메뉴 건너뛰기




Volumn 2, Issue 6, 2005, Pages 901-913

How proteomics reveals potential biomarkers in brain diseases

Author keywords

2D; Alzheimer; Biomarker; Brain; DIGE; HUPO; LC; Mass spectrometry; Parkinson; Proteomics; Schizophrenia

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; BIOLOGICAL MARKER; PARKIN; TAU PROTEIN; UBIQUITIN;

EID: 28544449259     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.2.6.901     Document Type: Review
Times cited : (14)

References (150)
  • 1
    • 25144513449 scopus 로고    scopus 로고
    • CSF Biomarkers for Alzheimer's disease: Use in early diagnosis and evaluation of drug treatment
    • Blennow K. CSF Biomarkers for Alzheimer's disease: use in early diagnosis and evaluation of drug treatment. Expert Rev. Mol. Diagn. 5, 661-672 (2005).
    • (2005) Expert Rev. Mol. Diagn. , vol.5 , pp. 661-672
    • Blennow, K.1
  • 2
    • 10744229989 scopus 로고    scopus 로고
    • Neurochemical diagnosis of Alzheimer's dementia by CSF Ab42, Ab42/40 ratio and total tau
    • Lewczuk P, Esselmann H, Otto M et al. Neurochemical diagnosis of Alzheimer's dementia by CSF Ab42, Ab42/40 ratio and total tau. Neurobiol. Aging 25, 273-281 (2004).
    • (2004) Neurobiol. Aging , vol.25 , pp. 273-281
    • Lewczuk, P.1    Esselmann, H.2    Otto, M.3
  • 3
    • 14344256012 scopus 로고    scopus 로고
    • CSF protome: A protein repository for potential biomarker identification
    • Romeo MJ, Espina V, Lowenthal M et al. CSF protome: a protein repository for potential biomarker identification. Expert Rev. Proteomics 2, 57-70 (2005).
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 57-70
    • Romeo, M.J.1    Espina, V.2    Lowenthal, M.3
  • 5
    • 1842424944 scopus 로고    scopus 로고
    • The need for a public proteomics repository
    • Prince JT, Carlson MW, Wang R et al. The need for a public proteomics repository. Nature Biotechnol. 22, 471-472 (2004).
    • (2004) Nature Biotechnol. , vol.22 , pp. 471-472
    • Prince, J.T.1    Carlson, M.W.2    Wang, R.3
  • 6
    • 2442441066 scopus 로고    scopus 로고
    • Optimized sample-processing time and peptide recovery for the mass spectrometric analysis of protein digests
    • Terry DE, Umstot E, Desiderio DM. Optimized sample-processing time and peptide recovery for the mass spectrometric analysis of protein digests. J. Am. Soc. Mass Spectrom. 15, 784-794 (2004).
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 784-794
    • Terry, D.E.1    Umstot, E.2    Desiderio, D.M.3
  • 7
    • 4644364868 scopus 로고    scopus 로고
    • Cerebrospinal fluid amyloid β peptide patterns in Alzheimer's disease patients and nondemented controls depend on sample pretreatment: Indication of carrier-mediated epitope masking of amyloid β peptides
    • Bibl M, Esselmann H, Otto M et al. Cerebrospinal fluid amyloid β peptide patterns in Alzheimer's disease patients and nondemented controls depend on sample pretreatment: indication of carrier-mediated epitope masking of amyloid β peptides. Electrophoresis 25, 2912-2918 (2004).
    • (2004) Electrophoresis , vol.25 , pp. 2912-2918
    • Bibl, M.1    Esselmann, H.2    Otto, M.3
  • 8
    • 0142244516 scopus 로고    scopus 로고
    • Between-gel reproducibility of the human cerebrospinal fluid proteome
    • Terry DE, Desiderio DM. Between-gel reproducibility of the human cerebrospinal fluid proteome. Proteomics 3, 1962-1979 (2003).
    • (2003) Proteomics , vol.3 , pp. 1962-1979
    • Terry, D.E.1    Desiderio, D.M.2
  • 9
  • 10
    • 14344249723 scopus 로고    scopus 로고
    • HUPO Brain Proteome Project: Aims and needs in proteomics
    • Harnacher M, Meyer HE. HUPO Brain Proteome Project: aims and needs in proteomics. Expert Rev. Proteomics 2, 1-3 (2005).
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 1-3
    • Harnacher, M.1    Meyer, H.E.2
  • 11
    • 0141831172 scopus 로고    scopus 로고
    • Healthy aging and dementia: Findings from the Nun Study
    • Snowdon DA. Healthy aging and dementia: findings from the Nun Study. Ann. Intern. Med. 139, 450-454 (2003).
    • (2003) Ann. Intern. Med. , vol.139 , pp. 450-454
    • Snowdon, D.A.1
  • 12
    • 0029884053 scopus 로고    scopus 로고
    • Age, education, and changes in the Mini-Mental State Exam scores of older women: Findings from the Nun Study
    • Butler SM, Ashford JW, Snowdon DA. Age, education, and changes in the Mini-Mental State Exam scores of older women: findings from the Nun Study. J. Am. Geriatr. Soc. 44, 675-681 (1996).
    • (1996) J. Am. Geriatr. Soc. , vol.44 , pp. 675-681
    • Butler, S.M.1    Ashford, J.W.2    Snowdon, D.A.3
  • 13
    • 0031054674 scopus 로고    scopus 로고
    • Brain infarction and the clinical expression of Alzheimer's disease. The Nun Study
    • Snowdon DA, Greiner LH, Mortimer JA et al. Brain infarction and the clinical expression of Alzheimer's disease. The Nun Study. JAMA 277, 813-817 (1997).
    • (1997) JAMA , vol.277 , pp. 813-817
    • Snowdon, D.A.1    Greiner, L.H.2    Mortimer, J.A.3
  • 14
    • 0030964397 scopus 로고    scopus 로고
    • Aging and Alzheimer's disease: Lessons from the Nun Study
    • Snowdon DA. Aging and Alzheimer's disease: lessons from the Nun Study. Gerontologie 37, 150-156 (1997).
    • (1997) Gerontologie , vol.37 , pp. 150-156
    • Snowdon, D.A.1
  • 15
    • 2542544270 scopus 로고    scopus 로고
    • How industry is approaching the search for new diagnostic markers and biomarkers
    • Zolg JW, Langen H. How industry is approaching the search for new diagnostic markers and biomarkers. Mol. Cell. Proteomics 3, 345-354 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 345-354
    • Zolg, J.W.1    Langen, H.2
  • 16
    • 22344441685 scopus 로고    scopus 로고
    • The role of proteomics in investigating psychiatric disorders
    • Pennington K, Cotter D, Dunn M. The role of proteomics in investigating psychiatric disorders. Br. J. Psychiatry 187, 4-6 (2005).
    • (2005) Br. J. Psychiatry , vol.187 , pp. 4-6
    • Pennington, K.1    Cotter, D.2    Dunn, M.3
  • 17
    • 0035151481 scopus 로고    scopus 로고
    • Postmortem changes in the level of brain proteins
    • Fountoulakis M, Hardmeier R, Hoger H et al. Postmortem changes in the level of brain proteins. Exp. Neurol. 167, 86-94 (2001).
    • (2001) Exp. Neurol. , vol.167 , pp. 86-94
    • Fountoulakis, M.1    Hardmeier, R.2    Hoger, H.3
  • 18
    • 20844455428 scopus 로고    scopus 로고
    • Organelle proteomics of rat synaptic proteins: Correlation-profiling by isotope-coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal postsynaptic density specific proteins
    • Li K, Hornshaw MP, van Minnen J, Smalla KH, Gundelfinger ED, Smit AB. Organelle proteomics of rat synaptic proteins: correlation-profiling by isotope-coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal postsynaptic density specific proteins. J. Proteome Res. 4, 725-733 (2005).
    • (2005) J. Proteome Res. , vol.4 , pp. 725-733
    • Li, K.1    Hornshaw, M.P.2    Van Minnen, J.3    Smalla, K.H.4    Gundelfinger, E.D.5    Smit, A.B.6
  • 20
    • 22044450210 scopus 로고    scopus 로고
    • Application of fluorescence difference gel electrophoresis saturation labelling for the analysis of microdissected precursor lesions of pancreatic ductal adenocarcinoma
    • Sitek B, Luttges J, Marcus K et al. Application of fluorescence difference gel electrophoresis saturation labelling for the analysis of microdissected precursor lesions of pancreatic ductal adenocarcinoma. Proteomics 5, 2665-2679 (2005).
    • (2005) Proteomics , vol.5 , pp. 2665-2679
    • Sitek, B.1    Luttges, J.2    Marcus, K.3
  • 21
    • 0032612938 scopus 로고    scopus 로고
    • Large-gel 2D electrophoresis
    • Klose J. Large-gel 2D electrophoresis. Methods Mol. Biol. 112, 147-172 (1999).
    • (1999) Methods Mol. Biol. , vol.112 , pp. 147-172
    • Klose, J.1
  • 22
    • 0036208433 scopus 로고    scopus 로고
    • Two dimensional gel electrophoresis in proteomics: Old, old fashioned, but still climbs up the mountains
    • Rabilloud T. Two dimensional gel electrophoresis in proteomics: old, old fashioned, but still climbs up the mountains. Proteomics 2, 3-10 (2002).
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 23
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutation in mammals
    • Klose J. Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutation in mammals. Humangenetik 26, 231-233 (1975).
    • (1975) Humangenetik , vol.26 , pp. 231-233
    • Klose, J.1
  • 24
    • 84988129091 scopus 로고
    • Improved horizontal two-dimensional electrophoresis with hybrid isoelectric focusing in immobilized pH gradients in the first dimension and laying-on transfer to the second dimension
    • Görg A, Postel W, Günther S, Weser J. Improved horizontal two-dimensional electrophoresis with hybrid isoelectric focusing in immobilized pH gradients in the first dimension and laying-on transfer to the second dimension. Electrophoresis 6, 599-604 (1985).
    • (1985) Electrophoresis , vol.6 , pp. 599-604
    • Görg, A.1    Postel, W.2    Günther, S.3    Weser, J.4
  • 25
    • 0023692584 scopus 로고
    • Sodium dodecyl sulfate-gel electrophoresis: Staining of polypeptides using heavy metal salts
    • Dzandu JK, Johnson JF, Wise GE. Sodium dodecyl sulfate-gel electrophoresis: staining of polypeptides using heavy metal salts. Anal. Biochem. 174, 157-167 (1988).
    • (1988) Anal. Biochem. , vol.174 , pp. 157-167
    • Dzandu, J.K.1    Johnson, J.F.2    Wise, G.E.3
  • 26
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw J, Rowlinson R, Nickson J et al. Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics 3, 1181-1195 (2003).
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3
  • 27
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18, 2071-2077 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 28
    • 0037420424 scopus 로고    scopus 로고
    • Multi-dimensional liquid phase-based seperations in proteomics
    • Wang H, Hanash S. Multi-dimensional liquid phase-based seperations in proteomics. J. Chromatogr. B 787, 11-18 (2003).
    • (2003) J. Chromatogr. B , vol.787 , pp. 11-18
    • Wang, H.1    Hanash, S.2
  • 29
    • 0012573999 scopus 로고    scopus 로고
    • Multidimensional peptide separations in proteomics
    • Link A. Multidimensional peptide separations in proteomics. Trends Biotechnol. 20, 8-13 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 8-13
    • Link, A.1
  • 30
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D, Washburn M, Yates JR III. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683-5690 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.1    Washburn, M.2    Yates III, J.R.3
  • 31
    • 17444368353 scopus 로고    scopus 로고
    • A simplified monobuffer multidimensional chromatography for high-throughput proteome fractionation
    • Guerrier L, Lomas L, Boschetti E. A simplified monobuffer multidimensional chromatography for high-throughput proteome fractionation. J. Chromatogr. A 1073, 25-33 (2005).
    • (2005) J. Chromatogr. A , vol.1073 , pp. 25-33
    • Guerrier, L.1    Lomas, L.2    Boschetti, E.3
  • 32
    • 23944517301 scopus 로고    scopus 로고
    • A wide range of protein isoforms in serum and plasma uncovered by a quantitative intact protein analysis system
    • Misek D, Kuick R, Wang H et al. A wide range of protein isoforms in serum and plasma uncovered by a quantitative intact protein analysis system. Proteomics 5, 3343-3352 (2005).
    • (2005) Proteomics , vol.5 , pp. 3343-3352
    • Misek, D.1    Kuick, R.2    Wang, H.3
  • 33
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB. Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64-71 (1989).
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1
  • 34
    • 0343775584 scopus 로고    scopus 로고
    • Ionization in matrix-assisted laser desorption/ionization: Singly charged molecular ions are the lucky survivors
    • Karas M, Gluckmann M, Schafer J. Ionization in matrix-assisted laser desorption/ionization: singly charged molecular ions are the lucky survivors. J. Mass Spectrom. 35, 1-12 (2000).
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1-12
    • Karas, M.1    Gluckmann, M.2    Schafer, J.3
  • 35
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R, Goodlett DR. Mass spectrometry in proteomics. Chem. Rev. 101, 269-295 (2001).
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 36
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR III et al. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989 (1994).
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 37
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates III JR, Eng JK, McCormack AL, Schieltz D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67, 1426-1436 (1995).
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 38
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 39
    • 0034213595 scopus 로고    scopus 로고
    • Propound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang W, Chait BT. Propound: an expert system for protein identification using mass spectrometric peptide mapping information. Anal. Chem. 72, 2482-2489 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2
  • 40
    • 10544244161 scopus 로고    scopus 로고
    • Linking genome and proteome by mass spectrometry: LargeHscale identification of yeast proteins from two dimensional gels
    • Shevchenko A, Jensen ON, Podtelejnikov AV et al. Linking genome and proteome by mass spectrometry: largeHscale identification of yeast proteins from two dimensional gels. Proc. Natl Acad. Sci. USA 93, 14440-14445 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14440-14445
    • Shevchenko, A.1    Jensen, O.N.2    Podtelejnikov, A.V.3
  • 41
    • 0026811273 scopus 로고
    • Peptide sequencing by matrix assisted laser desorption mass spectrometry
    • Spengler B, Kirsch D. Peptide sequencing by matrix assisted laser desorption mass spectrometry. Rapid Comm. Mass Spectrom. 6, 105-108 (1992).
    • (1992) Rapid Comm. Mass Spectrom. , vol.6 , pp. 105-108
    • Spengler, B.1    Kirsch, D.2
  • 42
    • 27744536440 scopus 로고    scopus 로고
    • The last neural division: A unifying hypothesis for the pathogenisis of Alzheimer's Disease
    • Nagy Z. The last neural division: a unifying hypothesis for the pathogenisis of Alzheimer's Disease. J. Cell Mol. Med. 9, 531-541 (2005).
    • (2005) J. Cell Mol. Med. , vol.9 , pp. 531-541
    • Nagy, Z.1
  • 44
    • 0023105114 scopus 로고
    • The precursors of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A et al. The precursors of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736 (1987).
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 45
    • 0027333557 scopus 로고
    • Cellular processing of β-amyolid precursor protein and the genesis of amyloid β-peptide
    • Haas C, Selkoe DJ. Cellular processing of β-amyolid precursor protein and the genesis of amyloid β-peptide. Cell 75, 1039-1042 (1993).
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haas, C.1    Selkoe, D.J.2
  • 46
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyolid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT Jr. The carboxy terminus of the β-amyolid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 47
    • 0028915895 scopus 로고
    • Amyloid β-protein (A β) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A40 or Aβ42(43)
    • Gravina SA, Ho L, Eckman CB et al. Amyloid β-protein (A β) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A40 or Aβ42(43). J. Biol. Chem. 270, 7013-7016 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3
  • 48
    • 0030064140 scopus 로고    scopus 로고
    • Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of Aβ42(43) and association of Aβ40 with cored plaques
    • Fukumoto H, Asami-Odaka A, Suzuki N, Shimada H, Ihara Y, Iwatsubo T. Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of Aβ42(43) and association of Aβ40 with cored plaques. Am. J. Pathol. 148, 259-265 (1996).
    • (1996) Am. J. Pathol. , vol.148 , pp. 259-265
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Shimada, H.4    Ihara, Y.5    Iwatsubo, T.6
  • 49
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monodonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monodonals: evidence that an initially deposited species is Aβ42(43). Neuron 13,45-53 (1994).
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 50
    • 0028096692 scopus 로고
    • Biochemical evidence for the long-tail form (Aβ 1-42/43) of amyloid β protein as a seed molecule cerebral deposits of Alzheimer's disease
    • Tamaoka A, Kondo T, Odaka A et al. Biochemical evidence for the long-tail form (Aβ 1-42/43) of amyloid β protein as a seed molecule cerebral deposits of Alzheimer's disease. Biochem. Biophys. Res. Commun. 205, 834-842 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 834-842
    • Tamaoka, A.1    Kondo, T.2    Odaka, A.3
  • 51
    • 0028982454 scopus 로고
    • Reduction of β-amyloid peptide 42 in the cerebrospinal fluid of patients with Alzheimer's disease
    • Motter R, Vigo-Pelfrey C, Kholodenko D et al. Reduction of β-amyloid peptide 42 in the cerebrospinal fluid of patients with Alzheimer's disease. Ann. Neurol. 38, 643-648 (1995).
    • (1995) Ann. Neurol. , vol.38 , pp. 643-648
    • Motter, R.1    Vigo-Pelfrey, C.2    Kholodenko, D.3
  • 52
    • 0002683274 scopus 로고    scopus 로고
    • Development of a specific diagnostic test for measurement of β-amyloid (1-42) in CSF
    • Fisher A, Hanin I, Yoshida M (Eds), Plenum, NY, USA
    • Vanderstichele H, Blennow K, D'Heuvaert N et al. Development of a specific diagnostic test for measurement of β-amyloid (1-42) in CSF. In: Progress in Alzheimer's and Parkinsons Disease. Fisher A, Hanin I, Yoshida M (Eds) 773-778, Plenum, NY, USA (1998).
    • (1998) Progress in Alzheimer's and Parkinsons Disease , pp. 773-778
    • Vanderstichele, H.1    Blennow, K.2    D'Heuvaert, N.3
  • 53
    • 0033975837 scopus 로고    scopus 로고
    • Plasma and cerebrospinal fluid levels of amyloid β proteins 1-40 and 1-42 in Alzheimer's disease
    • Mehta PD, Pirttila T, Mehta SP, Sersen EA, Aisen PS, Wisniewski HM. Plasma and cerebrospinal fluid levels of amyloid β proteins 1-40 and 1-42 in Alzheimer's disease. Arch. Neurol. 57, 100-105 (2000).
    • (2000) Arch. Neurol. , vol.57 , pp. 100-105
    • Mehta, P.D.1    Pirttila, T.2    Mehta, S.P.3    Sersen, E.A.4    Aisen, P.S.5    Wisniewski, H.M.6
  • 54
    • 0037514257 scopus 로고    scopus 로고
    • Decreased β-amyloid 1-42 and increased tau level in cerebrospinal fluid of patients with Alzheimer's disease
    • Sunderland T, Linker G, Mirza N et al. Decreased β-amyloid 1-42 and increased tau level in cerebrospinal fluid of patients with Alzheimer's disease. JAMA 289, 2094-2103 (2003).
    • (2003) JAMA , vol.289 , pp. 2094-2103
    • Sunderland, T.1    Linker, G.2    Mirza, N.3
  • 55
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Hartmann T, Pantel J et al. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271, 22908-22914 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3
  • 56
    • 0030831053 scopus 로고    scopus 로고
    • Cerebral changes and cerebrospinal fluid β-amyloid in Alzheimer's disease: A study with quantitative magnetic resonance imaging
    • Schroder J, Pantel J, Ida N et al. Cerebral changes and cerebrospinal fluid β-amyloid in Alzheimer's disease: a study with quantitative magnetic resonance imaging. Mol. Psychiatry 2, 505-507 (1997).
    • (1997) Mol. Psychiatry , vol.2 , pp. 505-507
    • Schroder, J.1    Pantel, J.2    Ida, N.3
  • 57
    • 18444393054 scopus 로고    scopus 로고
    • Highly conserved and disease-specific patterns of carboxyterminally truncated Aβ peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation
    • Wiltfang J, Esselmann H, Bibl M et al. Highly conserved and disease-specific patterns of carboxyterminally truncated Aβ peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation. J. Neurochem. 81, 481-496 (2002).
    • (2002) J. Neurochem. , vol.81 , pp. 481-496
    • Wiltfang, J.1    Esselmann, H.2    Bibl, M.3
  • 58
    • 0038268072 scopus 로고    scopus 로고
    • The amyloid-β (Aβ) peptide pattern in cerebrospinal fluid in Alzheimer's disease: Evidence of a novel carboxyterminally elongated Aβ peptide
    • Lewczuk P, Esselmann H, Meyer M et al. The amyloid-β (Aβ) peptide pattern in cerebrospinal fluid in Alzheimer's disease: evidence of a novel carboxyterminally elongated Aβ peptide. Rapid Commun. Mass Spectrom. 17, 1291-1296 (2003).
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1291-1296
    • Lewczuk, P.1    Esselmann, H.2    Meyer, M.3
  • 59
    • 14444269228 scopus 로고    scopus 로고
    • Longitudinal study of cerebrospinal fluid levels of tau, Aβ1-40 and Aβ-42(43) in Alzheimer's disease: A study in Japan
    • Kanai M, Matsubara E, Isoe K et al. Longitudinal study of cerebrospinal fluid levels of tau, Aβ1-40 and Aβ-42(43) in Alzheimer's disease: a study in Japan. Ann. Neurol Sci 44, 17-26 (1998).
    • (1998) Ann. Neurol Sci , vol.44 , pp. 17-26
    • Kanai, M.1    Matsubara, E.2    Isoe, K.3
  • 60
    • 0032581113 scopus 로고    scopus 로고
    • Combination assay of CSF tau. Aβ1-40 and Aβ1-42(43) as a biochemical marker of Alzheimer's disease
    • Shoji M, Matsubara E, Kanai M et al. Combination assay of CSF tau. Aβ1-40 and Aβ1-42(43) as a biochemical marker of Alzheimer's disease.J. Neurol. Sci. 158, 134-140 (1998).
    • (1998) J. Neurol. Sci. , vol.158 , pp. 134-140
    • Shoji, M.1    Matsubara, E.2    Kanai, M.3
  • 61
    • 0034027642 scopus 로고    scopus 로고
    • Age-dependent change in the levels of Aβ40 and Aβ42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of Aβ42 to Aβ40 level in cerebrospinal fluid from Alzheimer's disease patients
    • Fukuyama R, Mizuno T, Mori S, Nakajima K, Fushiki S, Yanagisawa K. Age-dependent change in the levels of Aβ40 and Aβ42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of Aβ42 to Aβ40 level in cerebrospinal fluid from Alzheimer's disease patients. Eur. Neurol. 43, 155-160 (2000).
    • (2000) Eur. Neurol. , vol.43 , pp. 155-160
    • Fukuyama, R.1    Mizuno, T.2    Mori, S.3    Nakajima, K.4    Fushiki, S.5    Yanagisawa, K.6
  • 62
    • 0037465449 scopus 로고    scopus 로고
    • CSF Aβ42 levels correlate with amyloid-neuropathology in a population-based autopsy study
    • Strozyk D, Blennow K, White LR, Launer LJ. CSF Aβ42 levels correlate with amyloid-neuropathology in a population-based autopsy study. Neurology 60, 652-656 (2003).
    • (2003) Neurology , vol.60 , pp. 652-656
    • Strozyk, D.1    Blennow, K.2    White, L.R.3    Launer, L.J.4
  • 63
    • 0031947586 scopus 로고    scopus 로고
    • Cerebrospinal fluid tau protein as a biochemical marker for Alzheimer's disease: A community-based follow-up study
    • Andreasen N, Vanmechelen E, Van de Voorde A et al. Cerebrospinal fluid tau protein as a biochemical marker for Alzheimer's disease: a community-based follow-up study. J. Neurol. Neurosurg. Psychiatry 64, 298-305 (1998).
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.64 , pp. 298-305
    • Andreasen, N.1    Vanmechelen, E.2    Van De Voorde, A.3
  • 64
    • 0034899223 scopus 로고    scopus 로고
    • Large-scale, multicenter study of cerebrospinal fluid tau protein phosphorylated at serine 199 for the antemortem diagnosis of Alzheimer's disease
    • Itoh N, Arai H, Urakami K et al. Large-scale, multicenter study of cerebrospinal fluid tau protein phosphorylated at serine 199 for the antemortem diagnosis of Alzheimer's disease. Ann. Neurol. 50, 150-156 (2001).
    • (2001) Ann. Neurol. , vol.50 , pp. 150-156
    • Itoh, N.1    Arai, H.2    Urakami, K.3
  • 65
    • 0033618534 scopus 로고    scopus 로고
    • Phosphorylated tau in human cerebrospinal fluid is a diagnostic marker for Alzheimer's disease
    • Ishiguro K, Ohno H, Arai H et al. Phosphorylated tau in human cerebrospinal fluid is a diagnostic marker for Alzheimer's disease. Neurosci. Lett. 270, 91-94 (1999).
    • (1999) Neurosci. Lett. , vol.270 , pp. 91-94
    • Ishiguro, K.1    Ohno, H.2    Arai, H.3
  • 66
    • 0034733918 scopus 로고    scopus 로고
    • Detection of tau phosphorylated at threonine 231 in cerebrospinal fluid of Alzheimer's disease patients
    • Kohnken R, Buerger K, Zinkowski R et al. Detection of tau phosphorylated at threonine 231 in cerebrospinal fluid of Alzheimer's disease patients. Neurosci. Lett. 287, 187-190 (2000).
    • (2000) Neurosci. Lett. , vol.287 , pp. 187-190
    • Kohnken, R.1    Buerger, K.2    Zinkowski, R.3
  • 67
    • 0035066999 scopus 로고    scopus 로고
    • Tracking Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231
    • Hampel H, Buerger K, Kohnken R et al. Tracking Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231. Ann. Neurol. 49, 199-206 (2001).
    • (2001) Ann. Neurol. , vol.49 , pp. 199-206
    • Hampel, H.1    Buerger, K.2    Kohnken, R.3
  • 68
    • 0037183481 scopus 로고    scopus 로고
    • Differential diagnosis of Alzheimer's disease with cerebrospinal fluid levels of tau protein phosphorylated at threononine 231
    • Buerger K, Teipel SJ, Zinkowski R et al. Differential diagnosis of Alzheimer's disease with cerebrospinal fluid levels of tau protein phosphorylated at threononine 231. Arch. Neurol. 59, 627-629 (2002).
    • (2002) Arch. Neurol. , vol.59 , pp. 627-629
    • Buerger, K.1    Teipel, S.J.2    Zinkowski, R.3
  • 69
    • 0036107977 scopus 로고    scopus 로고
    • Levels of nonphosphorylated and phosphorylted tau in cerebrospinal fluid of Alzheimer's disease patients: An ultrasensitive bienzyme-substrate-recyde enzyme-linked immunosorbent assay
    • Hu YY. Levels of nonphosphorylated and phosphorylted tau in cerebrospinal fluid of Alzheimer's disease patients: an ultrasensitive bienzyme-substrate- recyde enzyme-linked immunosorbent assay. Am. J. Pathol. 2, 1269-1278 (2002).
    • (2002) Am. J. Pathol. , vol.2 , pp. 1269-1278
    • Hu, Y.Y.1
  • 71
    • 0036052571 scopus 로고    scopus 로고
    • Pharmacological targets to inhibit Alzheimer neurofibrillary degeneration
    • Iqbal K, Alonso Adel C, El-Akkad E et al. Pharmacological targets to inhibit Alzheimer neurofibrillary degeneration. J. Neural Transm. Suppl. 62, 309-319 (2002).
    • (2002) J. Neural Transm. Suppl. , vol.62 , pp. 309-319
    • Iqbal, K.1    Alonso Adel, C.2    El-Akkad, E.3
  • 72
    • 0033624418 scopus 로고    scopus 로고
    • Mechanism of neurofibrillary degeneration and pharmacologic therapeutic approach
    • Iqbal K, Alonso AD, Gondal JA et al. Mechanism of neurofibrillary degeneration and pharmacologic therapeutic approach. J. Neural. Transm. Suppl. 59, 213-122 (2000).
    • (2000) J. Neural. Transm. Suppl. , vol.59 , pp. 213-1122
    • Iqbal, K.1    Alonso, A.D.2    Gondal, J.A.3
  • 74
    • 1242314764 scopus 로고    scopus 로고
    • The allelic modulation of apolipoprotein e expression by oestrogen: Potential relevance for Alzheimer's disease
    • Lambert JC, Coyle N, Lendon C. The allelic modulation of apolipoprotein E expression by oestrogen: potential relevance for Alzheimer's disease. Med. Genet. 41, 104-112 (2004).
    • (2004) Med. Genet. , vol.41 , pp. 104-112
    • Lambert, J.C.1    Coyle, N.2    Lendon, C.3
  • 75
    • 0023133252 scopus 로고
    • Apolipoprotein E isoform phenotyping methodology and population frequency with identicifation of ApoE1 and ApoE5 isoforms
    • Ordovas JM. Apolipoprotein E isoform phenotyping methodology and population frequency with identicifation of ApoE1 and ApoE5 isoforms. J. Lipid Res. 28, 371-380 (1987).
    • (1987) J. Lipid Res. , vol.28 , pp. 371-380
    • Ordovas, J.M.1
  • 76
    • 0042889048 scopus 로고    scopus 로고
    • ApoE ε3/ε4 heterozygotes have an elevated proportion of apolipoprotein E4 in cerebrospinal fuid relative to plasma, independent of Alzheimer's disease diagnosis
    • Fukumoto H, Ingelsson M, Garevik N et al. ApoE ε3/ε4 heterozygotes have an elevated proportion of apolipoprotein E4 in cerebrospinal fuid relative to plasma, independent of Alzheimer's disease diagnosis. Exp. Neurol. 183, 249-253 (2003).
    • (2003) Exp. Neurol. , vol.183 , pp. 249-253
    • Fukumoto, H.1    Ingelsson, M.2    Garevik, N.3
  • 77
    • 70449628747 scopus 로고    scopus 로고
    • Identification of the apolipoprotein E4 isoform in cerebrospinal fluid with with preparative two-dimensional electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry
    • Hesse C, Nilsson Cl, Blennow K et al. Identification of the apolipoprotein E4 isoform in cerebrospinal fluid with with preparative two-dimensional electrophoresis and matrix assisted laser desorption/ionization- time of flight-mass spectrometry. Electrophoresis 22(9), 1834-1837 (2001).
    • (2001) Electrophoresis , vol.22 , Issue.9 , pp. 1834-1837
    • Hesse, Cl.1    Nilsson, C.2    Blennow, K.3
  • 78
    • 0030050286 scopus 로고    scopus 로고
    • Clinical and pathological correlates of apolipoprotein e ε4 in Alzheimer's disease
    • Gomez-Isla T, West HL, Rebeck GW et al. Clinical and pathological correlates of apolipoprotein E ε4 in Alzheimer's disease. Ann. Neurol. 39, 62-70 (1996).
    • (1996) Ann. Neurol. , vol.39 , pp. 62-70
    • Gomez-Isla, T.1    West, H.L.2    Rebeck, G.W.3
  • 79
    • 0343247789 scopus 로고    scopus 로고
    • Preferential deposition of amyloid β protein (Aβ) in the form Aβ40 in Alzheimer's disease is associated with a gene dosage effect of the apolipoprotein E E4 allele
    • Mann DM, Iwatsubo T, Pickering-Brown SM, Owen F, Saido TC, Perry RH. Preferential deposition of amyloid β protein (Aβ) in the form Aβ40 in Alzheimer's disease is associated with a gene dosage effect of the apolipoprotein E E4 allele. Neurosci. Lett. 17, 81-84 (1997).
    • (1997) Neurosci. Lett. , vol.17 , pp. 81-84
    • Mann, D.M.1    Iwatsubo, T.2    Pickering-Brown, S.M.3    Owen, F.4    Saido, T.C.5    Perry, R.H.6
  • 80
    • 0030823158 scopus 로고    scopus 로고
    • Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer's disease. A meta-analysis
    • ApoE and Alzheimer's disease Meta Analysis Consortium
    • Farrer LA, Cupples LA, Haines JL et al. Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer's disease. A meta-analysis. ApoE and Alzheimer's disease Meta Analysis Consortium. JAMA 278, 1349-1356 (1997).
    • (1997) JAMA , vol.278 , pp. 1349-1356
    • Farrer, L.A.1    Cupples, L.A.2    Haines, J.L.3
  • 82
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of β amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen FW, Kleijn DP, van den Hurk HH et al. Frameshift mutants of β amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279, 242-247 (1998).
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1    Kleijn, D.P.2    Van Den Hurk, H.H.3
  • 83
    • 0038155122 scopus 로고    scopus 로고
    • Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression
    • Hope AD, de Silva R, Fischer DF, Hol EM, van Leeuwen FW, Lees AJ. Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression. J. Neurochem. 86, 394-404 (2003).
    • (2003) J. Neurochem. , vol.86 , pp. 394-404
    • Hope, A.D.1    De Silva, R.2    Fischer, D.F.3    Hol, E.M.4    Van Leeuwen, F.W.5    Lees, A.J.6
  • 84
    • 0242611535 scopus 로고    scopus 로고
    • Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain
    • Fischer DF, De Vos RA, Van Dijk R et al. Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain. FASEB J. 17, 2014-2024 (2003).
    • (2003) FASEB J. , vol.17 , pp. 2014-2024
    • Fischer, D.F.1    De Vos, R.A.2    Van Dijk, R.3
  • 85
    • 0028013249 scopus 로고
    • Alzheimer's disease: Correlation of cerebro-spinal fluid and brain ubiquitin levels
    • Kudo T, Iqbal K, Ravid R, Swaab DF, Grundke-Iqbal I. Alzheimer's disease: correlation of cerebro-spinal fluid and brain ubiquitin levels. Brain Res. 639, 1-7 (1994).
    • (1994) Brain Res. , vol.639 , pp. 1-7
    • Kudo, T.1    Iqbal, K.2    Ravid, R.3    Swaab, D.F.4    Grundke-Iqbal, I.5
  • 86
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castgegna A, Aksenov M, Aksenova M et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol Med. 33, 562-571 (2002).
    • (2002) Free Radic. Biol Med. , vol.33 , pp. 562-571
    • Castgegna, A.1    Aksenov, M.2    Aksenova, M.3
  • 87
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and downregulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinsons and Alzheimer's diseases
    • Choi J, Levey AI, Weintraub ST et al. Oxidative modifications and downregulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinsons and Alzheimer's diseases. J. Biol. Chem. 279(13), 13256-13264 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3
  • 88
    • 0346100510 scopus 로고    scopus 로고
    • Proteomics for the identification of specifically oxidized proteins in brain: Technology and application to the study of neurodegenerative disorders
    • Butterfield DA, Castegna A. Proteomics for the identification of specifically oxidized proteins in brain: technology and application to the study of neurodegenerative disorders. Amino Acids 25, 419-425 (2003).
    • (2003) Amino Acids , vol.25 , pp. 419-425
    • Butterfield, D.A.1    Castegna, A.2
  • 89
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: A new approach to investigate oxidative stress in Alzheimer's disease brain
    • Butterfield DA. Proteomics: a new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 1000, 1-7 (2004).
    • (2004) Brain Res. , vol.1000 , pp. 1-7
    • Butterfield, D.A.1
  • 90
    • 0036079419 scopus 로고    scopus 로고
    • Identification of oxidized plasma proteins in Alzheimer's disease
    • Choi J, Malakowsky CA, Talent JM et al. Identification of oxidized plasma proteins in Alzheimer's disease. Biochem. Biophys. Res. Commun. 293, 1566-1570 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1566-1570
    • Choi, J.1    Malakowsky, C.A.2    Talent, J.M.3
  • 91
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase related protein II, α-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase related protein II, α-enolase and heat shock cognate 71. J. Neurochem. 82, 1524-1532 (2002).
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3
  • 92
    • 4344570364 scopus 로고    scopus 로고
    • Proteomic amyloid plaques isolated by laser capture microdissection
    • Liao L, Cheng D, Wang J et al. Proteomic amyloid plaques isolated by laser capture microdissection. J. Biol. Chem. 279, 37061-37068 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 37061-37068
    • Liao, L.1    Cheng, D.2    Wang, J.3
  • 93
    • 0037117721 scopus 로고    scopus 로고
    • Proteome analysis of cerebrospinal fluid proteins in Alzheimer's patients
    • Davidsson P, Westman-Brinkmalm A, Nilsson CL et al. Proteome analysis of cerebrospinal fluid proteins in Alzheimer's patients. Neuroreport 13(5), 611-615 (2002).
    • (2002) Neuroreport , vol.13 , Issue.5 , pp. 611-615
    • Davidsson, P.1    Westman-Brinkmalm, A.2    Nilsson, C.L.3
  • 94
    • 0041358773 scopus 로고    scopus 로고
    • A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease
    • Carrette O, Demalte I, Scherl A et al. A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease. Proteomics 3(8), 1487-1494 (2003).
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1487-1494
    • Carrette, O.1    Demalte, I.2    Scherl, A.3
  • 95
    • 0141957321 scopus 로고    scopus 로고
    • Proteomic studies of potential cerebospinal fluid protein markers for Alzheimer's disease
    • Puchades M, Hansson SF, Nilsson CL et al. Proteomic studies of potential cerebospinal fluid protein markers for Alzheimer's disease. Brain Res. Mol Brain Res. 118(1-2), 140-146 (2003).
    • (2003) Brain Res. Mol Brain Res. , vol.118 , Issue.1-2 , pp. 140-146
    • Puchades, M.1    Hansson, S.F.2    Nilsson, C.L.3
  • 96
    • 20944443414 scopus 로고    scopus 로고
    • Quantitative proteomics of cerebrospinal fluid from patients with Alzheimer's disease
    • Zhang J, Goodlett DR, Quinn JF et al. Quantitative proteomics of cerebrospinal fluid from patients with Alzheimer's disease. J. Alzheimer's Dis. 7, 125-133 (2005).
    • (2005) J. Alzheimer's Dis. , vol.7 , pp. 125-133
    • Zhang, J.1    Goodlett, D.R.2    Quinn, J.F.3
  • 98
    • 20744435383 scopus 로고    scopus 로고
    • Molecular pathophysiology of Parkinson's disease
    • Moore DJ, West AB, Dawson VL et al. Molecular pathophysiology of Parkinson's disease. Ann. Rev. Neurosci. 28, 57-87 (2005).
    • (2005) Ann. Rev. Neurosci. , vol.28 , pp. 57-87
    • Moore, D.J.1    West, A.B.2    Dawson, V.L.3
  • 99
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S. Parkinson's disease: mechanisms and models. Neuron 39, 889-909 (2003).
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 100
    • 3142523288 scopus 로고    scopus 로고
    • Genetic clues to the pathogenesis of Parkinsons disease
    • Vila M, Przedborski S. Genetic clues to the pathogenesis of Parkinsons disease. Nature Med. 10, 58-62 (2004).
    • (2004) Nature Med. , vol.10 , pp. 58-62
    • Vila, M.1    Przedborski, S.2
  • 101
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • Braak H, DelTridici K, Rub U et al. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol. Aging 24, 197-211 (2003).
    • (2003) Neurobiol. Aging , vol.24 , pp. 197-211
    • Braak, H.1    DelTridici, K.2    Rub, U.3
  • 102
    • 0033969735 scopus 로고    scopus 로고
    • Altered redox state of platelet coenzyme Q1O in Parkinson's disease
    • Gotz ME, Gerstner A, Harth R et al. Altered redox state of platelet coenzyme Q1O in Parkinson's disease. J. Neural Transm. 107, 41-48 (2000).
    • (2000) J. Neural Transm. , vol.107 , pp. 41-48
    • Gotz, M.E.1    Gerstner, A.2    Harth, R.3
  • 103
    • 0036197296 scopus 로고    scopus 로고
    • Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy
    • Kikuchi A, Takeda A, Onodera H et al. Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy. Neurobiol Dis, 9, 244-248 (2002).
    • (2002) Neurobiol Dis , vol.9 , pp. 244-248
    • Kikuchi, A.1    Takeda, A.2    Onodera, H.3
  • 104
    • 0033020233 scopus 로고    scopus 로고
    • Effects of cerebrospinal fluids from patients with Parkinson's disease on dopaminergic cells
    • Le WD, Rowe D, Jankovic J et al. Effects of cerebrospinal fluids from patients with Parkinson's disease on dopaminergic cells. Arch. Neurol. 56, 194-200 (1999).
    • (1999) Arch. Neurol. , vol.56 , pp. 194-200
    • Le, W.D.1    Rowe, D.2    Jankovic, J.3
  • 106
    • 10744221260 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant A53T human α-synuclein show neuronal dysfunction in the absence of aggregate formation
    • Gispert S, Del Turco D, Garrett L et al. Transgenic mice expressing mutant A53T human α-synuclein show neuronal dysfunction in the absence of aggregate formation. Mol. Cell. Neurosci. 24, 419-429 (2003).
    • (2003) Mol. Cell. Neurosci. , vol.24 , pp. 419-429
    • Gispert, S.1    Del Turco, D.2    Garrett, L.3
  • 107
  • 108
    • 0345269757 scopus 로고    scopus 로고
    • Nigrostriatal α-synucleinopathy induced by viral vector-mediated overexpression of human α-synuclein
    • Kirik D, Annett LE, Burger C et al. Nigrostriatal α-synucleinopathy induced by viral vector-mediated overexpression of human α-synuclein. Proc. Natl. Acad. Sci. USA 100, 2884-2889 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2884-2889
    • Kirik, D.1    Annett, L.E.2    Burger, C.3
  • 109
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight to α-synuclein biology and pathobiology
    • Outerio TF, Lindquist S. Yeast cells provide insight to α-synuclein biology and pathobiology. Science 302, 1772-1775 (2003).
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outerio, T.F.1    Lindquist, S.2
  • 110
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilisation by protofibrillar α-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles MJ, Lansbury PT, Rochet JC et al. Vesicle permeabilisation by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40, 7812-7819 (2001).
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lansbury, P.T.2    Rochet, J.C.3
  • 111
    • 0031824780 scopus 로고    scopus 로고
    • α-synuclein in neurodegenerative disorders
    • Mezey E, Dehejia A, Harta G et al. α-synuclein in neurodegenerative disorders. Nature Med. 4, 755-757 (1998).
    • (1998) Nature Med. , vol.4 , pp. 755-757
    • Mezey, E.1    Dehejia, A.2    Harta, G.3
  • 112
    • 0031715399 scopus 로고    scopus 로고
    • Accumulation of α-synuclein/NACP is a cytophatological feature common to Lewy body disease and multiple system atrophy
    • Wakabayashi K, Hayashi S, Kakita A et al. Accumulation of α-synuclein/NACP is a cytophatological feature common to Lewy body disease and multiple system atrophy. Acta Neuropathol. 96, 445-452 (1998).
    • (1998) Acta Neuropathol. , vol.96 , pp. 445-452
    • Wakabayashi, K.1    Hayashi, S.2    Kakita, A.3
  • 113
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile Parkinsonism
    • Kitada T, Asakawa S, Hattori N et al. Mutations in the parkin gene cause autosomal recessive juvenile Parkinsonism. Nature 392, 605-608 (1998).
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 114
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of doperminergic neurons
    • Goldberg MS, Fleming SM, Palacino JJ et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of doperminergic neurons. J. Biol Chem. 278, 43628-43635 (2003).
    • (2003) J. Biol Chem. , vol.278 , pp. 43628-43635
    • Goldberg, M.S.1    Fleming, S.M.2    Palacino, J.J.3
  • 115
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino JJ, Sagi D, Goldberg MS et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J. Biol. Chem. 279, 18614-18622 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 18614-18622
    • Palacino, J.J.1    Sagi, D.2    Goldberg, M.S.3
  • 116
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkins protective function
    • Chung KK, Thomas B, Li X et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkins protective function. Science 304, 1328-1331 (2004).
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3
  • 117
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinsons disease
    • Leroy E, Boyer R, Auburger G et al. The ubiquitin pathway in Parkinsons disease. Nature 392, 451-452 (1998).
    • (1998) Nature , vol.392 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3
  • 118
    • 12144289221 scopus 로고    scopus 로고
    • UCH-L1 is a Parkinson's disease susceptibility gene
    • Maraganore DM, Lesnick TG, Elbaz A et al. UCH-L1 is a Parkinson's disease susceptibility gene. Ann. Neurol. 55, 512-521 (2004).
    • (2004) Ann. Neurol. , vol.55 , pp. 512-521
    • Maraganore, D.M.1    Lesnick, T.G.2    Elbaz, A.3
  • 119
    • 0032846416 scopus 로고    scopus 로고
    • Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice
    • Saigoh K, Wang YL, Suh JG et al. Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. Nature Genet. 23, 47-51 (1999).
    • (1999) Nature Genet. , vol.23 , pp. 47-51
    • Saigoh, K.1    Wang, Y.L.2    Suh, J.G.3
  • 120
    • 0037426917 scopus 로고    scopus 로고
    • Pathways to Parkinsonism
    • Cookson MR. Pathways to Parkinsonism. Neuron 37, 7-10 (2003).
    • (2003) Neuron , vol.37 , pp. 7-10
    • Cookson, M.R.1
  • 122
    • 1642527499 scopus 로고    scopus 로고
    • DJ-1 has a role in anti-oxidative stress to prevent cell death
    • Taira T, Saito Y, Niki T et al. DJ-1 has a role in anti-oxidative stress to prevent cell death. EMBO Rep. 5, 213-218 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 213-218
    • Taira, T.1    Saito, Y.2    Niki, T.3
  • 123
    • 0346434141 scopus 로고    scopus 로고
    • Amissense mutation (L166P) in DJ-1, linked to familial Parkinsons disease, confers reduced protein stability and impairs homo-oligomerization
    • Moore DJ, Zhang L, Dawson TM et al. Amissense mutation (L166P) in DJ-1, linked to familial Parkinsons disease, confers reduced protein stability and impairs homo-oligomerization. J. Neurochem. 87, 1558-1567 (2003).
    • (2003) J. Neurochem. , vol.87 , pp. 1558-1567
    • Moore, D.J.1    Zhang, L.2    Dawson, T.M.3
  • 124
    • 0035068574 scopus 로고    scopus 로고
    • Localisation of a novel locus for autosomal recessive early onset parkinsonism, PARK6, on human chromosome 1p35-p36
    • Valente EM, Bentivoglio AR, Dixon PH et al. Localisation of a novel locus for autosomal recessive early onset parkinsonism, PARK6, on human chromosome 1p35-p36. Am. J. Hum. Geneti. 68, 895-900 (2001).
    • (2001) Am. J. Hum. Geneti. , vol.68 , pp. 895-900
    • Valente, E.M.1    Bentivoglio, A.R.2    Dixon, P.H.3
  • 125
    • 0242321145 scopus 로고    scopus 로고
    • BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential
    • Nakajima A, Kataoka K, Hong M et al. BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett. 201, 195-201 (2003).
    • (2003) Cancer Lett. , vol.201 , pp. 195-201
    • Nakajima, A.1    Kataoka, K.2    Hong, M.3
  • 126
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset parkinson's disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V et al. Hereditary early-onset parkinson's disease caused by mutations in PINK1. Science 304, 1158-1160 (2004).
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 127
    • 4644352414 scopus 로고    scopus 로고
    • Proteomic approaches in brain research and neuropharmacology
    • Vercauteren FG, Bergeron JJ, Vandesande F et al. Proteomic approaches in brain research and neuropharmacology. Eur. J. Pharmacol. 500, 385-398 (2004).
    • (2004) Eur. J. Pharmacol. , vol.500 , pp. 385-398
    • Vercauteren, F.G.1    Bergeron, J.J.2    Vandesande, F.3
  • 128
    • 3142724647 scopus 로고    scopus 로고
    • Neuroproteomics: Expression profiling of the brain's proteomes in health and disease
    • Kim SI, Voshol H, van OJ et al. Neuroproteomics: expression profiling of the brain's proteomes in health and disease. Neurochem Res. 29, 1317-1331 (2004).
    • (2004) Neurochem Res. , vol.29 , pp. 1317-1331
    • Kim, S.I.1    Voshol, H.2    Van, O.J.3
  • 129
    • 0033950615 scopus 로고    scopus 로고
    • Comparative proteome analysis of the hippocampus implicates chromosome 6q in schizophrenia
    • Edgar PF, Douglas JE, Cooper GJ et al. Comparative proteome analysis of the hippocampus implicates chromosome 6q in schizophrenia. Mol Psychiatry 5, 85-90 (2000).
    • (2000) Mol Psychiatry , vol.5 , pp. 85-90
    • Edgar, P.F.1    Douglas, J.E.2    Cooper, G.J.3
  • 130
    • 0037441519 scopus 로고    scopus 로고
    • Comparative genome- and proteome analysis of cerebral cortex from MK-801-treated rats
    • Paulson L, Martin P, Persson A et al. Comparative genome- and proteome analysis of cerebral cortex from MK-801-treated rats. J. Neurosci. Res. 71, 526-533 (2003).
    • (2003) J. Neurosci. Res. , vol.71 , pp. 526-533
    • Paulson, L.1    Martin, P.2    Persson, A.3
  • 131
    • 8844229540 scopus 로고    scopus 로고
    • Effects on rat thalamic proteome by acute subchronic MK-801-treatment
    • Paulson L, Martin P, Ljung E et al. Effects on rat thalamic proteome by acute subchronic MK-801-treatment. Eur. J. Pharmacol 505, 103-109 (2004).
    • (2004) Eur. J. Pharmacol , vol.505 , pp. 103-109
    • Paulson, L.1    Martin, P.2    Ljung, E.3
  • 132
    • 0035280535 scopus 로고    scopus 로고
    • Evidence for a mitochondrial oxidative phosphorylation defect in brains from patients with schizophrenia
    • Maurer I, Ziers S, Moller H et al. Evidence for a mitochondrial oxidative phosphorylation defect in brains from patients with schizophrenia. Schizophr. Res. 48, 125-136 (2001).
    • (2001) Schizophr. Res. , vol.48 , pp. 125-136
    • Maurer, I.1    Ziers, S.2    Moller, H.3
  • 133
    • 0034668907 scopus 로고    scopus 로고
    • Dopamine D2 long receptor-deficient mice display alterations in striatum-dependent functions
    • Wang Y, Xu R, Sasaoka T et al. Dopamine D2 long receptor-deficient mice display alterations in striatum-dependent functions. J. Neurosci. 20, 8305-8314 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 8305-8314
    • Wang, Y.1    Xu, R.2    Sasaoka, T.3
  • 134
    • 0035809776 scopus 로고    scopus 로고
    • Schizophrenia: Elevated mRNA for dopamine D2(Longer) receptors in frontal cortex
    • Tallerico T, Novak G, Liu IS et al. Schizophrenia: elevated mRNA for dopamine D2(Longer) receptors in frontal cortex. Brain Res. Mol Brain Res. 87, 160-165 (2001).
    • (2001) Brain Res. Mol Brain Res. , vol.87 , pp. 160-165
    • Tallerico, T.1    Novak, G.2    Liu, I.S.3
  • 135
  • 136
    • 3142745187 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in schizophrenia: Evidence for compromised brain metabolism and oxidative stress
    • Prabakaran S, Swatton JE, Ryan MM et al. Mitochondrial dysfunction in schizophrenia: evidence for compromised brain metabolism and oxidative stress. Mol Psychiatry 9, 684-697 (2004).
    • (2004) Mol Psychiatry , vol.9 , pp. 684-697
    • Prabakaran, S.1    Swatton, J.E.2    Ryan, M.M.3
  • 137
    • 22344441908 scopus 로고    scopus 로고
    • Proteome analysis of the anterior cingulate cortex in major psychiatric disorders
    • Pennigton K, Beasley CB, Dunn M et al. Proteome analysis of the anterior cingulate cortex in major psychiatric disorders. Biol. Psychiatry 55, 132-133 (2004).
    • (2004) Biol. Psychiatry , vol.55 , pp. 132-133
    • Pennigton, K.1    Beasley, C.B.2    Dunn, M.3
  • 138
    • 0032545939 scopus 로고    scopus 로고
    • Utility of the apolipoprotein E genotype in the diagnosis of Alzheimer's disease
    • Alzheimer's Disease Centers Consortium on Apolipoprotein E and Alzheimer's Disease
    • Mayeux R, Saunders AM, Shea S et al. Utility of the apolipoprotein E genotype in the diagnosis of Alzheimer's disease. Alzheimer's Disease Centers Consortium on Apolipoprotein E and Alzheimer's Disease. N. Engl. J. Med. 338, 506-511 (1998).
    • (1998) N. Engl. J. Med. , vol.338 , pp. 506-511
    • Mayeux, R.1    Saunders, A.M.2    Shea, S.3
  • 139
    • 0034892016 scopus 로고    scopus 로고
    • Highly increased CSF tau protein and decreased β-amyloid (1-42) in sporadic CJD: A discrimination from Alzheimer's disease?
    • Kapaki E, Kilidireas K, Paraskevas GP, Michalopoulou M, Patsouris E. Highly increased CSF tau protein and decreased β-amyloid (1-42) in sporadic CJD: a discrimination from Alzheimer's disease? J. Neurol. Neurosurg. Psychiatry 71, 401-403 (2001).
    • (2001) J. Neurol. Neurosurg. Psychiatry , vol.71 , pp. 401-403
    • Kapaki, E.1    Kilidireas, K.2    Paraskevas, G.P.3    Michalopoulou, M.4    Patsouris, E.5
  • 140
    • 0037154135 scopus 로고    scopus 로고
    • Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeld-Jakob disease
    • Otto M, Wiltfang J, Cepek L et al. Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeld-Jakob disease. Neurology 58, 192-197 (2002).
    • (2002) Neurology , vol.58 , pp. 192-197
    • Otto, M.1    Wiltfang, J.2    Cepek, L.3
  • 141
    • 0037837209 scopus 로고    scopus 로고
    • Phospho-tau/total tau ratio in cerebrospinal fluid discriminates Creuzfeld-Jakob disease from other dementias
    • Riemenschneider M, Wagenpfeil S, Vanderstichele H et al. Phospho-tau/total tau ratio in cerebrospinal fluid discriminates Creuzfeld-Jakob disease from other dementias. Mol Psychiatry 8, 343-347 (2003).
    • (2003) Mol Psychiatry , vol.8 , pp. 343-347
    • Riemenschneider, M.1    Wagenpfeil, S.2    Vanderstichele, H.3
  • 143
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data
    • Carr S, Aebersold R, Baldwin M et al. The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data. Mol Cell. Proteomics 3, 531-533 (2004).
    • (2004) Mol Cell. Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3
  • 145
    • 2542596176 scopus 로고    scopus 로고
    • HUPO initiatives relevant to clinical proteomics
    • Hanash S. HUPO initiatives relevant to clinical proteomics. Mol. Cell. Proteomics 3, 298-301 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 298-301
    • Hanash, S.1
  • 146
    • 14344257378 scopus 로고    scopus 로고
    • Building a foundation for the human proteome: The role of the Human Proteome Organization
    • Hanash S. Building a foundation for the human proteome: the role of the Human Proteome Organization. J. Proteome Res. 3, 197-199 (2004).
    • (2004) J. Proteome Res. , vol.3 , pp. 197-199
    • Hanash, S.1
  • 147
    • 0742323374 scopus 로고    scopus 로고
    • The HUPO PSI's molecular interaction format - A community standard for the representation of protein interaction data
    • Hermjakob H, Montecchi-Palazzi L, Bader G et al. The HUPO PSI's molecular interaction format - a community standard for the representation of protein interaction data. Nature Biotechnol. 22, 177-183 (2004).
    • (2004) Nature Biotechnol. , vol.22 , pp. 177-183
    • Hermjakob, H.1    Montecchi-Palazzi, L.2    Bader, G.3
  • 149
    • 1242339568 scopus 로고    scopus 로고
    • Common interchange standards for proteomics data: Public availability of tools and schema
    • Orchard S, Hermjakob H, Julian RK et al. Common interchange standards for proteomics data: public availability of tools and schema. Proteomics 4, 490-491 (2004).
    • (2004) Proteomics , vol.4 , pp. 490-491
    • Orchard, S.1    Hermjakob, H.2    Julian, R.K.3
  • 150
    • 3042776096 scopus 로고    scopus 로고
    • 'Does understanding the brain need proteomics and does understanding proteomics need brains?' - Second HUPO HBPP Workshop hosted in Paris
    • Harnacher M, Klose J, Rossier J et al. 'Does understanding the brain need proteomics and does understanding proteomics need brains?' - Second HUPO HBPP Workshop hosted in Paris. Proteomics 4, 1932-1934 (2004).
    • (2004) Proteomics , vol.4 , pp. 1932-1934
    • Harnacher, M.1    Klose, J.2    Rossier, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.