trenkwalder, C.5    Schlossmacher, M.G.6
  • 58
    • 0036459335 scopus 로고    scopus 로고
    • Neuroinflammation of the nigrostriatal pathway during progressive 6-OHDA dopamine degeneration in rats monitored by immunohistochemistry and PET imaging
    • DOI 10.1046/j.1460-9568.2002.01938.x
    • Cicchetti F., Brownell A. L., Williams K., Chen Y. I., Livni E., Isacson O., Neuroinflammation of the nigrostriatal pathway during progressive 6-OHDA dopamine degeneration in rats monitored by immunohistochemistry and PET imaging. European Journal of Neuroscience 2002 15 6 991 998 2-s2.0-0036459335 10.1046/j.1460-9568.2002.01938.x (Pubitemid 35463634)
    • (2002) European Journal of Neuroscience , vol.15 , Issue.6 , pp. 991-998
    • Cicchetti, F.1    Brownell, A.L.2    Williams, K.3    Chen, Y.I.4    Livni, E.5    Isacson, O.6
  • 59
    • 4344645719 scopus 로고    scopus 로고
    • Selective COX-2 inhibition prevents progressive dopamine neuron degeneration in a rat model of Parkinson's disease
    • DOI 10.1186/1742-2094-1-6
    • Sánchez-Pernaute R., Ferree A., Cooper O., Yu M., Brownell A. L., Isacson O., Selective COX-2 inhibition prevents progressive dopamine neuron degeneration in a rat model of Parkinson's disease. Journal of Neuroinflammation 2004 1, article 6 2-s2.0-4344645719 10.1186/1742-2094-1-6 (Pubitemid 39130328)
    • (2004) Journal of Neuroinflammation , vol.1 , pp. 6
    • Sanchez-Pernaute, R.1    Ferree, A.2    Cooper, O.3    Yu, M.4    Brownell, A.-L.5    Isacson, O.6
  • 60
    • 84857225543 scopus 로고    scopus 로고
    • Viral and inflammatory triggers of neurodegenerative diseases
    • 121ps3 2-s2.0-84857225543 10.1126/scitranslmed.3003492
    • Deleidi M., Isacson O., Viral and inflammatory triggers of neurodegenerative diseases. Science Translational Medicine 2012 4 121 121ps3 2-s2.0-84857225543 10.1126/scitranslmed.3003492
    • (2012) Science Translational Medicine , vol.4 , Issue.121
    • Deleidi, M.1    Isacson, O.2
  • 61
    • 84864379214 scopus 로고    scopus 로고
    • Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity
    • 2-s2.0-84864379214 10.1016/j.neurobiolaging.2011.12.006
    • Teismann P., Sathe K., Bierhaus A., Leng L., Martin H. L., Bucala R., Weigle B., Nawroth P. P., Schulz J. B., Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity. Neurobiology of Aging 2012 33 10 2478 2490 2-s2.0-84864379214 10.1016/j.neurobiolaging.2011.12. 006
    • (2012) Neurobiology of Aging , vol.33 , Issue.10 , pp. 2478-2490
    • Teismann, P.1    Sathe, K.2    Bierhaus, A.3    Leng, L.4    Martin, H.L.5    Bucala, R.6    Weigle, B.7    Nawroth, P.P.8    Schulz, J.B.9
  • 62
    • 33847237667 scopus 로고    scopus 로고
    • Osteopontin is elevated in Parkinson's disease and its absence leads to reduced neurodegeneration in the MPTP model
    • 2-s2.0-33847237667 10.1016/j.nbd.2006.10.020
    • Maetzler W., Berg D., Schalamberidze N., Melms A., Schott K., Mueller J. C., Liaw L., Gasser T., Nitsch C., Osteopontin is elevated in Parkinson's disease and its absence leads to reduced neurodegeneration in the MPTP model. Neurobiology of Disease 2007 25 3 473 482 2-s2.0-33847237667 10.1016/j.nbd.2006.10.020
    • (2007) Neurobiology of Disease , vol.25 , Issue.3 , pp. 473-482
    • Maetzler, W.1    Berg, D.2    Schalamberidze, N.3    Melms, A.4    Schott, K.5    Mueller, J.C.6    Liaw, L.7    Gasser, T.8    Nitsch, C.9
  • 63
    • 79951499176 scopus 로고    scopus 로고
    • Glia: Initiators and progressors of pathology in Parkinson's disease
    • 2-s2.0-79951499176 10.1002/mds.23455
    • Halliday G. M., Stevens C. H., Glia: initiators and progressors of pathology in Parkinson's disease. Movement Disorders 2011 26 1 6 17 2-s2.0-79951499176 10.1002/mds.23455
    • (2011) Movement Disorders , vol.26 , Issue.1 , pp. 6-17
    • Halliday, G.M.1    Stevens, C.H.2
  • 64
    • 77951077317 scopus 로고    scopus 로고
    • Astrocytic expression of Parkinson's disease-related A53T α -synuclein causes neurodegeneration in mice
    • 2-s2.0-77951077317 10.1186/1756-6606-3-12
    • Gu X. L., Long C. X., Sun L., Xie C., Lin X., Cai H., Astrocytic expression of Parkinson's disease-related A53T α -synuclein causes neurodegeneration in mice. Molecular Brain 2010 3 1, article 12 2-s2.0-77951077317 10.1186/1756-6606-3-12
    • (2010) Molecular Brain , vol.3 , Issue.1 ARTICLE 12
    • Gu, X.L.1    Long, C.X.2    Sun, L.3    Xie, C.4    Lin, X.5    Cai, H.6
  • 65
    • 0034641287 scopus 로고    scopus 로고
    • Activated microglia in dementia with Lewy bodies
    • 2-s2.0-0034641287
    • Mackenzie I. R. A., Activated microglia in dementia with Lewy bodies. Neurology 2000 55 1 132 134 2-s2.0-0034641287
    • (2000) Neurology , vol.55 , Issue.1 , pp. 132-134
    • MacKenzie, I.R.A.1
  • 66
    • 34547727312 scopus 로고    scopus 로고
    • Development of α-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease
    • DOI 10.1007/s00401-007-0244-3
    • Braak H., Sastre M., Del Tredici K., Development of α -synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease. Acta Neuropathologica 2007 114 3 231 241 2-s2.0-34547727312 10.1007/s00401-007-0244-3 (Pubitemid 47226149)
    • (2007) Acta Neuropathologica , vol.114 , Issue.3 , pp. 231-241
    • Braak, H.1    Sastre, M.2    Del Tredici, K.3
  • 67
    • 44749090147 scopus 로고    scopus 로고
    • Clearance and deposition of extracellular α -synuclein aggregates in microglia
    • 2-s2.0-44749090147 10.1016/j.bbrc.2008.05.045
    • Lee H. J., Suk J. E., Bae E. J., Lee S. J., Clearance and deposition of extracellular α -synuclein aggregates in microglia. Biochemical and Biophysical Research Communications 2008 372 3 423 428 2-s2.0-44749090147 10.1016/j.bbrc.2008.05.045
    • (2008) Biochemical and Biophysical Research Communications , vol.372 , Issue.3 , pp. 423-428
    • Lee, H.J.1    Suk, J.E.2    Bae, E.J.3    Lee, S.J.4
  • 70
    • 0030222037 scopus 로고    scopus 로고
    • Microglia: A sensor for pathological events in the CNS
    • DOI 10.1016/0166-2236(96)10049-7
    • Kreutzberg G. W., Microglia: a sensor for pathological events in the CNS. Trends in Neurosciences 1996 19 8 312 318 2-s2.0-0030222037 10.1016/0166-2236(96)10049-7 (Pubitemid 26349059)
    • (1996) Trends in Neurosciences , vol.19 , Issue.8 , pp. 312-318
    • Kreutzberg, G.W.1
  • 71
    • 27644531857 scopus 로고    scopus 로고
    • A possible role for humoral immunity in the pathogenesis of Parkinson's disease
    • DOI 10.1093/brain/awh625
    • Orr C. F., Rowe D. B., Mizuno Y., Mori H., Halliday G. M., A possible role for humoral immunity in the pathogenesis of Parkinson's disease. Brain 2005 128 11 2665 2674 2-s2.0-27644531857 10.1093/brain/awh625 (Pubitemid 41552950)
    • (2005) Brain , vol.128 , Issue.11 , pp. 2665-2674
    • Orr, C.F.1    Rowe, D.B.2    Mizuno, Y.3    Mori, H.4    Halliday, G.M.5
  • 72
    • 80052850843 scopus 로고    scopus 로고
    • Autoantibodies against amyloid and glial-derived antigens are increased in serum and cerebrospinal fluid of lewy body-associated dementias
    • 2-s2.0-80052850843 10.3233/JAD-2011-110221
    • Maetzler W., Berg D., Synofzik M., Brockmann K., Godau J., Melms A., Gasser T., Hörnig S., Langkamp M., Autoantibodies against amyloid and glial-derived antigens are increased in serum and cerebrospinal fluid of lewy body-associated dementias. Journal of Alzheimer's Disease 2011 26 1 171 179 2-s2.0-80052850843 10.3233/JAD-2011-110221
    • (2011) Journal of Alzheimer's Disease , vol.26 , Issue.1 , pp. 171-179
    • Maetzler, W.1    Berg, D.2    Synofzik, M.3    Brockmann, K.4    Godau, J.5    Melms, A.6    Gasser, T.7    Hörnig, S.8    Langkamp, M.9
  • 77
    • 78649990079 scopus 로고    scopus 로고
    • Detection of elevated levels of α -synuclein oligomers in CSF from patients with Parkinson disease
    • 2-s2.0-78649990079 10.1212/WNL.0b013e3181fd613b
    • Tokuda T., Qureshi M. M., Ardah M. T., Varghese S., Shehab S. A. S., Kasai T., Ishigami N., Tamaoka A., Nakagawa M., El-Agnaf O. M. A., Detection of elevated levels of α -synuclein oligomers in CSF from patients with Parkinson disease. Neurology 2010 75 20 1766 1772 2-s2.0-78649990079 10.1212/WNL.0b013e3181fd613b
    • (2010) Neurology , vol.75 , Issue.20 , pp. 1766-1772
    • Tokuda, T.1    Qureshi, M.M.2    Ardah, M.T.3    Varghese, S.4    Shehab, S.A.S.5    Kasai, T.6    Ishigami, N.7    Tamaoka, A.8    Nakagawa, M.9    El-Agnaf, O.M.A.10
  • 80
  • 83
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • 2-s2.0-38349046973 10.1242/jcs.019265
    • Nixon R. A., Autophagy, amyloidogenesis and Alzheimer disease. Journal of Cell Science 2007 120 23 4081 4091 2-s2.0-38349046973 10.1242/jcs.019265
    • (2007) Journal of Cell Science , vol.120 , Issue.23 , pp. 4081-4091
    • Nixon, R.A.1
  • 84
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • 2-s2.0-49049096562 10.1523/JNEUROSCI.0800-08.2008
    • Boland B., Kumar A., Lee S., Platt F. M., Wegiel J., Yu W. H., Nixon R. A., Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. Journal of Neuroscience 2008 28 27 6926 6937 2-s2.0-49049096562 10.1523/JNEUROSCI.0800-08.2008
    • (2008) Journal of Neuroscience , vol.28 , Issue.27 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 87
    • 0036450037 scopus 로고    scopus 로고
    • Cerebrovascular disease is a major factor in the failure of elimination of Aβ from the aging human brain: Implications for therapy of Alzheimer's disease
    • Weller R. O., Yow H. Y., Preston S. D., Mazanti I., Nicoll J. A. R., Cerebrovascular disease is a major factor in the failure of elimination of A β from the aging human brain: implications for therapy of Alzheimer's disease. Annals of the New York Academy of Sciences 2002 977 162 168 2-s2.0-0036450037 (Pubitemid 35418150)
    • (2002) Annals of the New York Academy of Sciences , vol.977 , pp. 162-168
    • Weller, R.O.1    Yow, H.-Y.2    Preston, S.D.3    Mazanti, I.4    Nicoll, J.A.R.5
  • 88
    • 42149125510 scopus 로고    scopus 로고
    • Amyloid-degrading enzymes as therapeutic targets in Alzheimer's disease
    • DOI 10.2174/156720508783954785
    • Nalivaeva N. N., Fisk L. R., Belyaev N. D., Turner A. J., Amyloid-degrading enzymes as therapeutic targets in Alzheimer's disease. Current Alzheimer Research 2008 5 2 212 224 2-s2.0-42149125510 10.2174/ 156720508783954785 (Pubitemid 351536346)
    • (2008) Current Alzheimer Research , vol.5 , Issue.2 , pp. 212-224
    • Nalivaeva, N.N.1    Fisk, L.R.2    Belyaev, N.D.3    Turner, A.J.4
  • 89
    • 79954623282 scopus 로고    scopus 로고
    • Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy
    • 2-s2.0-79954623282 10.1007/s00401-011-0801-7
    • Hawkes C. A., Härtig W., Kacza J., Schliebs R., Weller R. O., Nicoll J. A., Carare R. O., Perivascular drainage of solutes is impaired in the ageing mouse brain and in the presence of cerebral amyloid angiopathy. Acta Neuropathologica 2011 121 4 431 443 2-s2.0-79954623282 10.1007/s00401-011-0801-7
    • (2011) Acta Neuropathologica , vol.121 , Issue.4 , pp. 431-443
    • Hawkes, C.A.1    Härtig, W.2    Kacza, J.3    Schliebs, R.4    Weller, R.O.5    Nicoll, J.A.6    Carare, R.O.7
  • 90
    • 0029061685 scopus 로고
    • Neutral endopeptidase can hydrolyze β -amyloid(140) but shows no effect on β -amyloid precursor protein metabolism
    • 2-s2.0-0029061685 10.1016/0196-9781(95)00021-B
    • Howell S., Nalbantoglu J., Crine P., Neutral endopeptidase can hydrolyze β -amyloid(140) but shows no effect on β -amyloid precursor protein metabolism. Peptides 1995 16 4 647 652 2-s2.0-0029061685 10.1016/0196-9781(95) 00021-B
    • (1995) Peptides , vol.16 , Issue.4 , pp. 647-652
    • Howell, S.1    Nalbantoglu, J.2    Crine, P.3
  • 92
    • 0025277862 scopus 로고
    • Characterization of endopeptidase 3.4.24.11 ('enkephalinase') activity in human plasma and cerebrospinal fluid
    • DOI 10.1016/0006-2952(90)90012-A
    • Spillantini M. G., Sicuteri F., Salmon S., Malfroy B., Characterization of endopeptidase 3.4.24.11 (enkephalinase) activity in human plasma and cerebrospinal fluid. Biochemical Pharmacology 1990 39 8 1353 1356 2-s2.0-0025277862 10.1016/0006-2952(90)90012-A (Pubitemid 20119211)
    • (1990) Biochemical Pharmacology , vol.39 , Issue.8 , pp. 1353-1356
    • Spillantini, M.G.1    Sicuteri, F.2    Salmon, S.3    Malfroy, B.4
  • 94
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
    • DOI 10.1002/jnr.10390
    • Iwata N., Takaki Y., Fukami S., Tsubuki S., Saido T. C., Region-specific reduction of A β -degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. Journal of Neuroscience Research 2002 70 3 493 500 2-s2.0-0037010286 10.1002/jnr.10390 (Pubitemid 35222386)
    • (2002) Journal of Neuroscience Research , vol.70 , Issue.3 , pp. 493-500
    • Iwata, N.1    Takaki, Y.2    Fukami, S.3    Tsubuki, S.4    Saido, T.C.5
  • 95
    • 0034637296 scopus 로고    scopus 로고
    • Involvement of cystatin C in oxidative stress-induced apoptosis of cultured rat CNS neurons
    • DOI 10.1016/S0006-8993(00)02540-3, PII S0006899300025403
    • Nishio C., Yoshida K., Nishiyama K., Hatanaka H., Yamada M., Involvement of cystatin C in oxidative stress-induced apoptosis of cultured rat CNS neurons. Brain Research 2000 873 2 252 262 2-s2.0-0034637296 10.1016/S0006-8993(00) 02540-3 (Pubitemid 30619049)
    • (2000) Brain Research , vol.873 , Issue.2 , pp. 252-262
    • Nishio, C.1    Yoshida, K.2    Nishiyama, K.3    Hatanaka, H.4    Yamada, M.5
  • 96
    • 0027058414 scopus 로고
    • Diagnostic value of analysis of cystatin C and protein HC in biological fluids
    • Grubb A., Diagnostic value of analysis of cystatin C and protein HC in biological fluids. Clinical Nephrology 1992 38 supplement 1 S20 S27 2-s2.0-0027058414 (Pubitemid 23092541)
    • (1992) Clinical Nephrology , vol.38 , Issue.SUPPL. 1
    • Grubb, A.1
  • 98
    • 2942737051 scopus 로고    scopus 로고
    • Binding of cystatin C to Alzheimer's amyloid β inhibits in vitro amyloid fibril formation
    • DOI 10.1016/j.neurobiolaging.2003.11.006, PII S0197458003002227
    • Sastre M., Calero M., Pawlik M., Mathews P. M., Kumar A., Danilov V., Schmidt S. D., Nixon R. A., Frangione B., Levy E., Binding of cystatin C to Alzheimer's amyloid β inhibits in vitro amyloid fibril formation. Neurobiology of Aging 2004 25 8 1033 1043 2-s2.0-2942737051 10.1016/j. neurobiolaging.2003.11.006 (Pubitemid 38798065)
    • (2004) Neurobiology of Aging , vol.25 , Issue.8 , pp. 1033-1043
    • Sastre, M.1    Calero, M.2    Pawlik, M.3    Mathews, P.M.4    Kumar, A.5    Danilov, V.6    Schmidt, S.D.7    Nixon, R.A.8    Frangione, B.9    Levy, E.10
  • 99
    • 60349101411 scopus 로고    scopus 로고
    • Reduced levels of amyloid- β -binding proteins in cerebrospinal fluid from Alzheimer's disease patients
    • 2-s2.0-60349101411 10.3233/JAD-2009-0966
    • Hansson S. F., Andréasson U., Wall M., Skoog I., Andreasen N., Wallin A., Zetterberg H., Blennow K., Reduced levels of amyloid- β -binding proteins in cerebrospinal fluid from Alzheimer's disease patients. Journal of Alzheimer's Disease 2009 16 2 389 397 2-s2.0-60349101411 10.3233/JAD-2009-0966
    • (2009) Journal of Alzheimer's Disease , vol.16 , Issue.2 , pp. 389-397
    • Hansson, S.F.1    Andréasson, U.2    Wall, M.3    Skoog, I.4    Andreasen, N.5    Wallin, A.6    Zetterberg, H.7    Blennow, K.8
  • 100
    • 36448997798 scopus 로고    scopus 로고
    • A novel panel of cerebrospinal fluid biomarkers for the differential diagnosis of Alzheimer's disease versus normal aging and frontotemporal dementia
    • DOI 10.1159/000110576
    • Simonsen A. H., McGuire J., Podust V. N., Hagnelius N. O., Nilsson T. K., Kapaki E., Vassilopoulos D., Waldemar G., A novel panel of cerebrospinal fluid biomarkers for the differential diagnosis of Alzheimer's disease versus normal aging and frontotemporal dementia. Dementia and Geriatric Cognitive Disorders 2007 24 6 434 440 2-s2.0-36448997798 10.1159/000110576 (Pubitemid 350175903)
    • (2007) Dementia and Geriatric Cognitive Disorders , vol.24 , Issue.6 , pp. 434-440
    • Simonsen, A.H.1    McGuire, J.2    Podust, V.N.3    Hagnelius, N.-O.4    Nilsson, T.K.5    Kapaki, E.6    Vassilopoulos, D.7    Waldemar, G.8
  • 104
    • 7244221537 scopus 로고    scopus 로고
    • Unexpected intracellular localization of the AMD-associated cystatin C variant
    • DOI 10.1111/j.1600-0854.2004.00230.x
    • Paraoan L., Ratnayaka A., Spiller D. G., Hiscott P., White M. R. H., Grierson I., Unexpected intracellular localization of the AMD-associated cystatin C variant. Traffic 2004 5 11 884 895 2-s2.0-7244221537 10.1111/j.1600-0854.2004.00230.x (Pubitemid 39433558)
    • (2004) Traffic , vol.5 , Issue.11 , pp. 884-895
    • Paraoan, L.1    Ratnayaka, A.2    Spiller, D.G.3    Hiscott, P.4    White, M.R.H.5    Grierson, I.6
  • 106
    • 0032731763 scopus 로고    scopus 로고
    • Brain inflammation in Alzheimer disease and the therapeutic implications
    • McGeer E. G., McGeer P. L., Brain inflammation in Alzheimer disease and the therapeutic implications. Current Pharmaceutical Design 1999 5 10 821 836 2-s2.0-0032731763 (Pubitemid 29510788)
    • (1999) Current Pharmaceutical Design , vol.5 , Issue.10 , pp. 821-836
    • McGeer, E.G.1    McGeer, P.L.2
  • 108
    • 55849114955 scopus 로고    scopus 로고
    • The complement cascade: Yin-Yang in neuroinflammationneuro-protection and -degeneration
    • 2-s2.0-55849114955 10.1111/j.1471-4159.2008.05668.x
    • Alexander J. J., Anderson A. J., Barnum S. R., Stevens B., Tenner A. J., The complement cascade: Yin-Yang in neuroinflammationneuro-protection and -degeneration. Journal of Neurochemistry 2008 107 5 1169 1187 2-s2.0-55849114955 10.1111/j.1471-4159.2008.05668.x
    • (2008) Journal of Neurochemistry , vol.107 , Issue.5 , pp. 1169-1187
    • Alexander, J.J.1    Anderson, A.J.2    Barnum, S.R.3    Stevens, B.4    Tenner, A.J.5
  • 109
    • 0035101055 scopus 로고    scopus 로고
    • Expression of scavenger receptor class B, type I, by astrocytes and vascular smooth muscle cells in normal adult mouse and human brain and in Alzheimer's disease brain
    • Husemann J., Silverstein S. C., Expression of scavenger receptor class B, type I, by astrocytes and vascular smooth muscle cells in normal adult mouse and human brain and in Alzheimer's disease brain. American Journal of Pathology 2001 158 3 825 832 2-s2.0-0035101055 (Pubitemid 32221775)
    • (2001) American Journal of Pathology , vol.158 , Issue.3 , pp. 825-832
    • Husemann, J.1    Silverstein, S.C.2
  • 111
    • 57649178322 scopus 로고    scopus 로고
    • The A β Cs of A β -cleaving proteases
    • 2-s2.0-57649178322 10.1074/jbc.R800022200
    • Leissring M. A., The A β Cs of A β -cleaving proteases. The Journal of Biological Chemistry 2008 283 44 29645 29649 2-s2.0-57649178322 10.1074/jbc.R800022200
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.44 , pp. 29645-29649
    • Leissring, M.A.1
  • 112
    • 34547328074 scopus 로고    scopus 로고
    • New insights into the roles of metalloproteinases in neurodegeneration and neuroprotection
    • 2-s2.0-34547328074 10.1016/S0074-7742(07)82006-X
    • Turner A. J., Nalivaeva N. N., New insights into the roles of metalloproteinases in neurodegeneration and neuroprotection. International Review of Neurobiology 2007 82 113 135 2-s2.0-34547328074 10.1016/S0074-7742(07) 82006-X
    • (2007) International Review of Neurobiology , vol.82 , pp. 113-135
    • Turner, A.J.1    Nalivaeva, N.N.2
  • 113
    • 28344439699 scopus 로고    scopus 로고
    • Maximal COX-2 and ppRb expression in neurons occurs during early Braak stages prior to the maximal activation of astrocytes and microglia in Alzheimer's disease
    • DOI 10.1186/1742-2094-2-27
    • Hoozemans J. J. M., van Haastert E. S., Veerhuis R., Arendt T., Scheper W., Eikelenboom P., Rozemuller A. J. M., Maximal COX-2 and ppRb expression in neurons occurs during early Braak stages prior to the maximal activation of astrocytes and microglia in Alzheimer's disease. Journal of Neuroinflammation 2005 2, article 27 2-s2.0-28344439699 10.1186/1742-2094-2-27 (Pubitemid 41715845)
    • (2005) Journal of Neuroinflammation , vol.2 , pp. 27
    • Hoozemans, J.J.M.1    Van Haastert, E.S.2    Veerhuis, R.3    Arendt, T.4    Scheper, W.5    Eikelenboom, P.6    Rozemuller, A.J.M.7
  • 114
    • 0035845283 scopus 로고    scopus 로고
    • In-vivo measurement of activated microglia in dementia
    • DOI 10.1016/S0140-6736(01)05625-2
    • Cagnin A., Brooks D. J., Kennedy A. M., Gunn R. N., Myers R., Turkheimer F. E., Jones T., Banati R. B., In-vivo measurement of activated microglia in dementia. The Lancet 2001 358 9280 461 467 2-s2.0-0035845283 10.1016/S0140-6736(01)05625-2 (Pubitemid 32769854)
    • (2001) Lancet , vol.358 , Issue.9280 , pp. 461-467
    • Cagnin, A.1    Brooks, D.J.2    Kennedy, A.M.3    Gunn, R.N.4    Myers, R.5    Turkheimer, F.E.6    Jones, T.7    Banati, R.B.8
  • 115
    • 0024436506 scopus 로고
    • Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease
    • DOI 10.1016/0165-5728(89)90115-X
    • Itagaki S., McGeer P. L., Akiyama H., Zhu S., Selkoe D., Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease. Journal of Neuroimmunology 1989 24 3 173 182 2-s2.0-0024436506 (Pubitemid 19271472)
    • (1989) Journal of Neuroimmunology , vol.24 , Issue.3 , pp. 173-182
    • Itagaki, S.1    McGeer, P.L.2    Akiyama, H.3    Zhu, S.4    Selkoe, D.5
  • 117
    • 34547127632 scopus 로고    scopus 로고
    • Neuroprotective role of the innate immune system by microglia
    • DOI 10.1016/j.neuroscience.2007.02.055, PII S0306452207002588
    • Glezer I., Simard A. R., Rivest S., Neuroprotective role of the innate immune system by microglia. Neuroscience 2007 147 4 867 883 2-s2.0-34547127632 10.1016/j.neuroscience.2007.02.055 (Pubitemid 47102534)
    • (2007) Neuroscience , vol.147 , Issue.4 , pp. 867-883
    • Glezer, I.1    Simard, A.R.2    Rivest, S.3
  • 119
    • 33750576993 scopus 로고    scopus 로고
    • Role of toll-like receptor signalling in Aβ uptake and clearance
    • DOI 10.1093/brain/awl249
    • Tahara K., Kim H. D., Jin J. J., Maxwell J. A., Li L., Fukuchi K. I., Role of toll-like receptor signalling in A β uptake and clearance. Brain 2006 129 11 3006 3019 2-s2.0-33750576993 10.1093/brain/awl249 (Pubitemid 44684521)
    • (2006) Brain , vol.129 , Issue.11 , pp. 3006-3019
    • Tahara, K.1    Kim, H.-D.2    Jin, J.-J.3    Maxwell, J.A.4    Li, L.5    Fukuchi, K.-I.6
  • 120
    • 45949106077 scopus 로고    scopus 로고
    • Toll-like receptor 2 acts as a natural innate immune receptor to clear amyloid β 142 and delay the cognitive decline in a mouse model of Alzheimer's disease
    • 2-s2.0-45949106077 10.1523/JNEUROSCI.1146-08.2008
    • Richard K. L., Filali M., Préfontaine P., Rivest S., Toll-like receptor 2 acts as a natural innate immune receptor to clear amyloid β 142 and delay the cognitive decline in a mouse model of Alzheimer's disease. Journal of Neuroscience 2008 28 22 5784 5793 2-s2.0-45949106077 10.1523/JNEUROSCI.1146- 08.2008
    • (2008) Journal of Neuroscience , vol.28 , Issue.22 , pp. 5784-5793
    • Richard, K.L.1    Filali, M.2    Préfontaine, P.3    Rivest, S.4
  • 122
    • 84867487110 scopus 로고    scopus 로고
    • Lowered serum amyloid-beta142 autoantibodies in individuals with lifetime depression
    • 10.3233/JAD-2012-120625
    • Maetzler W., Langkamp M., Lerche S., Godau J., Brockmann K., Lowered serum amyloid-beta142 autoantibodies in individuals with lifetime depression. Journal of Alzheimer's Disease 2012 32 1 95 100 10.3233/JAD-2012-120625
    • (2012) Journal of Alzheimer's Disease , vol.32 , Issue.1 , pp. 95-100
    • Maetzler, W.1    Langkamp, M.2    Lerche, S.3    Godau, J.4    Brockmann, K.5
  • 126
    • 80155190079 scopus 로고    scopus 로고
    • Serum and cerebrospinal fluid uric acid levels in lewy body disorders: Associations with disease occurrence and amyloid- β pathway
    • 2-s2.0-80155190079 10.3233/JAD-2011-110587
    • Maetzler W., Stapf A. K., Schulte C., Hauser A.-K., Lerche S., Wurster I., Schleicher E., Melms A., Berg D., Serum and cerebrospinal fluid uric acid levels in lewy body disorders: associations with disease occurrence and amyloid- β pathway. Journal of Alzheimer's Disease 2011 27 1 119 126 2-s2.0-80155190079 10.3233/JAD-2011-110587
    • (2011) Journal of Alzheimer's Disease , vol.27 , Issue.1 , pp. 119-126
    • Maetzler, W.1    Stapf, A.K.2    Schulte, C.3    Hauser, A.-K.4    Lerche, S.5    Wurster, I.6    Schleicher, E.7    Melms, A.8    Berg, D.9
  • 127
    • 50649114611 scopus 로고    scopus 로고
    • Amyloid- β dynamics correlate with neurological status in the injured human brain
    • 2-s2.0-50649114611 10.1126/science.1161591
    • Brody D. L., Magnoni S., Schwetye K. E., Spinner M. L., Esparza T. J., Stocchetti N., Zipfel G. J., Holtzman D. M., Amyloid- β dynamics correlate with neurological status in the injured human brain. Science 2008 321 5893 1221 1224 2-s2.0-50649114611 10.1126/science.1161591
    • (2008) Science , vol.321 , Issue.5893 , pp. 1221-1224
    • Brody, D.L.1    Magnoni, S.2    Schwetye, K.E.3    Spinner, M.L.4    Esparza, T.J.5    Stocchetti, N.6    Zipfel, G.J.7    Holtzman, D.M.8
  • 128
    • 78650656088 scopus 로고    scopus 로고
    • Neprilysin activity in cerebrospinal fluid is associated with dementia and amyloid- β 42 levels in lewy body disease
    • 2-s2.0-78650656088 10.3233/JAD-2010-101197
    • Maetzler W., Stoycheva V., Schmid B., Schulte C., Hauser A. K., Brockmann K., Melms A., Gasser T., Berg D., Neprilysin activity in cerebrospinal fluid is associated with dementia and amyloid- β 42 levels in lewy body disease. Journal of Alzheimer's Disease 2010 22 3 933 938 2-s2.0-78650656088 10.3233/JAD-2010-101197
    • (2010) Journal of Alzheimer's Disease , vol.22 , Issue.3 , pp. 933-938
    • Maetzler, W.1    Stoycheva, V.2    Schmid, B.3    Schulte, C.4    Hauser, A.K.5    Brockmann, K.6    Melms, A.7    Gasser, T.8    Berg, D.9
  • 129
    • 77149165424 scopus 로고    scopus 로고
    • The CST3 BB genotype and low cystatin C cerebrospinal fluid levels are associated with dementia in lewy body disease
    • 2-s2.0-77149165424 10.3233/JAD-2010-1289
    • Maetzler W., Schmid B., Synofzik M., Schulte C., Riester K., Huber H., Brockmann K., Gasser T., Berg D., Melms A., The CST3 BB genotype and low cystatin C cerebrospinal fluid levels are associated with dementia in lewy body disease. Journal of Alzheimer's Disease 2010 19 3 937 942 2-s2.0-77149165424 10.3233/JAD-2010-1289
    • (2010) Journal of Alzheimer's Disease , vol.19 , Issue.3 , pp. 937-942
    • Maetzler, W.1    Schmid, B.2    Synofzik, M.3    Schulte, C.4    Riester, K.5    Huber, H.6    Brockmann, K.7    Gasser, T.8    Berg, D.9    Melms, A.10
  • 130
    • 0034717256 scopus 로고    scopus 로고
    • Degeneration process of Lewy bodies in the brains of patients with dementia with Lewy bodies using α-synuclein-immunohistochemistry
    • DOI 10.1016/S0304-3940(00)01090-9, PII S0304394000010909
    • Iseki E., Marui W., Akiyama H., Uéda K., Kosaka K., Degeneration process of Lewy bodies in the brains of patients with dementia with Lewy bodies using α -synuclein-immunohistochemistry. Neuroscience Letters 2000 286 1 69 73 2-s2.0-0034717256 10.1016/S0304-3940(00)01090-9 (Pubitemid 30259123)
    • (2000) Neuroscience Letters , vol.286 , Issue.1 , pp. 69-73
    • Iseki, E.1    Marui, W.2    Akiyama, H.3    Ueda, K.4    Kosaka, K.5
  • 132
    • 14644417871 scopus 로고    scopus 로고
    • Oxidative stress in transgenic mice with oligodendroglial α-synuclein overexpression replicates the characteristic neuropathology of multiple system atrophy
    • Stefanova N., Reindl M., Neumann M., Haass C., Poewe W., Kahle P. J., Wenning G. K., Oxidative stress in transgenic mice with oligodendroglial α -synuclein overexpression replicates the characteristic neuropathology of multiple system atrophy. American Journal of Pathology 2005 166 3 869 876 2-s2.0-14644417871 (Pubitemid 40315643)
    • (2005) American Journal of Pathology , vol.166 , Issue.3 , pp. 869-876
    • Stefanova, N.1    Reindl, M.2    Neumann, M.3    Haass, C.4    Poewe, W.5    Kahle, P.J.6    Wenning, G.K.7
  • 133
    • 18344365433 scopus 로고    scopus 로고
    • Tuft-shaped astrocytes in Lewy body disease
    • DOI 10.1007/s00401-004-0967-3
    • Hishikawa N., Hashizume Y., Yoshida M., Niwa J. I., Tanaka F., Sobue G., Tuft-shaped astrocytes in Lewy body disease. Acta Neuropathologica 2005 109 4 373 380 2-s2.0-18344365433 10.1007/s00401-004-0967-3 (Pubitemid 40637309)
    • (2005) Acta Neuropathologica , vol.109 , Issue.4 , pp. 373-380
    • Hishikawa, N.1    Hashizume, Y.2    Yoshida, M.3    Niwa, J.-I.4    Tanaka, F.5    Sobue, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.