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Volumn 12, Issue 12, 2013, Pages 3543-3558

Alpha-Synuclein post-Translational modifications as potential biomarkers for parkinson disease and other synucleinopathies

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN;

EID: 84890574796     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.R113.032730     Document Type: Review
Times cited : (151)

References (133)
  • 1
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson's disease. First of two parts
    • Lang, A. E., and Lozano, A. M. (1998) Parkinson's disease. First of two parts. N. Engl. J. Med. 339, 1044-1053
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 2
    • 0032531924 scopus 로고    scopus 로고
    • Parkinson's disease. Second of two parts
    • Lang, A. E., and Lozano, A. M. (1998) Parkinson's disease. Second of two parts. N. Engl. J. Med. 339, 1130-1143
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1130-1143
    • Lang, A.E.1    Lozano, A.M.2
  • 6
    • 0035097503 scopus 로고    scopus 로고
    • Clinical and pathological features of a parkinsonian syndrome in a family with an ala53Thr alpha-Synuclein mutation
    • Spira, P. J., Sharpe, D. M., Halliday, G., Cavanagh, J., and Nicholson, G. A. (2001) Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alpha-synuclein mutation. Ann. Neurol. 49, 313-319
    • (2001) Ann. Neurol. , vol.49 , pp. 313-319
    • Spira, P.J.1    Sharpe, D.M.2    Halliday, G.3    Cavanagh, J.4    Nicholson, G.A.5
  • 10
    • 0036550101 scopus 로고    scopus 로고
    • Parkinson-Like neurodegeneration induced by targeted overexpression of alpha-Synuclein in the nigrostriatal system
    • Kirik, D., Rosenblad, C., Burger, C., Lundberg, C., Johansen, T. E., Muzyczka, N., Mandel, R. J., and Bjorklund, A. (2002) Parkinson-like neurodegeneration induced by targeted overexpression of alpha-synuclein in the nigrostriatal system. J. Neurosci. 22, 2780-2791
    • (2002) J. Neurosci. , vol.22 , pp. 2780-2791
    • Kirik, D.1    Rosenblad, C.2    Burger, C.3    Lundberg, C.4    Johansen, T.E.5    Muzyczka, N.6    Mandel, R.J.7    Bjorklund, A.8
  • 11
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-Synuclein mice: Implications for neurodegenerative disorders
    • Masliah, E., Rockenstein, E., Veinbergs, I., Mallory, M., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., and Mucke, L. (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 287, 1265-1269
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 19
  • 24
    • 82655171636 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein can be detected in blood plasma and is potentially a useful biomarker for parkinson's disease
    • Foulds, P. G., Mitchell, J. D., Parker, A., Turner, R., Green, G., Diggle, P., Hasegawa, M., Taylor, M., Mann, D., and Allsop, D. (2011) Phosphorylated alpha-synuclein can be detected in blood plasma and is potentially a useful biomarker for Parkinson's disease. FASEB J. 25, 4127-4137
    • (2011) FASEB J. , vol.25 , pp. 4127-4137
    • Foulds, P.G.1    Mitchell, J.D.2    Parker, A.3    Turner, R.4    Green, G.5    Diggle, P.6    Hasegawa, M.7    Taylor, M.8    Mann, D.9    Allsop, D.10
  • 25
    • 84872189834 scopus 로고    scopus 로고
    • Low CSF levels of both alphasynuclein and the alpha-Synuclein cleaving enzyme neurosin in patients with synucleinopathy
    • Wennstrom, M., Surova, Y., Hall, S., Nilsson, C., Minthon, L., Bostrom, F., Hansson, O., and Nielsen, H. M. (2013) Low CSF levels of both alphasynuclein and the alpha-synuclein cleaving enzyme neurosin in patients with synucleinopathy. PloS One 8, e53250
    • (2013) PloS One 8
    • Wennstrom, M.1    Surova, Y.2    Hall, S.3    Nilsson, C.4    Minthon, L.5    Bostrom, F.6    Hansson, O.7    Nielsen, H.M.8
  • 26
    • 84858136734 scopus 로고    scopus 로고
    • Altered CSF orexin and alpha-synuclein levels in dementia patients
    • Wennstrom, M., Londos, E., Minthon, L., and Nielsen, H. M. (2012) Altered CSF orexin and alpha-synuclein levels in dementia patients. J. Alzheimers Dis. 29, 125-132
    • (2012) J. Alzheimers Dis. , vol.29 , pp. 125-132
    • Wennstrom, M.1    Londos, E.2    Minthon, L.3    Nielsen, H.M.4
  • 33
    • 0034699375 scopus 로고    scopus 로고
    • Multiplexed particle-Based flow cytometric assays
    • Vignali, D. A. (2000) Multiplexed particle-based flow cytometric assays. J. Immunol. Methods 243, 243-255
    • (2000) J. Immunol. Methods , vol.243 , pp. 243-255
    • Vignali, D.A.1
  • 38
    • 77953716788 scopus 로고    scopus 로고
    • Differential levels of alpha-Synuclein, beta-Amyloid42 and tau in CSF between patients with dementia with lewy bodies and alzheimer's disease
    • Kasuga, K., Tokutake, T., Ishikawa, A., Uchiyama, T., Tokuda, T., Onodera, O., Nishizawa, M., and Ikeuchi, T. (2010) Differential levels of alpha-synuclein, beta-amyloid42 and tau in CSF between patients with dementia with Lewy bodies and Alzheimer's disease. J. Neurol. Neurosurg. Psychiatry 81, 608-610
    • (2010) J. Neurol. Neurosurg. Psychiatry , vol.81 , pp. 608-610
    • Kasuga, K.1    Tokutake, T.2    Ishikawa, A.3    Uchiyama, T.4    Tokuda, T.5    Onodera, O.6    Nishizawa, M.7    Ikeuchi, T.8
  • 40
    • 60349122813 scopus 로고    scopus 로고
    • Cerebrospinal fluid alpha-Synuclein does not discriminate between dementia disorders
    • Spies, P. E., Melis, R. J., Sjogren, M. J., Rikkert, M. G., and Verbeek, M. M. (2009) Cerebrospinal fluid alpha-synuclein does not discriminate between dementia disorders. J. Alzheimers Dis. 16, 363-369
    • (2009) J. Alzheimers Dis. , vol.16 , pp. 363-369
    • Spies, P.E.1    Melis, R.J.2    Sjogren, M.J.3    Rikkert, M.G.4    Verbeek, M.M.5
  • 41
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 42
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-Synuclein mutations linked to early-Onset parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T., Jr. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U.S.A. 97, 571-576
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, Jr.P.T.6
  • 43
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-Synuclein protein in human plasma as a potential biomarker for parkinson's disease
    • El-Agnaf, O. M., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., and Allsop, D. (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 20, 419-425
    • (2006) FASEB J. , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6    Schlossmacher, M.G.7    Allsop, D.8
  • 45
    • 5444249974 scopus 로고    scopus 로고
    • Overexpression of alpha-Synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-Synuclein and activation of caspase-9: Resemblance to pathogenetic changes in parkinson's disease
    • Yamada, M., Iwatsubo, T., Mizuno, Y., and Mochizuki, H. (2004) Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: resemblance to pathogenetic changes in Parkinson's disease. Journal Neurochem. 91, 451-461
    • (2004) Journal Neurochem. , vol.91 , pp. 451-461
    • Yamada, M.1    Iwatsubo, T.2    Mizuno, Y.3    Mochizuki, H.4
  • 46
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a drosophila model of Parkinson disease
    • Chen, L., and Feany, M. B. (2005) Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 8, 657-663
    • (2005) Nat. Neurosci. , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 49
    • 77955366745 scopus 로고    scopus 로고
    • Role of post-Translational modifications in modulating the structure, function and toxicity of alpha-Synuclein: Implications for parkinson's disease pathogenesis and therapies
    • Oueslati, A., Fournier, M., and Lashuel, H. A. (2010) Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies. Prog. Brain Res. 183, 115-145
    • (2010) Prog. Brain Res. , vol.183 , pp. 115-145
    • Oueslati, A.1    Fournier, M.2    Lashuel, H.A.3
  • 50
    • 81455136019 scopus 로고    scopus 로고
    • Phosphorylation of alpha-Synuclein at Y125 and S129 alters its metal binding properties: Implications for understanding the role of alphasynuclein in the pathogenesis of parkinson's disease and related disorders
    • Lu, Y., Prudent, M., Fauvet, B., Lashuel, H. A., and Girault, H. H. (2011) Phosphorylation of alpha-synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of alphasynuclein in the pathogenesis of Parkinson's disease and related disorders. ACS Chem. Neurosci. 2, 667-675
    • (2011) ACS Chem. Neurosci. , vol.2 , pp. 667-675
    • Lu, Y.1    Prudent, M.2    Fauvet, B.3    Lashuel, H.A.4    Girault, H.H.5
  • 52
    • 34147130637 scopus 로고    scopus 로고
    • Isolation of a human single chain antibody fragment against oligomeric alpha-Synuclein that inhibits aggregation and prevents alpha-Synuclein-Induced toxicity
    • Emadi, S., Barkhordarian, H., Wang, M. S., Schulz, P., and Sierks, M. R. (2007) Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha- synuclein-induced toxicity. J. Mol. Biol. 368, 1132-1144
    • (2007) J. Mol. Biol. , vol.368 , pp. 1132-1144
    • Emadi, S.1    Barkhordarian, H.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 54
    • 0036415838 scopus 로고    scopus 로고
    • α-Synuclein, especially the Parkinson's disease-Associated mutants, forms pore-Like annular and tubular protofibrils
    • Lashuel, H. A., Petre, B. M., Wall, J., Simon, M., Nowak, R. J., Walz, T., and Lansbury, P. T. (2002) α-Synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322, 1089-1102
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury, P.T.7
  • 55
    • 9344233839 scopus 로고    scopus 로고
    • Calcium(2) selectively induces alpha-Synuclein annular oligomers via interaction with the C-Terminal domain
    • Lowe, R., Pountney, D. L., Jensen, P. H., Gai, W. P., and Voelcker, N. H. (2004) Calcium(2) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain. Protein Sci. 13, 3245-3252
    • (2004) Protein Sci. , vol.13 , pp. 3245-3252
    • Lowe, R.1    Pountney, D.L.2    Jensen, P.H.3    Gai, W.P.4    Voelcker, N.H.5
  • 57
    • 0036484302 scopus 로고    scopus 로고
    • Multiple phosphorylation of alpha-Synuclein by protein tyrosine kinase syk prevents eosin-Induced aggregation
    • Negro, A., Brunati, A. M., Donella-Deana, A., Massimino, M. L., and Pinna, L. A. (2002) Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation. FASEB J. 16, 210-212
    • (2002) FASEB J. , vol.16 , pp. 210-212
    • Negro, A.1    Brunati, A.M.2    Donella-Deana, A.3    Massimino, M.L.4    Pinna, L.A.5
  • 59
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-Linking promotes formation of stable alphasynuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M., and Ischiropoulos, H. (2000) Dityrosine cross-linking promotes formation of stable alphasynuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275, 18344-18349
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 60
    • 0038404977 scopus 로고    scopus 로고
    • Nitration inhibits fibrillation of human alpha-Synuclein in vitro by formation of soluble oligomers
    • Yamin, G., Uversky, V. N., and Fink, A. L. (2003) Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. FEBS Lett. 542, 147-152
    • (2003) FEBS Lett. , vol.542 , pp. 147-152
    • Yamin, G.1    Uversky, V.N.2    Fink, A.L.3
  • 62
    • 78650866766 scopus 로고    scopus 로고
    • Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated alphasynuclein
    • Hejjaoui, M., Haj-Yahya, M., Kumar, K. S., Brik, A., and Lashuel, H. A. (2011) Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated alphasynuclein. Angew. Chem. 50, 405-409
    • (2011) Angew. Chem. , vol.50 , pp. 405-409
    • Hejjaoui, M.1    Haj-Yahya, M.2    Kumar, K.S.3    Brik, A.4    Lashuel, H.A.5
  • 63
    • 33745264884 scopus 로고    scopus 로고
    • Dynamic range of mass accuracy in LTQ orbitrap hybrid mass spectrometer
    • Makarov, A., Denisov, E., Lange, O., and Horning, S. (2006) Dynamic range of mass accuracy in LTQ Orbitrap hybrid mass spectrometer. J. Am. Soc. Mass Spectrom. 17, 977-982
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 977-982
    • Makarov, A.1    Denisov, E.2    Lange, O.3    Horning, S.4
  • 65
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J., and Hunt, D. F. (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101, 9528-9533
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 66
    • 34548336772 scopus 로고    scopus 로고
    • Higher-Energy C-Trap dissociation for peptide modification analysis
    • Olsen, J. V., Macek, B., Lange, O., Makarov, A., Horning, S., and Mann, M. (2007) Higher-energy C-trap dissociation for peptide modification analysis. Nat. Methods 4, 709-712
    • (2007) Nat. Methods , vol.4 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 67
    • 83055182135 scopus 로고    scopus 로고
    • Evaluation of HCD- and CID-Type fragmentation within their respective detection platforms for murine phosphoproteomics
    • Jedrychowski, M. P., Huttlin, E. L., Haas, W., Sowa, M. E., Rad, R., and Gygi, S. P. (2011) Evaluation of HCD- and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics. Mol. Cell. Proteomics 10
    • (2011) Mol. Cell. Proteomics , vol.10
    • Jedrychowski, M.P.1    Huttlin, E.L.2    Haas, W.3    Sowa, M.E.4    Rad, R.5    Gygi, S.P.6
  • 68
    • 84863323068 scopus 로고    scopus 로고
    • Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues
    • Lundby, A., Secher, A., Lage, K., Nordsborg, N. B., Dmytriyev, A., Lundby, C., and Olsen, J. V. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat. Commun. 3, 876
    • (2012) Nat. Commun. , vol.3 , pp. 876
    • Lundby, A.1    Secher, A.2    Lage, K.3    Nordsborg, N.B.4    Dmytriyev, A.5    Lundby, C.6    Olsen, J.V.7
  • 70
    • 84874619400 scopus 로고    scopus 로고
    • Refined preparation and use of anti-K-ε-GG antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments
    • Udeshi, N. D., Svinkina, T., Mertins, P., Kuhn, E., Mani, D. R., Qiao, J. W., and Carr, S. A. (2012) Refined preparation and use of anti-K-ε-GG antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Mol. Cell. Proteomics 12, 825-831
    • (2012) Mol. Cell. Proteomics , vol.12 , pp. 825-831
    • Udeshi, N.D.1    Svinkina, T.2    Mertins, P.3    Kuhn, E.4    Mani, D.R.5    Qiao, J.W.6    Carr, S.A.7
  • 72
    • 84874625369 scopus 로고    scopus 로고
    • Proteoform: A single term describing protein complexity
    • and Consortium for Top Down P.
    • Smith, L. M., Kelleher, N. L., and Consortium for Top Down, P. (2013) Proteoform: a single term describing protein complexity. Nat. Methods 10, 186-187
    • (2013) Nat. Methods , vol.10 , pp. 186-187
    • Smith, L.M.1    Kelleher, N.L.2
  • 75
    • 70449347241 scopus 로고    scopus 로고
    • Tyrosine and serine phosphorylation of alphasynuclein have opposing effects on neurotoxicity and soluble oligomer formation
    • Chen, L., Periquet, M., Wang, X., Negro, A., McLean, P. J., Hyman, B. T., and Feany, M. B. (2009) Tyrosine and serine phosphorylation of alphasynuclein have opposing effects on neurotoxicity and soluble oligomer formation. J. Clin. Invest. 119, 3257-3265
    • (2009) J. Clin. Invest. , vol.119 , pp. 3257-3265
    • Chen, L.1    Periquet, M.2    Wang, X.3    Negro, A.4    McLean, P.J.5    Hyman, B.T.6    Feany, M.B.7
  • 76
    • 84874616206 scopus 로고    scopus 로고
    • Protein digestion: An overview of the available techniques and recent developments
    • Switzar, L., Giera, M., and Niessen, W. M. (2013) Protein digestion: an overview of the available techniques and recent developments. J. Proteome Res. 12, 1067-1077
    • (2013) J. Proteome Res. , vol.12 , pp. 1067-1077
    • Switzar, L.1    Giera, M.2    Niessen, W.M.3
  • 77
    • 84867036962 scopus 로고    scopus 로고
    • Enrichment techniques employed in phosphoproteomics
    • Fila, J., and Honys, D. (2012) Enrichment techniques employed in phosphoproteomics. Amino Acids 43, 1025-1047
    • (2012) Amino Acids , vol.43 , pp. 1025-1047
    • Fila, J.1    Honys, D.2
  • 78
    • 0023888308 scopus 로고
    • High-Performance immobilized-Metal-Ion affinity chromatography of peptides and proteins
    • Porath, J. (1988) High-performance immobilized-metal-ion affinity chromatography of peptides and proteins. J. Chromatogr. 443, 3-11
    • (1988) J. Chromatogr. , vol.443 , pp. 3-11
    • Porath, J.1
  • 79
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(3) affinity chromatography of phosphopeptides
    • Posewitz, M. C., and Tempst, P. (1999) Immobilized gallium(3) affinity chromatography of phosphopeptides. Anal. Chem. 71, 2883-2892
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 80
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., and Jorgensen, T. J. (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 4, 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 81
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B., and Heck, A. J. (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76, 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 84
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-Based proteomics
    • Choudhary, C., and Mann, M. (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell Biol. 11, 427-439
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 85
    • 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., and Gygi, S. P. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. U.S.A. 100, 6940-6945
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 86
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin-Dependent kinases
    • Mayya, V., Rezual, K., Wu, L., Fong, M. B., and Han, D. K. (2006) Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases. Mol. Cell. Proteomics 5, 1146-1157
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1146-1157
    • Mayya, V.1    Rezual, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 88
    • 55849104840 scopus 로고    scopus 로고
    • Protein Standard Absolute Quantification (PSAQ) for improved investigation of staphylococcal food poisoning outbreaks
    • Dupuis, A., Hennekinne, J. A., Garin, J., and Brun, V. (2008) Protein Standard Absolute Quantification (PSAQ) for improved investigation of staphylococcal food poisoning outbreaks. Proteomics 8, 4633-4636
    • (2008) Proteomics , vol.8 , pp. 4633-4636
    • Dupuis, A.1    Hennekinne, J.A.2    Garin, J.3    Brun, V.4
  • 89
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated alpha-Synuclein and the proteasome in alpha-Synuclein aggregation: Implications for pathogenesis of Parkinson disease
    • Liu, C. W., Giasson, B. I., Lewis, K. A., Lee, V. M., Demartino, G. N., and Thomas, P. J. (2005) A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease. J. Biol. Chem. 280, 22670-22678
    • (2005) J. Biol. Chem. , vol.280 , pp. 22670-22678
    • Liu, C.W.1    Giasson, B.I.2    Lewis, K.A.3    Lee, V.M.4    Demartino, G.N.5    Thomas, P.J.6
  • 91
    • 77954693076 scopus 로고    scopus 로고
    • Proteome-Wide analysis of protein carboxy termini C terminomics
    • Schilling, O., Barre, O., Huesgen, P. F., and Overall, C. M. (2010) Proteome- wide analysis of protein carboxy termini: C terminomics. Nat. Methods 7, 508-511
    • (2010) Nat Methods , vol.7 , pp. 508-511
    • Schilling, O.1    Barre, O.2    Huesgen, P.F.3    Overall, C.M.4
  • 93
    • 79961202534 scopus 로고    scopus 로고
    • The importance of the digest: Proteolysis and absolute quantification in proteomics
    • Brownridge, P., and Beynon, R. J. (2011) The importance of the digest: proteolysis and absolute quantification in proteomics. Methods 54, 351-360
    • (2011) Methods , vol.54 , pp. 351-360
    • Brownridge, P.1    Beynon, R.J.2
  • 95
    • 84865791474 scopus 로고    scopus 로고
    • Peptide production and decay rates affect the quantitative accuracy of protein cleavage isotope dilution mass spectrometry (PC-IDMS)
    • Shuford, C. M., Sederoff, R. R., Chiang, V. L., and Muddiman, D. C. (2012) Peptide production and decay rates affect the quantitative accuracy of protein cleavage isotope dilution mass spectrometry (PC-IDMS). Mol. Cell. Proteomics 11, 814-823
    • (2012) Mol Cell Proteomics , vol.11 , pp. 814-823
    • Shuford, C.M.1    Sederoff, R.R.2    Chiang, V.L.3    Muddiman, D.C.4
  • 96
    • 84874610996 scopus 로고    scopus 로고
    • Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring-Mass spectrometry
    • Chambers, A. G., Percy, A. J., Yang, J., Camenzind, A. G., and Borchers, C. H. (2013) Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring-mass spectrometry. Mol. Cell. Proteomics 12, 781-791
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 781-791
    • Chambers, A.G.1    Percy, A.J.2    Yang, J.3    Camenzind, A.G.4    Borchers, C.H.5
  • 99
    • 84884796103 scopus 로고    scopus 로고
    • Proteomic approaches to analyze protein tyrosine nitration
    • Feeney, M. B., and Schoneich, C. (2013) Proteomic approaches to analyze protein tyrosine nitration. Antioxid. Redox Signal.
    • (2013) Antioxid. Redox Signal.
    • Feeney, M.B.1    Schoneich, C.2
  • 100
    • 58149291366 scopus 로고    scopus 로고
    • Factors that contribute to the misidentification of tyrosine nitration by shotgun proteomics
    • Stevens, S. M., Jr., Prokai-Tatrai, K., and Prokai, L. (2008) Factors that contribute to the misidentification of tyrosine nitration by shotgun proteomics. Mol. Cell. Proteomics 7, 2442-2451
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2442-2451
    • Stevens, Jr.S.M.1    Prokai-Tatrai, K.2    Prokai, L.3
  • 101
    • 79952303178 scopus 로고    scopus 로고
    • A stringent approach to improve the quality of nitrotyrosine peptide identifications
    • Ghesquiere, B., Helsens, K., Vandekerckhove, J., and Gevaert, K. (2011) A stringent approach to improve the quality of nitrotyrosine peptide identifications. Proteomics 11, 1094-1098
    • (2011) Proteomics , vol.11 , pp. 1094-1098
    • Ghesquiere, B.1    Helsens, K.2    Vandekerckhove, J.3    Gevaert, K.4
  • 102
    • 70349144524 scopus 로고    scopus 로고
    • Preferentially increased nitration of alpha-Synuclein at tyrosine-39 in a cellular oxidative model of parkinson's disease
    • Danielson, S. R., Held, J. M., Schilling, B., Oo, M., Gibson, B. W., and Andersen, J. K. (2009) Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease. Anal. Chem. 81, 7823-7828
    • (2009) Anal. Chem. , vol.81 , pp. 7823-7828
    • Danielson, S.R.1    Held, J.M.2    Schilling, B.3    Oo, M.4    Gibson, B.W.5    Andersen, J.K.6
  • 103
    • 84890749782 scopus 로고    scopus 로고
    • Characterization of the human NACP/alpha-Synuclein gene: Genomic structure, transcription start site, promoter region and polymorphisms
    • Ueda, K., Xia, Y., and Masliah, E. (2002) Characterization of the human NACP/alpha-synuclein gene: genomic structure, transcription start site, promoter region and polymorphisms. Neurobiol. Aging 23, S411
    • (2002) Neurobiol. Aging , vol.23
    • Ueda, K.1    Xia, Y.2    Masliah, E.3
  • 104
    • 0028618190 scopus 로고
    • Tissue-Dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of alzheimer's disease amyloid
    • Ueda, K., Saitoh, T., and Mori, H. (1994) Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid. Biochem. Biophys. Res. Commun. 205, 1366-1372
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1366-1372
    • Ueda, K.1    Saitoh, T.2    Mori, H.3
  • 106
    • 38649119157 scopus 로고    scopus 로고
    • Identification and characterization of a new alpha-Synuclein isoform and its role in lewy body diseases
    • Beyer, K., Domingo-Sabat, M., Lao, J. I., Carrato, C., Ferrer, I., and Ariza, A. (2008) Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases. Neurogenetics 9, 15-23
    • (2008) Neurogenetics , vol.9 , pp. 15-23
    • Beyer, K.1    Domingo-Sabat, M.2    Lao, J.I.3    Carrato, C.4    Ferrer, I.5    Ariza, A.6
  • 107
    • 33747778534 scopus 로고    scopus 로고
    • Low alpha-Synuclein 126 mRNA levels in dementia with Lewy bodies and alzheimer disease
    • Beyer, K., Humbert, J., Ferrer, A., Lao, J. I., Carrato, C., Lopez, D., Ferrer, I., and Ariza, A. (2006) Low alpha-synuclein 126 mRNA levels in dementia with Lewy bodies and Alzheimer disease. Neuroreport 17, 1327-1330
    • (2006) Neuroreport , vol.17 , pp. 1327-1330
    • Beyer, K.1    Humbert, J.2    Ferrer, A.3    Lao, J.I.4    Carrato, C.5    Lopez, D.6    Ferrer, I.7    Ariza, A.8
  • 109
    • 84855809551 scopus 로고    scopus 로고
    • Transcript expression levels of full-Length alpha-Synuclein and its three alternatively spliced variants in Parkinson's disease brain regions and in a transgenic mouse model of alpha-Synuclein overexpression
    • McLean, J. R., Hallett, P. J., Cooper, O., Stanley, M., and Isacson, O. (2012) Transcript expression levels of full-length alpha-synuclein and its three alternatively spliced variants in Parkinson's disease brain regions and in a transgenic mouse model of alpha-synuclein overexpression. Mol. Cell. Neurosci. 49, 230-239
    • (2012) Mol. Cell. Neurosci. , vol.49 , pp. 230-239
    • McLean, J.R.1    Hallett, P.J.2    Cooper, O.3    Stanley, M.4    Isacson, O.5
  • 110
    • 0037012778 scopus 로고    scopus 로고
    • An alternatively spliced form of rodent alpha-Synuclein forms intracellular inclusions in vitro: Role of the carboxy-Terminus in alpha-Synuclein aggregation
    • McLean, P. J., and Hyman, B. T. (2002) An alternatively spliced form of rodent alpha-synuclein forms intracellular inclusions in vitro: role of the carboxy-terminus in alpha-synuclein aggregation. Neurosci. Lett. 323, 219-223
    • (2002) Neurosci. Lett. , vol.323 , pp. 219-223
    • McLean, P.J.1    Hyman, B.T.2
  • 111
    • 73449099224 scopus 로고    scopus 로고
    • Oxidants induce alternative splicing of alpha-Synuclein: Implications for parkinson's disease
    • Kalivendi, S. V., Yedlapudi, D., Hillard, C. J., and Kalyanaraman, B. (2010) Oxidants induce alternative splicing of alpha-synuclein: implications for Parkinson's disease. Free Radic. Biol. Med. 48, 377-383
    • (2010) Free Radic. Biol. Med. , Issue.48 , pp. 377-383
    • Kalivendi, S.V.1    Yedlapudi, D.2    Hillard, C.J.3    Kalyanaraman, B.4
  • 112
    • 79951580097 scopus 로고    scopus 로고
    • Over-Expression of alpha-Synuclein 98 triggers intracellular oxidative stress and enhances susceptibility to rotenone
    • Ma, K. L., Yuan, Y. H., Song, L. K., Han, N., and Chen, N. H. (2011) Over-expression of alpha-synuclein 98 triggers intracellular oxidative stress and enhances susceptibility to rotenone. Neurosci. Lett. 491, 148-152
    • (2011) Neurosci. Lett. , vol.491 , pp. 148-152
    • Ma, K.L.1    Yuan, Y.H.2    Song, L.K.3    Han, N.4    Chen, N.H.5
  • 113
    • 84870552532 scopus 로고    scopus 로고
    • Deletion in exon 5 of the SNCA gene and exposure to rotenone leads to oligomerization of alpha-Synuclein and toxicity to PC12 cells
    • Ma, K. L., Song, L. K., Long, W. A., Yuan, Y. H., Zhang, Y., Song, X. Y., Niu, F., Han, N., and Chen, N. H. (2013) Deletion in exon 5 of the SNCA gene and exposure to rotenone leads to oligomerization of alpha-synuclein and toxicity to PC12 cells. Brain Res. Bull. 90, 127-131
    • (2013) Brain Res. Bull. , vol.90 , pp. 127-131
    • Ma, K.L.1    Song, L.K.2    Long, W.A.3    Yuan, Y.H.4    Zhang, Y.5    Song, X.Y.6    Niu, F.7    Han, N.8    Chen, N.H.9
  • 115
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semisynthetic and naturally Nalpha-Acetylated alpha-Synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of alpha-Synuclein
    • Fauvet, B., Fares, M. B., Samuel, F., Dikiy, I., Tandon, A., Eliezer, D., and Lashuel, H. A. (2012) Characterization of semisynthetic and naturally Nalpha-acetylated alpha-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of alpha-synuclein. J. Biol. Chem. 287, 28243-28262
    • (2012) J. Biol. Chem. , vol.287 , pp. 28243-28262
    • Fauvet, B.1    Fares, M.B.2    Samuel, F.3    Dikiy, I.4    Tandon, A.5    Eliezer, D.6    Lashuel, H.A.7
  • 117
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange, V., Picotti, P., Domon, B., and Aebersold, R. (2008) Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 4, 222
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 118
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-Based proteomics: Workflows, potential, pitfalls and future directions
    • Picotti, P., and Aebersold, R. (2012) Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat Methods 9, 555-566
    • (2012) Nat Methods , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 120
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir, T. W., Sondhi, D., and Cole, P. A. (1998) Expressed protein ligation: a general method for protein engineering. Proc. Natl. Acad. Sci. U.S.A. 95, 6705-6710
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 121
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B. (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 122
    • 37349094422 scopus 로고    scopus 로고
    • Free-Radical-Based, specific desulfurization of cysteine: A powerful advance in the synthesis of polypeptides and glycopolypeptides
    • Wan, Q., and Danishefsky, S. J. (2007) Free-radical-based, specific desulfurization of cysteine: a powerful advance in the synthesis of polypeptides and glycopolypeptides. Angew. Chem. 46, 9248-9252
    • (2007) Angew. Chem. , vol.46 , pp. 9248-9252
    • Wan, Q.1    Danishefsky, S.J.2
  • 123
    • 80053573543 scopus 로고    scopus 로고
    • Small changes, big impact: Posttranslational modifications and function of huntingtin in Huntington disease
    • Ehrnhoefer, D. E., Sutton, L., and Hayden, M. R. (2011) Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease. Neuroscientist 17, 475-492
    • (2011) Neuroscientist , vol.17 , pp. 475-492
    • Ehrnhoefer, D.E.1    Sutton, L.2    Hayden, M.R.3
  • 125
    • 68349135058 scopus 로고    scopus 로고
    • Histone modification patterns and epigenetic codes
    • Lennartsson, A., and Ekwall, K. (2009) Histone modification patterns and epigenetic codes. Biochim. Biophys. Acta 1790, 863-868
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 863-868
    • Lennartsson, A.1    Ekwall, K.2
  • 126
    • 2442457100 scopus 로고    scopus 로고
    • Semisynthesis of phosphovariants of Smad2 reveals a substrate preference of the activated T beta RI kinase
    • Ottesen, J. J., Huse, M., Sekedat, M. D., and Muir, T. W. (2004) Semisynthesis of phosphovariants of Smad2 reveals a substrate preference of the activated T beta RI kinase. Biochemistry 43, 5698-5706
    • (2004) Biochemistry , vol.43 , pp. 5698-5706
    • Ottesen, J.J.1    Huse, M.2    Sekedat, M.D.3    Muir, T.W.4
  • 127
    • 79959516046 scopus 로고    scopus 로고
    • Total chemical synthesis of a 304 amino acid K48-Linked tetraubiquitin protein
    • Kumar, K. S., Bavikar, S. N., Spasser, L., Moyal, T., Ohayon, S., and Brik, A. (2011) Total chemical synthesis of a 304 amino acid K48-linked tetraubiquitin protein. Angew. Chem. 50, 6137-6141
    • (2011) Angew. Chem. , vol.50 , pp. 6137-6141
    • Kumar, K.S.1    Bavikar, S.N.2    Spasser, L.3    Moyal, T.4    Ohayon, S.5    Brik, A.6
  • 128
    • 0037036754 scopus 로고    scopus 로고
    • Semisynthesis and folding of the potassium channel KcsA
    • Valiyaveetil, F. I., MacKinnon, R., and Muir, T. W. (2002) Semisynthesis and folding of the potassium channel KcsA. J. Am. Chem. Soc. 124, 9113-9120
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9113-9120
    • Valiyaveetil, F.I.1    Mackinnon, R.2    Muir, T.W.3
  • 129
    • 79954584825 scopus 로고    scopus 로고
    • Total chemical synthesis of an integral membrane enzyme: Diacylglycerol kinase from Escherichia coli
    • Lahiri, S., Brehs, M., Olschewski, D., and Becker, C. F. (2011) Total chemical synthesis of an integral membrane enzyme: diacylglycerol kinase from Escherichia coli. Angew. Chem. 50, 3988-3992
    • (2011) Angew. Chem. , vol.50 , pp. 3988-3992
    • Lahiri, S.1    Brehs, M.2    Olschewski, D.3    Becker, C.F.4
  • 132
    • 79961000536 scopus 로고    scopus 로고
    • Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools
    • Kaiser, S. E., Riley, B. E., Shaler, T. A., Trevino, R. S., Becker, C. H., Schulman, H., and Kopito, R. R. (2011) Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools. Nat. Methods 8, 691-696
    • (2011) Nat. Methods , vol.8 , pp. 691-696
    • Kaiser, S.E.1    Riley, B.E.2    Shaler, T.A.3    Trevino, R.S.4    Becker, C.H.5    Schulman, H.6    Kopito, R.R.7


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