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Volumn 2, Issue 10-11, 2008, Pages 1484-1497

Proteomic identification of proteins in the human brain: Towards a more comprehensive understanding of neurodegenerative disease

Author keywords

Alzheimer disease; Biomarkers; Cerebrospinal fluid; Human brain proteome; Laser dissection microscopy

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; APOLIPOPROTEIN E; PRESENILIN 1; PRESENILIN 2; TAU PROTEIN;

EID: 67449118593     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200800043     Document Type: Review
Times cited : (19)

References (121)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotopecoded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F. et al., Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nat. Biotechnol. 1999, 17, 994-999.
    • (1999) Nat. Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4
  • 3
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 4
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B. et al., Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4
  • 5
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao, X., Freas, A., Ramirez, J., Demirev, P. A., Fenselau, C., Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal. Chem. 2001, 73, 2836-2842.
    • (2001) Anal. Chem , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 6
    • 39449131119 scopus 로고    scopus 로고
    • Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data
    • Finney, G. L., Blackler, A. R., Hoopmann, M. R., Canterbury, J. D. et al., Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data. Anal. Chem. 2008, 80, 961-971.
    • (2008) Anal. Chem , vol.80 , pp. 961-971
    • Finney, G.L.1    Blackler, A.R.2    Hoopmann, M.R.3    Canterbury, J.D.4
  • 7
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas, P. R., Vanhaesebroeck, B., Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol. Cell. Proteomics 2007, 6, 1560-1573.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1560-1573
    • Cutillas, P.R.1    Vanhaesebroeck, B.2
  • 8
    • 33749242423 scopus 로고    scopus 로고
    • Profiling human brain proteome by multi-dimensional separations coupled with MS
    • Park, Y. M., Kim, J. Y., Kwon, K. H., Lee, S. K. et al., Profiling human brain proteome by multi-dimensional separations coupled with MS. Proteomics 2006, 6, 4978-4986.
    • (2006) Proteomics , vol.6 , pp. 4978-4986
    • Park, Y.M.1    Kim, J.Y.2    Kwon, K.H.3    Lee, S.K.4
  • 9
    • 33749238369 scopus 로고    scopus 로고
    • Proteomic analysis and comparison of the biopsy and autopsy specimen of human brain temporal lobe
    • He, S., Wang, Q., He, J., Pu, H. et al., Proteomic analysis and comparison of the biopsy and autopsy specimen of human brain temporal lobe. Proteomics 2006, 6, 4987-4996.
    • (2006) Proteomics , vol.6 , pp. 4987-4996
    • He, S.1    Wang, Q.2    He, J.3    Pu, H.4
  • 10
    • 33749235698 scopus 로고    scopus 로고
    • Gel-free analysis of the human brain proteome: Application of liquid chromatography and mass spectrometry on biopsy and autopsy samples
    • Dumont, D., Noben, J. P., Verhaert, P., Stinissen, P., Robben, J., Gel-free analysis of the human brain proteome: Application of liquid chromatography and mass spectrometry on biopsy and autopsy samples. Proteomics 2006, 6, 4967-4977.
    • (2006) Proteomics , vol.6 , pp. 4967-4977
    • Dumont, D.1    Noben, J.P.2    Verhaert, P.3    Stinissen, P.4    Robben, J.5
  • 11
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., Yates, J. R. III, An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73, 5683-5690.
    • (2001) Anal. Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 12
    • 35649020712 scopus 로고    scopus 로고
    • Proteomics identification of proteins in human cortex using multi-dimensional separations and MALDI tandem mass spectrometer
    • Pan, S., Shi, M., Jin, J., Albin, R. L. et al., Proteomics identification of proteins in human cortex using multi-dimensional separations and MALDI tandem mass spectrometer. Mol. Cell. Proteomics 2007 6, 1818-1823.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1818-1823
    • Pan, S.1    Shi, M.2    Jin, J.3    Albin, R.L.4
  • 13
    • 24744458338 scopus 로고    scopus 로고
    • Apolipoprotein E epsilon4 allele differentiates the clinical response to donepezil in Alzheimer's disease
    • Bizzarro, A., Marra, C., Acciarri, A., Valenza, A. et al., Apolipoprotein E epsilon4 allele differentiates the clinical response to donepezil in Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 2005, 20, 254-261.
    • (2005) Dement. Geriatr. Cogn. Disord , vol.20 , pp. 254-261
    • Bizzarro, A.1    Marra, C.2    Acciarri, A.3    Valenza, A.4
  • 14
    • 0034049387 scopus 로고    scopus 로고
    • A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease
    • Papassotiropoulos, A., Bagli, M., Kurz, A., Kornhuber, J. et al., A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease. Ann. Neurol. 2000, 47, 399-403.
    • (2000) Ann. Neurol , vol.47 , pp. 399-403
    • Papassotiropoulos, A.1    Bagli, M.2    Kurz, A.3    Kornhuber, J.4
  • 15
    • 0029366767 scopus 로고
    • A role for neurofilaments in the pathogenesis of amyotrophic lateral sclerosis
    • Julien, J. P., A role for neurofilaments in the pathogenesis of amyotrophic lateral sclerosis. Biochem. Cell Biol. 1995, 73, 593-597.
    • (1995) Biochem. Cell Biol , vol.73 , pp. 593-597
    • Julien, J.P.1
  • 16
    • 44649194448 scopus 로고    scopus 로고
    • Kitsou, E., Pan, S.Zhang, J. P. Shi, M. et al., Identification of proteins in human substantia nigra. Proteomics Clin. Appl. 2008, 2, 776-782.
    • Kitsou, E., Pan, S.Zhang, J. P. Shi, M. et al., Identification of proteins in human substantia nigra. Proteomics Clin. Appl. 2008, 2, 776-782.
  • 18
    • 0029743757 scopus 로고    scopus 로고
    • Dementia with Lewy bodies
    • Kosaka, K., Iseki, E., Dementia with Lewy bodies. Curr. Opin. Neurol. 1996, 9, 271-275.
    • (1996) Curr. Opin. Neurol , vol.9 , pp. 271-275
    • Kosaka, K.1    Iseki, E.2
  • 19
    • 34648819365 scopus 로고    scopus 로고
    • The LB in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates
    • Wakabayashi, K., Tanji, K., Mori, F., Takahashi, H., The LB in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates. Neuropathology 2007, 27, 494-506.
    • (2007) Neuropathology , vol.27 , pp. 494-506
    • Wakabayashi, K.1    Tanji, K.2    Mori, F.3    Takahashi, H.4
  • 20
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • Braak, H., Del Tredici, K., Rub, U., de Vos, R. A. et al., Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol. Aging 2003, 24, 197-211.
    • (2003) Neurobiol. Aging , vol.24 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rub, U.3    de Vos, R.A.4
  • 21
    • 33947537591 scopus 로고    scopus 로고
    • Proteomic identification of novel proteins in cortical lewy bodies
    • Leverenz, J. B., Umar, I., Wang, Q., Montine, T. J. et al., Proteomic identification of novel proteins in cortical lewy bodies. Brain Pathol. 2007, 17, 139-145.
    • (2007) Brain Pathol , vol.17 , pp. 139-145
    • Leverenz, J.B.1    Umar, I.2    Wang, Q.3    Montine, T.J.4
  • 22
    • 0029686696 scopus 로고    scopus 로고
    • Evolution of the neuropathology of Alzheimer's disease
    • Braak, H., Braak, E., Evolution of the neuropathology of Alzheimer's disease. Acta Neurol. Scand. Suppl. 1996, 165, 3-12.
    • (1996) Acta Neurol. Scand. Suppl , vol.165 , pp. 3-12
    • Braak, H.1    Braak, E.2
  • 23
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu, P. J., Wulf, G., Zhou, X. Z., Davies, P., Lu, K. P., The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 1999, 399, 784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 24
    • 0036938198 scopus 로고    scopus 로고
    • Inverse association of Pin1 and tau accumulation in Alzheimer's disease hippocampus
    • Holzer, M., Gartner, U., Stobe, A., Hartig, W. et al., Inverse association of Pin1 and tau accumulation in Alzheimer's disease hippocampus. Acta Neuropathol. (Berl.) 2002, 104, 471-481.
    • (2002) Acta Neuropathol. (Berl.) , vol.104 , pp. 471-481
    • Holzer, M.1    Gartner, U.2    Stobe, A.3    Hartig, W.4
  • 25
    • 0142157635 scopus 로고    scopus 로고
    • Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies
    • Ramakrishnan, P., Dickson, D. W., Davies, P., Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies. Neurobiol. Dis. 2003, 14, 251-264.
    • (2003) Neurobiol. Dis , vol.14 , pp. 251-264
    • Ramakrishnan, P.1    Dickson, D.W.2    Davies, P.3
  • 26
    • 33646511135 scopus 로고    scopus 로고
    • Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis
    • Sultana, R., Boyd-Kimball, D., Poon, H. F., Cai, J. et al., Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis. Neurobiol. Aging 2006, 27, 918-925.
    • (2006) Neurobiol. Aging , vol.27 , pp. 918-925
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4
  • 28
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang, Q., Woltjer, R. L., Cimino, P. J., Pan, C. et al., Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 2005, 19, 869-871.
    • (2005) FASEB J , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4
  • 29
    • 33750063178 scopus 로고    scopus 로고
    • Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies
    • Olah, J., Tokesi, N., Vincze, O., Horvath, I. et al., Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies. FEBS Lett. 2006, 580, 5807-5814.
    • (2006) FEBS Lett , vol.580 , pp. 5807-5814
    • Olah, J.1    Tokesi, N.2    Vincze, O.3    Horvath, I.4
  • 30
    • 34347332414 scopus 로고    scopus 로고
    • Proteomics analysis of the Alzheimer's disease hippocampal proteome
    • Sultana, R., Boyd-Kimball, D., Cai, J., Pierce, W. M. et al., Proteomics analysis of the Alzheimer's disease hippocampal proteome. J. Alzheimers Dis. 2007, 11, 153-164.
    • (2007) J. Alzheimers Dis , vol.11 , pp. 153-164
    • Sultana, R.1    Boyd-Kimball, D.2    Cai, J.3    Pierce, W.M.4
  • 31
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G., Wong, C. W., Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 1984, 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 32
  • 33
    • 0035997249 scopus 로고    scopus 로고
    • Senile plaque composition and posttranslational modification of amyloid-beta peptide and associated proteins
    • Atwood, C. S., Martins, R. N., Smith, M. A., Perry, G., Senile plaque composition and posttranslational modification of amyloid-beta peptide and associated proteins. Peptides 2002, 23, 1343-1350.
    • (2002) Peptides , vol.23 , pp. 1343-1350
    • Atwood, C.S.1    Martins, R.N.2    Smith, M.A.3    Perry, G.4
  • 34
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production
    • Pastorino, L., Sun, A., Lu, P. J., Zhou, X. Z. et al., The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 2006, 440, 528-534.
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1    Sun, A.2    Lu, P.J.3    Zhou, X.Z.4
  • 35
    • 4344570364 scopus 로고    scopus 로고
    • Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection
    • Liao, L., Cheng, D., Wang, J., Duong, D. M. et al., Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J. Biol. Chem. 2004, 279, 37061-37068.
    • (2004) J. Biol. Chem , vol.279 , pp. 37061-37068
    • Liao, L.1    Cheng, D.2    Wang, J.3    Duong, D.M.4
  • 36
    • 33750440804 scopus 로고    scopus 로고
    • Cognitive decline correlates with neuropathological stage in Parkinson's disease
    • Braak, H., Rub, U., Del Tredici, K., Cognitive decline correlates with neuropathological stage in Parkinson's disease. J. Neurol. Sci. 2006, 248, 255-258.
    • (2006) J. Neurol. Sci , vol.248 , pp. 255-258
    • Braak, H.1    Rub, U.2    Del Tredici, K.3
  • 37
    • 42949173485 scopus 로고    scopus 로고
    • Mortalin: A protein associated with progression of Parkinson disease?
    • Shi, M., Jin, J., Wang, Y., Beyer, R. P. et al., Mortalin: A protein associated with progression of Parkinson disease? J. Neuropathol. Exp. Neurol. 2008, 67, 117-124.
    • (2008) J. Neuropathol. Exp. Neurol , vol.67 , pp. 117-124
    • Shi, M.1    Jin, J.2    Wang, Y.3    Beyer, R.P.4
  • 38
    • 33847651284 scopus 로고    scopus 로고
    • Three faces of mortalin: A housekeeper, guardian and killer
    • Kaul, S. C., Deocaris, C. C., Wadhwa, R., Three faces of mortalin: A housekeeper, guardian and killer. Exp. Gerontol. 2007, 42, 263-274.
    • (2007) Exp. Gerontol , vol.42 , pp. 263-274
    • Kaul, S.C.1    Deocaris, C.C.2    Wadhwa, R.3
  • 39
    • 33746296891 scopus 로고    scopus 로고
    • Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: Relevance to Parkinson disease
    • Jin, J., Hulette, C., Wang, Y., Zhang, T. et al., Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: Relevance to Parkinson disease. Mol. Cell. Proteomics 2006, 5, 1193-1204.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1193-1204
    • Jin, J.1    Hulette, C.2    Wang, Y.3    Zhang, T.4
  • 40
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba, M., Nakajo, S., Tu, P. H., Tomita, T. et al., Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol. 1998, 152, 879-884.
    • (1998) Am. J. Pathol , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4
  • 41
    • 0035086103 scopus 로고    scopus 로고
    • Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders
    • Trojanowski, J. Q., Lee, V. M., Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders. J. Alzheimers Dis. 2001, 3, 117-119.
    • (2001) J. Alzheimers Dis , vol.3 , pp. 117-119
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 42
    • 33645728523 scopus 로고    scopus 로고
    • Neurodegenerative diseases: New concepts of pathogenesis and their therapeutic implications
    • Skovronsky, D. M., Lee, V. M., Trojanowski, J. Q., Neurodegenerative diseases: New concepts of pathogenesis and their therapeutic implications. Annu. Rev. Pathol. 2006, 1, 151-170.
    • (2006) Annu. Rev. Pathol , vol.1 , pp. 151-170
    • Skovronsky, D.M.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 43
    • 27744493923 scopus 로고    scopus 로고
    • Proteomic determination of widespread detergent-insolubility including Abeta but not tau early in the pathogenesis of Alzheimer's disease
    • Woltjer, R. L., Cimino, P. J., Boutte, A. M., Schantz, A. M. et al., Proteomic determination of widespread detergent-insolubility including Abeta but not tau early in the pathogenesis of Alzheimer's disease. FASEB J. 2005, 19, 1923-1925.
    • (2005) FASEB J , vol.19 , pp. 1923-1925
    • Woltjer, R.L.1    Cimino, P.J.2    Boutte, A.M.3    Schantz, A.M.4
  • 44
    • 34548845831 scopus 로고    scopus 로고
    • Quantitative proteomics identifies surfactant-resistant alpha-synuclein in cerebral cortex of Parkinsonism-dementia complex of Guam but not Alzheimer's disease or progressive supranuclear palsy
    • Yang, W., Woltjer, R. L., Sokal, I., Pan, C. et al., Quantitative proteomics identifies surfactant-resistant alpha-synuclein in cerebral cortex of Parkinsonism-dementia complex of Guam but not Alzheimer's disease or progressive supranuclear palsy. Am. J. Pathol. 2007, 171, 993-1002.
    • (2007) Am. J. Pathol , vol.171 , pp. 993-1002
    • Yang, W.1    Woltjer, R.L.2    Sokal, I.3    Pan, C.4
  • 45
    • 33646254380 scopus 로고    scopus 로고
    • Characterization of tau pathologies in gray and whitematter of Guam parkinsonism-dementia complex
    • Winton, M. J., Joyce, S., Zhukareva, V., Practico, D. et al., Characterization of tau pathologies in gray and whitematter of Guam parkinsonism-dementia complex. Acta Neuropathol. (Berl.) 2006, 111, 401-412.
    • (2006) Acta Neuropathol. (Berl.) , vol.111 , pp. 401-412
    • Winton, M.J.1    Joyce, S.2    Zhukareva, V.3    Practico, D.4
  • 46
    • 2942656929 scopus 로고    scopus 로고
    • Occurrence of alpha-synuclein pathology in the cerebellum of Guamanian patients with parkinsonism-dementia complex
    • Sebeo, J., Hof, P. R., Perl, D. P., Occurrence of alpha-synuclein pathology in the cerebellum of Guamanian patients with parkinsonism-dementia complex. Acta Neuropathol. 2004, 107, 497-503.
    • (2004) Acta Neuropathol , vol.107 , pp. 497-503
    • Sebeo, J.1    Hof, P.R.2    Perl, D.P.3
  • 47
    • 0036092271 scopus 로고    scopus 로고
    • Tau and alpha-synuclein pathology in amygdala of Parkinsonism-dementia complex patients of Guam
    • Forman, M. S., Schmidt, M. L., Kasturi, S., Perl, D. P. et al., Tau and alpha-synuclein pathology in amygdala of Parkinsonism-dementia complex patients of Guam. Am. J. Pathol. 2002, 160, 1725-1731.
    • (2002) Am. J. Pathol , vol.160 , pp. 1725-1731
    • Forman, M.S.1    Schmidt, M.L.2    Kasturi, S.3    Perl, D.P.4
  • 48
    • 0033936784 scopus 로고    scopus 로고
    • Alphasynuclein inclusions in amygdala in the brains of patients with the parkinsonism-dementia complex of Guam
    • Yamazaki, M., Arai, Y., Baba, M., Iwatsubo, T. et al., Alphasynuclein inclusions in amygdala in the brains of patients with the parkinsonism-dementia complex of Guam. J. Neuropathol. Exp. Neurol. 2000, 59, 585-591.
    • (2000) J. Neuropathol. Exp. Neurol , vol.59 , pp. 585-591
    • Yamazaki, M.1    Arai, Y.2    Baba, M.3    Iwatsubo, T.4
  • 49
    • 34250928307 scopus 로고
    • Distribution of noradrenaline and dopamine (3-hydroxytyramine) in the human brain and their behavior in diseases of the extrapyramidal system
    • Ehringer, H., Hornykiewicz, O., Distribution of noradrenaline and dopamine (3-hydroxytyramine) in the human brain and their behavior in diseases of the extrapyramidal system. Klin. Wochenschr. 1960, 38, 1236-1239.
    • (1960) Klin. Wochenschr , vol.38 , pp. 1236-1239
    • Ehringer, H.1    Hornykiewicz, O.2
  • 50
    • 10644277894 scopus 로고    scopus 로고
    • Proteome analysis of human substantia nigra in Parkinson's disease
    • Basso, M., Giraudo, S., Corpillo, D., Bergamasco, B. et al., Proteome analysis of human substantia nigra in Parkinson's disease. Proteomics 2004, 4, 3943-3952.
    • (2004) Proteomics , vol.4 , pp. 3943-3952
    • Basso, M.1    Giraudo, S.2    Corpillo, D.3    Bergamasco, B.4
  • 51
    • 33747409456 scopus 로고    scopus 로고
    • Detection of biomarkers with a multiplex quantitative proteomic platform in cerebrospinal fluid of patients with neurodegenerative disorders
    • Abdi, F., Quinn, J. F., Jankovic, J., McIntosh, M. et al., Detection of biomarkers with a multiplex quantitative proteomic platform in cerebrospinal fluid of patients with neurodegenerative disorders. J. Alzheimers Dis. 2006, 9, 293-348.
    • (2006) J. Alzheimers Dis , vol.9 , pp. 293-348
    • Abdi, F.1    Quinn, J.F.2    Jankovic, J.3    McIntosh, M.4
  • 52
    • 0026753557 scopus 로고
    • Mitochondrial function in Parkinson's disease. The Royal Kings and Queens Parkinson's Disease Research Group
    • Schapira, A. H., Mann, V. M., Cooper, J. M., Krige, D. et al., Mitochondrial function in Parkinson's disease. The Royal Kings and Queens Parkinson's Disease Research Group. Ann. Neurol. 1992, 32, S116-S124.
    • (1992) Ann. Neurol , vol.32
    • Schapira, A.H.1    Mann, V.M.2    Cooper, J.M.3    Krige, D.4
  • 53
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-S38
    • Jenner, P., Oxidative stress in Parkinson's disease. Ann. Neurol. 2003, 53, S26-36; discussion S36-S38.
    • (2003) Ann. Neurol , vol.53
    • Jenner, P.1
  • 55
    • 1942454250 scopus 로고    scopus 로고
    • Inflammation and neurodegeneration in Parkinson's disease
    • McGeer, P. L., McGeer, E. G., Inflammation and neurodegeneration in Parkinson's disease. Parkinsonism Relat. Disord. 2004, 10, S3-S7.
    • (2004) Parkinsonism Relat. Disord , vol.10
    • McGeer, P.L.1    McGeer, E.G.2
  • 56
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D. et al., Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 2004, 279, 13256-13264.
    • (2004) J. Biol. Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4
  • 57
    • 33646826619 scopus 로고    scopus 로고
    • Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases
    • Choi, J., Sullards, M. C., Olzmann, J. A., Rees, H. D. et al., Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases. J. Biol. Chem. 2006, 281, 10816-10824.
    • (2006) J. Biol. Chem , vol.281 , pp. 10816-10824
    • Choi, J.1    Sullards, M.C.2    Olzmann, J.A.3    Rees, H.D.4
  • 58
    • 0038727936 scopus 로고    scopus 로고
    • Description of Parkinson's disease as a clinical syndrome
    • Fahn, S., Description of Parkinson's disease as a clinical syndrome. Ann. N. Y. Acad. Sci. 2003, 991, 1-14.
    • (2003) Ann. N. Y. Acad. Sci , vol.991 , pp. 1-14
    • Fahn, S.1
  • 59
    • 0024450903 scopus 로고
    • The functional anatomy of basal ganglia disorders
    • Albin, R. L., Young, A. B., Penney, J. B., The functional anatomy of basal ganglia disorders. Trends Neurosci. 1989, 12, 366-375.
    • (1989) Trends Neurosci , vol.12 , pp. 366-375
    • Albin, R.L.1    Young, A.B.2    Penney, J.B.3
  • 60
    • 0024379639 scopus 로고
    • Neural mechanisms in disorders of movement
    • Crossman, A. R., Neural mechanisms in disorders of movement. Comp. Biochem. Physiol. A 1989, 93, 141-149.
    • (1989) Comp. Biochem. Physiol. A , vol.93 , pp. 141-149
    • Crossman, A.R.1
  • 61
    • 0025298139 scopus 로고
    • Primate models of movement disorders of basal ganglia origin
    • DeLong, M. R., Primate models of movement disorders of basal ganglia origin. Trends Neurosci. 1990, 13, 281-285.
    • (1990) Trends Neurosci , vol.13 , pp. 281-285
    • DeLong, M.R.1
  • 62
    • 0021165054 scopus 로고
    • Oxy-radical toxicity in catecholamine neurons
    • Cohen, G., Oxy-radical toxicity in catecholamine neurons. Neurotoxicology 1984, 5, 77-82.
    • (1984) Neurotoxicology , vol.5 , pp. 77-82
    • Cohen, G.1
  • 63
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • Halliwell, B., Oxidative stress and neurodegeneration: Where are we now? J. Neurochem. 2006, 97, 1634-1658.
    • (2006) J. Neurochem , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 64
    • 0032816549 scopus 로고    scopus 로고
    • The substantia nigra of the human brain. II. Patterns of loss of dopamine-containing neurons in Parkinson's disease
    • Damier, P., Hirsch, E. C., Agid, Y., Graybiel, A. M., The substantia nigra of the human brain. II. Patterns of loss of dopamine-containing neurons in Parkinson's disease. Brain 1999, 122, 1437-1448.
    • (1999) Brain , vol.122 , pp. 1437-1448
    • Damier, P.1    Hirsch, E.C.2    Agid, Y.3    Graybiel, A.M.4
  • 65
    • 0025954066 scopus 로고
    • Ageing and Parkinson's disease: Substantia nigra regional selectivity
    • Fearnley, J. M., Lees, A. J., Ageing and Parkinson's disease: Substantia nigra regional selectivity. Brain 1991, 114, 2283-2301.
    • (1991) Brain , vol.114 , pp. 2283-2301
    • Fearnley, J.M.1    Lees, A.J.2
  • 66
    • 0025964041 scopus 로고
    • The absolute number of nerve cells in substantia nigra in normal subjects and in patients with Parkinson's disease estimated with an unbiased stereological method
    • Pakkenberg, B., Moller, A., Gundersen, H. J., Mouritzen Dam, A., Pakkenberg, H., The absolute number of nerve cells in substantia nigra in normal subjects and in patients with Parkinson's disease estimated with an unbiased stereological method. J. Neurol. Neurosurg. Psychiatry 1991, 54, 30-33.
    • (1991) J. Neurol. Neurosurg. Psychiatry , vol.54 , pp. 30-33
    • Pakkenberg, B.1    Moller, A.2    Gundersen, H.J.3    Mouritzen Dam, A.4    Pakkenberg, H.5
  • 67
    • 0023740773 scopus 로고
    • Rate of cell death in parkinsonism indicates active neuropathological process
    • McGeer, P. L., Itagaki, S., Akiyama, H., McGeer, E. G., Rate of cell death in parkinsonism indicates active neuropathological process. Ann. Neurol. 1988, 24, 574-576.
    • (1988) Ann. Neurol , vol.24 , pp. 574-576
    • McGeer, P.L.1    Itagaki, S.2    Akiyama, H.3    McGeer, E.G.4
  • 68
    • 0031105375 scopus 로고    scopus 로고
    • Specific A10 dopaminergic nuclei in the midbrain degenerate in Parkinson's disease
    • McRitchie, D. A., Cartwright, H. R., Halliday, G. M., Specific A10 dopaminergic nuclei in the midbrain degenerate in Parkinson's disease. Exp. Neurol. 1997, 144, 202-213.
    • (1997) Exp. Neurol , vol.144 , pp. 202-213
    • McRitchie, D.A.1    Cartwright, H.R.2    Halliday, G.M.3
  • 69
    • 0023830780 scopus 로고    scopus 로고
    • German, D. C., Dubach, M., Askari, S., Speciale, S. G., Bowden, D. M., 1-Methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridineinduced parkinsonian syndrome in Macaca fascicularis: Which midbrain dopaminergic neurons are lost? Neuroscience 1988, 24, 161-174.
    • German, D. C., Dubach, M., Askari, S., Speciale, S. G., Bowden, D. M., 1-Methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridineinduced parkinsonian syndrome in Macaca fascicularis: Which midbrain dopaminergic neurons are lost? Neuroscience 1988, 24, 161-174.
  • 70
    • 0028171396 scopus 로고
    • Chronic MPTP treatment reproduces in baboons the differential vulnerability of mesencephalic dopaminergic neurons observed in Parkinson's disease
    • Varastet, M., Riche, D., Maziere, M., Hantraye, P., Chronic MPTP treatment reproduces in baboons the differential vulnerability of mesencephalic dopaminergic neurons observed in Parkinson's disease. Neuroscience 1994, 63, 47-56.
    • (1994) Neuroscience , vol.63 , pp. 47-56
    • Varastet, M.1    Riche, D.2    Maziere, M.3    Hantraye, P.4
  • 71
    • 0023550354 scopus 로고    scopus 로고
    • Waters, C. M., Hunt, S. P., Jenner, P., Marsden, C. D., An immunohistochemical study of the acute and long-term effects of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in the marmoset. Neuroscience 1987, 23, 1025-1039.
    • Waters, C. M., Hunt, S. P., Jenner, P., Marsden, C. D., An immunohistochemical study of the acute and long-term effects of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine in the marmoset. Neuroscience 1987, 23, 1025-1039.
  • 72
    • 0030499311 scopus 로고    scopus 로고
    • The neurotoxin MPTP causes degeneration of specific nucleus A8, A9 and A10 dopaminergic neurons in the mouse
    • German, D. C., Nelson, E. L., Liang, C. L., Speciale, S. G. et al., The neurotoxin MPTP causes degeneration of specific nucleus A8, A9 and A10 dopaminergic neurons in the mouse. Neurodegeneration 1996, 5, 299-312.
    • (1996) Neurodegeneration , vol.5 , pp. 299-312
    • German, D.C.1    Nelson, E.L.2    Liang, C.L.3    Speciale, S.G.4
  • 73
    • 0035020470 scopus 로고    scopus 로고
    • Similarities with cell loss in parkinson's disease
    • Dopamine cell degeneration induced by intraventricular administration of 6-hydroxydopamine in the rat
    • Rodriguez, M., Barroso-Chinea, P., Abdala, P., Obeso, J., Gonzalez-Hernandez, T., Dopamine cell degeneration induced by intraventricular administration of 6-hydroxydopamine in the rat: Similarities with cell loss in parkinson's disease. Exp. Neurol. 2001, 169, 163-181.
    • (2001) Exp. Neurol , vol.169 , pp. 163-181
    • Rodriguez, M.1    Barroso-Chinea, P.2    Abdala, P.3    Obeso, J.4    Gonzalez-Hernandez, T.5
  • 74
    • 0033681149 scopus 로고    scopus 로고
    • Chronic systemic pesticide exposure reproduces features of Parkinson's disease
    • Betarbet, R., Sherer, T. B., MacKenzie, G., Garcia-Osuna, M. et al., Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat. Neurosci. 2000, 3, 1301-1306.
    • (2000) Nat. Neurosci , vol.3 , pp. 1301-1306
    • Betarbet, R.1    Sherer, T.B.2    MacKenzie, G.3    Garcia-Osuna, M.4
  • 75
    • 11844262742 scopus 로고    scopus 로고
    • Gene expression profiling of rat midbrain dopamine neurons: Implications for selective vulnerability in parkinsonism
    • Greene, J. G., Dingledine, R., Greenamyre, J. T., Gene expression profiling of rat midbrain dopamine neurons: Implications for selective vulnerability in parkinsonism. Neurobiol. Dis. 2005, 18, 19-31.
    • (2005) Neurobiol. Dis , vol.18 , pp. 19-31
    • Greene, J.G.1    Dingledine, R.2    Greenamyre, J.T.3
  • 76
    • 26444529541 scopus 로고    scopus 로고
    • Cell type-specific gene expression of midbrain dopaminergic neurons reveals molecules involved in their vulnerability and protection
    • Chung, C. Y., Seo, H., Sonntag, K. C., Brooks, A. et al., Cell type-specific gene expression of midbrain dopaminergic neurons reveals molecules involved in their vulnerability and protection. Hum. Mol. Genet. 2005, 14, 1709-1725.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1709-1725
    • Chung, C.Y.1    Seo, H.2    Sonntag, K.C.3    Brooks, A.4
  • 77
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link, A. J., Eng, J., Schieltz, D. M., Carmack, E. et al., Direct analysis of protein complexes using mass spectrometry. Nat. Biotechnol. 1999, 17, 676-682.
    • (1999) Nat. Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3    Carmack, E.4
  • 78
    • 33745626459 scopus 로고    scopus 로고
    • Improved scoring of functional groups from gene expression data by decorrelating GO graph structure
    • Alexa, A., Rahnenfuhrer, J., Lengauer, T., Improved scoring of functional groups from gene expression data by decorrelating GO graph structure. Bioinformatics 2006, 22, 1600-1607.
    • (2006) Bioinformatics , vol.22 , pp. 1600-1607
    • Alexa, A.1    Rahnenfuhrer, J.2    Lengauer, T.3
  • 79
    • 38649136201 scopus 로고    scopus 로고
    • Integrated analysis of the cerebrospinal fluid peptidome and proteome
    • Zougman, A., Pilch, B., Podtelejnikov, A., Kiehntopf, M. et al., Integrated analysis of the cerebrospinal fluid peptidome and proteome. J. Proteome Res. 2008, 7, 386-399.
    • (2008) J. Proteome Res , vol.7 , pp. 386-399
    • Zougman, A.1    Pilch, B.2    Podtelejnikov, A.3    Kiehntopf, M.4
  • 80
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O. et al., Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 2003, 299, 256-259.
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    van Baren, M.J.3    Schaap, O.4
  • 81
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E. et al., Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 1997, 276, 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4
  • 82
    • 37349038248 scopus 로고    scopus 로고
    • Dopamine transporter relation to dopamine turnover in Parkinson's disease: A positron emission tomography study
    • Sossi, V., de la Fuente-Fernandez, R., Schulzer, M., Troiano, A. R. et al., Dopamine transporter relation to dopamine turnover in Parkinson's disease: A positron emission tomography study. Ann. Neurol. 2007, 62, 468-474.
    • (2007) Ann. Neurol , vol.62 , pp. 468-474
    • Sossi, V.1    de la Fuente-Fernandez, R.2    Schulzer, M.3    Troiano, A.R.4
  • 83
    • 0033592991 scopus 로고    scopus 로고
    • Abnormal neurotransmission in mice lacking synaptic vesicle protein 2A (SV2A)
    • Crowder, K. M., Gunther, J. M., Jones, T. A., Hale, B. D. et al., Abnormal neurotransmission in mice lacking synaptic vesicle protein 2A (SV2A). Proc. Natl. Acad. Sci. USA 1999, 96, 15268-15273.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15268-15273
    • Crowder, K.M.1    Gunther, J.M.2    Jones, T.A.3    Hale, B.D.4
  • 84
    • 27144483990 scopus 로고    scopus 로고
    • Mutations in SEPT9 cause hereditary neuralgic amyotrophy
    • Kuhlenbaumer, G., Hannibal, M. C., Nelis, E., Schirmacher, A. et al., Mutations in SEPT9 cause hereditary neuralgic amyotrophy. Nat. Genet. 2005, 37, 1044-1046.
    • (2005) Nat. Genet , vol.37 , pp. 1044-1046
    • Kuhlenbaumer, G.1    Hannibal, M.C.2    Nelis, E.3    Schirmacher, A.4
  • 85
    • 33644584055 scopus 로고    scopus 로고
    • Using proteomics and network analysis to elucidate the consequences of synaptic protein oxidation in a PS1 + AbetaPP mouse model of Alzheimer's disease
    • Soreghan, B. A., Lu, B. W., Thomas, S. N., Duff, K. et al., Using proteomics and network analysis to elucidate the consequences of synaptic protein oxidation in a PS1 + AbetaPP mouse model of Alzheimer's disease. J. Alzheimers Dis. 2005, 8, 227-241.
    • (2005) J. Alzheimers Dis , vol.8 , pp. 227-241
    • Soreghan, B.A.1    Lu, B.W.2    Thomas, S.N.3    Duff, K.4
  • 86
    • 33847151166 scopus 로고    scopus 로고
    • A combined dataset of human cerebrospinal fluid proteins identified by multi-dimensional chromatography and tandem mass spectrometry
    • Pan, S., Zhu, D., Quinn, J. F., Peskind, E. R. et al., A combined dataset of human cerebrospinal fluid proteins identified by multi-dimensional chromatography and tandem mass spectrometry. Proteomics 2007, 7, 469-473.
    • (2007) Proteomics , vol.7 , pp. 469-473
    • Pan, S.1    Zhu, D.2    Quinn, J.F.3    Peskind, E.R.4
  • 87
    • 0036323020 scopus 로고    scopus 로고
    • The role of tau in Alzheimer's disease
    • Trojanowski, J. Q., Lee, V. M., The role of tau in Alzheimer's disease. Med. Clin. North Am. 2002, 86, 615-627.
    • (2002) Med. Clin. North Am , vol.86 , pp. 615-627
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 88
    • 33645116252 scopus 로고    scopus 로고
    • Farrer, M. J., Genetics of Parkinson disease: Paradigm shifts and future prospects. Nat. Rev. Genet. 2006, 7, 306-318.
    • Farrer, M. J., Genetics of Parkinson disease: Paradigm shifts and future prospects. Nat. Rev. Genet. 2006, 7, 306-318.
  • 89
    • 0022541790 scopus 로고
    • Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
    • Andersson, L., Porath, J., Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Anal. Biochem. 1986, 154, 250-254.
    • (1986) Anal. Biochem , vol.154 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 91
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y., Wolf-Yadlin, A., Ross, P. L., Pappin, D. J. et al., Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 2005, 4, 1240-1250.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4
  • 92
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J., Moritz, A., Lee, K. A., Guo, A. et al., Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23, 94-101.
    • (2005) Nat. Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4
  • 93
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T., Chait, B. T., Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 2001, 19, 379-382.
    • (2001) Nat. Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 94
    • 0036674813 scopus 로고    scopus 로고
    • A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode
    • Steen, H., Mann, M., A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode. J. Am. Soc. Mass Spectrom. 2002, 13, 996-1003.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 996-1003
    • Steen, H.1    Mann, M.2
  • 95
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J. D., Aebersold, R., A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 2001, 19, 375-378.
    • (2001) Nat. Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 96
    • 34547863477 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of neuronal cell death by glutamate-induced oxidative stress
    • Kang, T. H., Bae, K. H., Yu, M. J., Kim, W. K. et al., Phosphoproteomic analysis of neuronal cell death by glutamate-induced oxidative stress. Proteomics 2007, 7, 2624-2635.
    • (2007) Proteomics , vol.7 , pp. 2624-2635
    • Kang, T.H.1    Bae, K.H.2    Yu, M.J.3    Kim, W.K.4
  • 97
    • 33947575134 scopus 로고    scopus 로고
    • Enhancement of the efficiency of phosphoproteomic identification by removing phosphates after phosphopeptide enrichment
    • Ishihama, Y., Wei, F. Y., Aoshima, K., Sato, T. et al., Enhancement of the efficiency of phosphoproteomic identification by removing phosphates after phosphopeptide enrichment. J. Proteome Res. 2007, 6, 1139-1144.
    • (2007) J. Proteome Res , vol.6 , pp. 1139-1144
    • Ishihama, Y.1    Wei, F.Y.2    Aoshima, K.3    Sato, T.4
  • 98
    • 17444413094 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of synaptosomes from human cerebral cortex
    • DeGiorgis, J. A., Jaffe, H., Moreira, J. E., Carlotti, C. G., Jr. et al., Phosphoproteomic analysis of synaptosomes from human cerebral cortex. J. Proteome Res. 2005, 4, 306-315.
    • (2005) J. Proteome Res , vol.4 , pp. 306-315
    • DeGiorgis, J.A.1    Jaffe, H.2    Moreira, J.E.3    Carlotti Jr., C.G.4
  • 99
    • 33847778786 scopus 로고    scopus 로고
    • Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry
    • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J. et al., Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc. Natl. Acad. Sci. USA 2007, 104, 2193-2198.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2193-2198
    • Chi, A.1    Huttenhower, C.2    Geer, L.Y.3    Coon, J.J.4
  • 100
    • 33845435463 scopus 로고    scopus 로고
    • The utility of ETD mass spectrometry in proteomic analysis
    • Mikesh, L.M., Ueberheide, B., Chi, A., Coon, J. J. et al., The utility of ETD mass spectrometry in proteomic analysis. Biochim. Biophys. Acta 2006, 1764, 1811-1822.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1811-1822
    • Mikesh, L.M.1    Ueberheide, B.2    Chi, A.3    Coon, J.J.4
  • 101
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev, R. A., Electron-capture dissociation tandem mass spectrometry. Curr. Opin. Biotechnol. 2004, 15, 12-16.
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 102
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • Ross, C. A., Pickart, C. M., The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol. 2004, 14, 703-711.
    • (2004) Trends Cell Biol , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 103
    • 2242472974 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions
    • Hasegawa, M., Fujiwara, H., Nonaka, T., Wakabayashi, K. et al., Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions. J. Biol. Chem. 2002, 277, 49071-49076.
    • (2002) J. Biol. Chem , vol.277 , pp. 49071-49076
    • Hasegawa, M.1    Fujiwara, H.2    Nonaka, T.3    Wakabayashi, K.4
  • 104
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M. et al., Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 1993, 10, 1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4
  • 106
    • 38149046578 scopus 로고    scopus 로고
    • Ubiquitin proteasome-mediated synaptic reorganization: A novel mechanism underlying rapid ischemic tolerance
    • Meller, R., Thompson, S. J., Lusardi, T. A., Ordonez, A. N. et al., Ubiquitin proteasome-mediated synaptic reorganization: A novel mechanism underlying rapid ischemic tolerance. J. Neurosci. 2008, 28, 50-59.
    • (2008) J. Neurosci , vol.28 , pp. 50-59
    • Meller, R.1    Thompson, S.J.2    Lusardi, T.A.3    Ordonez, A.N.4
  • 107
    • 33750130282 scopus 로고    scopus 로고
    • Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach
    • Pan, S., Wang, Y., Quinn, J. F., Peskind, E. R. et al., Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach. J. Proteome Res. 2006, 5, 2769-2779.
    • (2006) J. Proteome Res , vol.5 , pp. 2769-2779
    • Pan, S.1    Wang, Y.2    Quinn, J.F.3    Peskind, E.R.4
  • 108
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura, H., Hattori, N., Kubo, S., Mizuno, Y. et al., Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 2000, 25, 302-305.
    • (2000) Nat. Genet , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Mizuno, Y.4
  • 109
    • 0035213289 scopus 로고    scopus 로고
    • Wheat germ agglutinin-binding glycoproteins are decreased in Alzheimer's disease cerebrospinal fluid
    • Fodero, L. R., Saez-Valero, J., Barquero, M. S., Marcos, A. et al., Wheat germ agglutinin-binding glycoproteins are decreased in Alzheimer's disease cerebrospinal fluid. J. Neurochem. 2001, 79, 1022-1026.
    • (2001) J. Neurochem , vol.79 , pp. 1022-1026
    • Fodero, L.R.1    Saez-Valero, J.2    Barquero, M.S.3    Marcos, A.4
  • 110
    • 33645783001 scopus 로고    scopus 로고
    • Reelin expression and glycosylation patterns are altered in Alzheimer's disease
    • Botella-Lopez, A., Burgaya, F., Gavin, R., Garcia-Ayllon, M. S. et al., Reelin expression and glycosylation patterns are altered in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2006, 103, 5573-5578.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5573-5578
    • Botella-Lopez, A.1    Burgaya, F.2    Gavin, R.3    Garcia-Ayllon, M.S.4
  • 111
    • 33748754701 scopus 로고    scopus 로고
    • Lysosome-associated membrane protein 1 (LAMP-1) in Alzheimer's disease
    • Barrachina, M., Maes, T., Buesa, C., Ferrer, I., Lysosome-associated membrane protein 1 (LAMP-1) in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 2006, 32, 505-516.
    • (2006) Neuropathol. Appl. Neurobiol , vol.32 , pp. 505-516
    • Barrachina, M.1    Maes, T.2    Buesa, C.3    Ferrer, I.4
  • 112
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: A new approach to investigate oxidative stress in Alzheimer's disease brain
    • Butterfield, D. A., Proteomics: A new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 2004, 1000, 1-7.
    • (2004) Brain Res , vol.1000 , pp. 1-7
    • Butterfield, D.A.1
  • 113
    • 29244479196 scopus 로고    scopus 로고
    • Proteomic analysis of protein expression and oxidative modification in r6/2 transgenic mice: A model of Huntington disease
    • Perluigi, M., Poon, H. F., Maragos, W., Pierce, W. M. et al., Proteomic analysis of protein expression and oxidative modification in r6/2 transgenic mice: A model of Huntington disease. Mol. Cell. Proteomics 2005, 4, 1849-1861.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1849-1861
    • Perluigi, M.1    Poon, H.F.2    Maragos, W.3    Pierce, W.M.4
  • 114
    • 14744305520 scopus 로고    scopus 로고
    • Mitochondrial associated metabolic proteins are selectively oxidized in A30P alpha-synuclein transgenic mice - a model of familial Parkinson's disease
    • Poon, H. F., Frasier, M., Shreve, N., Calabrese, V. et al., Mitochondrial associated metabolic proteins are selectively oxidized in A30P alpha-synuclein transgenic mice - a model of familial Parkinson's disease. Neurobiol. Dis. 2005, 18, 492-498.
    • (2005) Neurobiol. Dis , vol.18 , pp. 492-498
    • Poon, H.F.1    Frasier, M.2    Shreve, N.3    Calabrese, V.4
  • 115
    • 0037434994 scopus 로고    scopus 로고
    • Constellations in a cellular universe
    • Aebersold, R., Constellations in a cellular universe. Nature 2003, 422, 115-116.
    • (2003) Nature , vol.422 , pp. 115-116
    • Aebersold, R.1
  • 116
    • 14944367554 scopus 로고    scopus 로고
    • High throughput proteome screening for biomarker detection
    • Pan, S., Zhang, H., Rush, J., Eng, J. et al., High throughput proteome screening for biomarker detection. Mol. Cell. Proteomics 2005, 4, 182-190.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 182-190
    • Pan, S.1    Zhang, H.2    Rush, J.3    Eng, J.4
  • 117
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., Gygi, S. P., Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 2003, 100, 6940-6945.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 118
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies (SISCAPA)
    • Anderson, N. L., Anderson, N. G., Haines, L. R., Hardie, D. B. et al., Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies (SISCAPA). J. Proteome Res. 2004, 3, 235-244.
    • (2004) J. Proteome Res , vol.3 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4
  • 119
    • 14844311934 scopus 로고    scopus 로고
    • Candidate-based proteomics in the search for biomarkers of cardiovascular disease
    • Anderson, L., Candidate-based proteomics in the search for biomarkers of cardiovascular disease. J. Physiol. 2005, 563, 23-60.
    • (2005) J. Physiol , vol.563 , pp. 23-60
    • Anderson, L.1
  • 120
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L., Hunter, C. L., Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 2006, 5, 573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 121
    • 39749171899 scopus 로고    scopus 로고
    • Application of targeted quantitative proteomics analysis in human cerebrospinal fluid using a liquid chromatography matrix-assisted laser desorption/ ionization time-of-flight tandem mass spectrometer (LC MALDI TOF/TOF) platform
    • Pan, S., Rush, J., Peskind, E. R., Galasko, D. et al., Application of targeted quantitative proteomics analysis in human cerebrospinal fluid using a liquid chromatography matrix-assisted laser desorption/ ionization time-of-flight tandem mass spectrometer (LC MALDI TOF/TOF) platform. J. Proteome Res. 2008, 8, 720-730.
    • (2008) J. Proteome Res , vol.8 , pp. 720-730
    • Pan, S.1    Rush, J.2    Peskind, E.R.3    Galasko, D.4


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