메뉴 건너뛰기




Volumn , Issue , 2009, Pages 1-16

Neuroproteomics

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85043394075     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (14)

References (108)
  • 1
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • Anderson, N. L. and Anderson, N. G. (1998) Proteome and proteomics: New technologies, new concepts, and new words, Electrophoresis 19:1853-61.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 3
    • 43449086439 scopus 로고    scopus 로고
    • Analysis of organelles within the nervous system: Impact on brain and organelle functions
    • Tribl, F., Meyer, H. E. and Marcus, K. (2008) Analysis of organelles within the nervous system: Impact on brain and organelle functions, Expert Rev Proteomics 5:333-51.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 333-351
    • Tribl, F.1    Meyer, H.E.2    Marcus, K.3
  • 4
    • 3042554008 scopus 로고    scopus 로고
    • Application of proteomics technologies in the investigation of the brain
    • Fountoulakis, M. (2004) Application of proteomics technologies in the investigation of the brain, Mass Spectrom Rev 23:231-58.
    • (2004) Mass Spectrom Rev , vol.23 , pp. 231-258
    • Fountoulakis, M.1
  • 5
    • 1642523823 scopus 로고    scopus 로고
    • Functional genomics and proteomics:Application in neurosciences
    • Wilson, K. E., Ryan, M. M., Prime, J. E., et al. (2004) Functional genomics and proteomics:Application in neurosciences, J Neurol Neurosurg Psychiatry 75:529-38.
    • (2004) J Neurol Neurosurg Psychiatry , vol.75 , pp. 529-538
    • Wilson, K.E.1    Ryan, M.M.2    Prime, J.E.3
  • 6
    • 33749256309 scopus 로고    scopus 로고
    • Methods for proteomics in neuroscience
    • Tannu, N. S. and Hemby, S. E. (2006) Methods for proteomics in neuroscience, Prog Brain Res 158:41-82.
    • (2006) Prog Brain Res , vol.158 , pp. 41-82
    • Tannu, N.S.1    Hemby, S.E.2
  • 8
    • 34548612001 scopus 로고    scopus 로고
    • Neuroproteomics comes of age
    • Butcher, J. (2007) Neuroproteomics comes of age, Lancet Neurol 6:850-1.
    • (2007) Lancet Neurol , vol.6 , pp. 850-851
    • Butcher, J.1
  • 9
    • 33745944665 scopus 로고    scopus 로고
    • Neuroproteomics of the synapse and drug addiction
    • Abul-Husn, N. S. and Devi, L. A. (2006) Neuroproteomics of the synapse and drug addiction, J Pharmacol Exp Ther 318:461-8.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 461-468
    • Abul-Husn, N.S.1    Devi, L.A.2
  • 10
    • 3142724647 scopus 로고    scopus 로고
    • Neuroproteomics: Expression profiling of the brain’s proteomes in health and disease
    • Kim, S. I., Voshol, H., van Oostrum, J. et al. (2004) Neuroproteomics: Expression profiling of the brain’s proteomes in health and disease, Neurochem Res 29:1317-31.
    • (2004) Neurochem Res , vol.29 , pp. 1317-1331
    • Kim, S.I.1    Voshol, H.2    van Oostrum, J.3
  • 11
    • 33746102556 scopus 로고    scopus 로고
    • Proteomics of the human brain:Sub-proteomes might hold the key to handle brain complexity
    • Tribl, F., Marcus, K., Bringmann, G. et al. (2006) Proteomics of the human brain:Sub-proteomes might hold the key to handle brain complexity, J Neural Transm 113:1041-54.
    • (2006) J Neural Transm , vol.113 , pp. 1041-1054
    • Tribl, F.1    Marcus, K.2    Bringmann, G.3
  • 13
    • 1542500226 scopus 로고    scopus 로고
    • Huntingtin fragments form aggresomelike inclusion bodies in mammalian cells
    • Boeddrich, A., Lurz, R. and Wanker, E. E. (2003) Huntingtin fragments form aggresomelike inclusion bodies in mammalian cells, Methods Mol Biol 232:217-29.
    • (2003) Methods Mol Biol , vol.232 , pp. 217-229
    • Boeddrich, A.1    Lurz, R.2    Wanker, E.E.3
  • 14
    • 62649150690 scopus 로고    scopus 로고
    • Neural cells secrete a unique repertoire of proteins
    • Schubert, D., Herrera, F., Cumming, R. et al. (2009) Neural cells secrete a unique repertoire of proteins, J Neurochem 109:427-35.
    • (2009) J Neurochem , vol.109 , pp. 427-435
    • Schubert, D.1    Herrera, F.2    Cumming, R.3
  • 15
    • 48649101596 scopus 로고    scopus 로고
    • Physiological and pathological actions of calpains in glutamatergic neurons
    • Liu, J., Liu, M. C. and Wang, K. K. (2008) Physiological and pathological actions of calpains in glutamatergic neurons, Sci Signal 1:tr3.
    • (2008) Sci Signal , vol.1 , pp. tr3
    • Liu, J.1    Liu, M.C.2    Wang, K.K.3
  • 16
    • 39149095902 scopus 로고    scopus 로고
    • Screening the brain: Molecular fingerprints of neural stem cells
    • Maurer, M. H. and Kuschinsky, W. (2006) Screening the brain: Molecular fingerprints of neural stem cells, Curr Stem Cell Res Ther 1:65-77.
    • (2006) Curr Stem Cell Res Ther , vol.1 , pp. 65-77
    • Maurer, M.H.1    Kuschinsky, W.2
  • 17
    • 49249104487 scopus 로고    scopus 로고
    • Comparative proteomic analysis reveals differentially expressed proteins regulated by a potential tumor promoter, BRE, in human esophageal carcinoma cells
    • Chen, H. B., Pan, K., Tang, M. K. et al. (2008) Comparative proteomic analysis reveals differentially expressed proteins regulated by a potential tumor promoter, BRE, in human esophageal carcinoma cells, Biochem Cell Biol 86:302-11.
    • (2008) Biochem Cell Biol , vol.86 , pp. 302-311
    • Chen, H.B.1    Pan, K.2    Tang, M.K.3
  • 18
    • 43849092637 scopus 로고    scopus 로고
    • Proteomics: The new frontier also for brain tumor research
    • Chumbalkar, V., Sawaya, R. and Bogler, O. (2008) Proteomics: The new frontier also for brain tumor research, Curr Probl Cancer 32:143-54.
    • (2008) Curr Probl Cancer , vol.32 , pp. 143-154
    • Chumbalkar, V.1    Sawaya, R.2    Bogler, O.3
  • 19
    • 70349316341 scopus 로고    scopus 로고
    • Proteomic and immunologic analyses of brain tumor exosomes
    • Graner, M. W., Alzate, O., Dechkovskaia, A. M. et al. (2009) Proteomic and immunologic analyses of brain tumor exosomes, FASEB J 23:1541-57.
    • (2009) FASEB J , vol.23 , pp. 1541-1557
    • Graner, M.W.1    Alzate, O.2    Dechkovskaia, A.M.3
  • 21
    • 38449113394 scopus 로고    scopus 로고
    • Synaptosome proteomics
    • Bai, F. and Witzmann, F. A. (2007) Synaptosome proteomics, Subcell Biochem 43:77-98.
    • (2007) Subcell Biochem , vol.43 , pp. 77-98
    • Bai, F.1    Witzmann, F.A.2
  • 22
    • 33745617102 scopus 로고    scopus 로고
    • Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum
    • Cheng, D., Hoogenraad, C. C., Rush, J. et al. (2006) Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum, Mol Cell Proteomics 5:1158-70.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1158-1170
    • Cheng, D.1    Hoogenraad, C.C.2    Rush, J.3
  • 23
    • 46049118809 scopus 로고    scopus 로고
    • Evolutionary expansion and anatomical specialization of synapse proteome complexity
    • Emes, R. D., Pocklington, A. J., Anderson, C. N. et al. (2008) Evolutionary expansion and anatomical specialization of synapse proteome complexity, Nat Neurosci 11:799-806.
    • (2008) Nat Neurosci , vol.11 , pp. 799-806
    • Emes, R.D.1    Pocklington, A.J.2    Anderson, C.N.3
  • 24
    • 5644266504 scopus 로고    scopus 로고
    • Identification and verification of novel rodent postsynaptic density proteins
    • Jordan, B. A., Fernholz, B. D., Boussac, M. et al. (2004) Identification and verification of novel rodent postsynaptic density proteins, Mol Cell Proteomics 3:857-71.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 857-871
    • Jordan, B.A.1    Fernholz, B.D.2    Boussac, M.3
  • 25
    • 9144265671 scopus 로고    scopus 로고
    • Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology
    • Li, K. W., Hornshaw, M. P., Van Der Schors, R. C. et al. (2004) Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology, J Biol Chem 279:987-1002.
    • (2004) J Biol Chem , vol.279 , pp. 987-1002
    • Li, K.W.1    Hornshaw, M.P.2    Van Der Schors, R.C.3
  • 26
    • 43449130945 scopus 로고    scopus 로고
    • Synapse proteomics: Current status and quantitative applications
    • Li, K. W. and Jimenez, C. R. (2008) Synapse proteomics: Current status and quantitative applications, Expert Rev Proteomics 5:353-60.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 353-360
    • Li, K.W.1    Jimenez, C.R.2
  • 27
    • 22044446815 scopus 로고    scopus 로고
    • Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry
    • Schrimpf, S. P., Meskenaite, V., Brunner, E. et al. (2005) Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry, Proteomics 5:2531-41.
    • (2005) Proteomics , vol.5 , pp. 2531-2541
    • Schrimpf, S.P.1    Meskenaite, V.2    Brunner, E.3
  • 28
    • 56949083650 scopus 로고    scopus 로고
    • Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils
    • Arimon, M., Grimminger, V., Sanz, F. and Lashuel, H. A. (2008) Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils, J Mol Biol 384:1157-73.
    • (2008) J Mol Biol , vol.384 , pp. 1157-1173
    • Arimon, M.1    Grimminger, V.2    Sanz, F.3    Lashuel, H.A.4
  • 29
    • 33646237341 scopus 로고    scopus 로고
    • Proteomics-driven progress in neurodegeneration research
    • Fountoulakis, M. and Kossida, S. (2006) Proteomics-driven progress in neurodegeneration research, Electrophoresis 27:1556-73.
    • (2006) Electrophoresis , vol.27 , pp. 1556-1573
    • Fountoulakis, M.1    Kossida, S.2
  • 30
    • 33745750191 scopus 로고    scopus 로고
    • Therapeutic approaches to polyglutamine diseases:Combating protein misfolding and aggregation
    • Herbst, M. and Wanker, E. E. (2006) Therapeutic approaches to polyglutamine diseases:Combating protein misfolding and aggregation, Curr Pharm Des 12:2543-55.
    • (2006) Curr Pharm Des , vol.12 , pp. 2543-2555
    • Herbst, M.1    Wanker, E.E.2
  • 31
    • 34347258879 scopus 로고    scopus 로고
    • Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation. A possible therapeutic strategy
    • Herbst, M. and Wanker, E. E. (2007) Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation. A possible therapeutic strategy, Neurodegener Dis 4:254-60.
    • (2007) Neurodegener Dis , vol.4 , pp. 254-260
    • Herbst, M.1    Wanker, E.E.2
  • 32
    • 35148859811 scopus 로고    scopus 로고
    • Mortalin is regulated by APOE in hippocampus of AD patients and by human APOE in TR mice
    • Osorio, C., Sullivan, P. M., He, D. N. et al. (2007) Mortalin is regulated by APOE in hippocampus of AD patients and by human APOE in TR mice, Neurobiol Aging 28:1853-62.
    • (2007) Neurobiol Aging , vol.28 , pp. 1853-1862
    • Osorio, C.1    Sullivan, P.M.2    He, D.N.3
  • 33
    • 1842505677 scopus 로고    scopus 로고
    • Proteomics: A new approach to investigate oxidative stress in Alzheimer’s disease brain
    • Butterfield, D. A. (2004) Proteomics: A new approach to investigate oxidative stress in Alzheimer’s disease brain, Brain Res 1000:1-7.
    • (2004) Brain Res , vol.1000 , pp. 1-7
    • Butterfield, D.A.1
  • 34
    • 33847192092 scopus 로고    scopus 로고
    • Oxidative damage, protein synthesis, and protein degradation in Alzheimer’s disease
    • Ding, Q., Dimayuga, E. and Keller, J. N. (2007) Oxidative damage, protein synthesis, and protein degradation in Alzheimer’s disease, Curr Alzheimer Res 4:73-9.
    • (2007) Curr Alzheimer Res , vol.4 , pp. 73-79
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 35
    • 33845328844 scopus 로고    scopus 로고
    • Synaptic dysfunction and oxidative stress in Alzheimer’s disease: Emerging mechanisms
    • Forero, D. A., Casadesus, G., Perry, G. and Arboleda, H. (2006) Synaptic dysfunction and oxidative stress in Alzheimer’s disease: Emerging mechanisms, J Cell Mol Med 10z:796-805.
    • (2006) J Cell Mol Med , vol.10z , pp. 796-805
    • Forero, D.A.1    Casadesus, G.2    Perry, G.3    Arboleda, H.4
  • 36
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer’s disease: Insights into mechanism of neurodegeneration from redox proteomics
    • Sultana, R., Perluigi, M. and Butterfield, D. A. (2006) Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer’s disease: Insights into mechanism of neurodegeneration from redox proteomics, Antioxid Redox Signal 8:2021-37.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 37
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimer’s disease brain and in vivo and in vitro models of AD centered around Abeta(1-42)
    • Sultana, R., Perluigi, M. and Butterfield, D. A. (2006) Redox proteomics identification of oxidatively modified proteins in Alzheimer’s disease brain and in vivo and in vitro models of AD centered around Abeta(1-42), J Chromatogr B Analyt Technol Biomed Life Sci 833:3-11.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.833 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 38
    • 42549125986 scopus 로고    scopus 로고
    • Subcellular proteomics in neuroscience
    • Li, K. W. and Smit, A. B. (2008) Subcellular proteomics in neuroscience, Front Biosci 13:4416-25.
    • (2008) Front Biosci , vol.13 , pp. 4416-4425
    • Li, K.W.1    Smit, A.B.2
  • 39
    • 44949192092 scopus 로고    scopus 로고
    • Clinical proteomics in neurodegenerative disorders
    • Zetterberg, H., Ruetschi, U., Portelius, E. et al. (2008) Clinical proteomics in neurodegenerative disorders, Acta Neurol Scand 118:1-11.
    • (2008) Acta Neurol Scand , vol.118 , pp. 1-11
    • Zetterberg, H.1    Ruetschi, U.2    Portelius, E.3
  • 40
    • 17244372264 scopus 로고    scopus 로고
    • Recent advances in 2D electrophoresis: An array of possibilities
    • Van den Bergh, G. and Arckens, L. (2005) Recent advances in 2D electrophoresis: An array of possibilities, Expert Rev Proteomics 2:243-52.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 243-252
    • Van den Bergh, G.1    Arckens, L.2
  • 41
    • 4644315283 scopus 로고    scopus 로고
    • Recent advances in neuroproteomics and potential application to studies of drug addiction
    • Williams, K., Wu, T., Colangelo, C. and Nairn, A. C. (2004) Recent advances in neuroproteomics and potential application to studies of drug addiction, Neuropharmacology 47 (Suppl 1):148-66.
    • (2004) Neuropharmacology , vol.47 , pp. 148-166
    • Williams, K.1    Wu, T.2    Colangelo, C.3    Nairn, A.C.4
  • 42
    • 32544432414 scopus 로고    scopus 로고
    • The synapse proteome and phosphoproteome: A new paradigm for synapse biology
    • Grant, S. G. (2006) The synapse proteome and phosphoproteome: A new paradigm for synapse biology, Biochem Soc Trans 34:59-63.
    • (2006) Biochem Soc Trans , vol.34 , pp. 59-63
    • Grant, S.G.1
  • 43
    • 29244482282 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation in mouse brain by hypothesis-driven multistage mass spectrometry
    • Jin, M., Bateup, H., Padovan, J. C. et al. (2005) Quantitative analysis of protein phosphorylation in mouse brain by hypothesis-driven multistage mass spectrometry, Anal Chem 77:7845-51.
    • (2005) Anal Chem , vol.77 , pp. 7845-7851
    • Jin, M.1    Bateup, H.2    Padovan, J.C.3
  • 44
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament- tau) from Alzheimer’s disease brain using nanoelectrospray mass spectrometry
    • Hanger, D. P., Betts, J. C., Loviny, T. L., Blackstock, W. P. and Anderton, B. H. (1998) New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament- tau) from Alzheimer’s disease brain using nanoelectrospray mass spectrometry, J Neurochem 71:2465-76.
    • (1998) J Neurochem , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3    Blackstock, W.P.4    Anderton, B.H.5
  • 45
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins:Purification and identification
    • Wan, J., Roth, A. F., Bailey, A. O. and Davis, N. G. (2007) Palmitoylated proteins:Purification and identification, Nat Protoc 2:1573-84.
    • (2007) Nat Protoc , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 46
    • 24344489020 scopus 로고    scopus 로고
    • Submicromolar concentrations of palmitoyl-CoA specifically thioesterify cysteine 244 in glyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: A novel mechanism potentially underlying fatty acid induced insulin resistance
    • Yang, J., Gibson, B., Snider, J. et al. (2005) Submicromolar concentrations of palmitoyl-CoA specifically thioesterify cysteine 244 in glyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: A novel mechanism potentially underlying fatty acid induced insulin resistance, Biochemistry 44:11903-12.
    • (2005) Biochemistry , vol.44 , pp. 11903-11912
    • Yang, J.1    Gibson, B.2    Snider, J.3
  • 47
    • 53849094776 scopus 로고    scopus 로고
    • High-resolution mass spectrometry analysis of protein oxidations and resultant loss of function
    • Barnes, S., Shonsey, E. M., Eliuk, S. M. et al. (2008) High-resolution mass spectrometry analysis of protein oxidations and resultant loss of function, Biochem Soc Trans 36:1037-44.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1037-1044
    • Barnes, S.1    Shonsey, E.M.2    Eliuk, S.M.3
  • 48
    • 34548588380 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in Alzheimer’s disease and mild cognitive impairment: Insights into the progression of this dementing disorder
    • Butterfield, D. A. and Sultana, R. (2007) Redox proteomics identification of oxidatively modified brain proteins in Alzheimer’s disease and mild cognitive impairment: Insights into the progression of this dementing disorder, J Alzheimers Dis 12:61-72.
    • (2007) J Alzheimers Dis , vol.12 , pp. 61-72
    • Butterfield, D.A.1    Sultana, R.2
  • 49
    • 59249100362 scopus 로고    scopus 로고
    • Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase
    • Hutson, S. M., Poole, L. B., Coles, S. and Conway, M. E. (2008) Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase, Methods Mol Biol 476:139-52.
    • (2008) Methods Mol Biol , vol.476 , pp. 139-152
    • Hutson, S.M.1    Poole, L.B.2    Coles, S.3    Conway, M.E.4
  • 50
    • 57649198018 scopus 로고    scopus 로고
    • Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability
    • Paige, J. S., Xu, G., Stancevic, B. and Jaffrey, S. R. (2008) Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability, Chem Biol 15:1307-16.
    • (2008) Chem Biol , vol.15 , pp. 1307-1316
    • Paige, J.S.1    Xu, G.2    Stancevic, B.3    Jaffrey, S.R.4
  • 51
    • 53249095492 scopus 로고    scopus 로고
    • Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease
    • Pamplona, R., Naudi, A., Gavin, R. et al. (2008) Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease, Free Radic Biol Med 45:1159-66.
    • (2008) Free Radic Biol Med , vol.45 , pp. 1159-1166
    • Pamplona, R.1    Naudi, A.2    Gavin, R.3
  • 52
    • 34548738223 scopus 로고    scopus 로고
    • 2D gel proteomics: An approach to study age-related differences in protein abundance or isoform complexity in biological samples
    • Kim, H., Eliuk, S., Deshane, J. et al. (2007) 2D gel proteomics: An approach to study age-related differences in protein abundance or isoform complexity in biological samples, Methods Mol Biol 371:349-91.
    • (2007) Methods Mol Biol , vol.371 , pp. 349-391
    • Kim, H.1    Eliuk, S.2    Deshane, J.3
  • 53
    • 0038025565 scopus 로고    scopus 로고
    • Proteomics in brain research:Potentials and limitations
    • Lubec, G., Krapfenbauer, K. and Fountoulakis, M. (2003) Proteomics in brain research:Potentials and limitations, Prog Neurobiol 69:193-211.
    • (2003) Prog Neurobiol , vol.69 , pp. 193-211
    • Lubec, G.1    Krapfenbauer, K.2    Fountoulakis, M.3
  • 54
    • 1842634504 scopus 로고    scopus 로고
    • Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer’s disease
    • Choi, J., Forster, M. J., McDonald, S. R. et al. (2004) Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer’s disease, Free Radic Biol Med 36:1155-62.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1155-1162
    • Choi, J.1    Forster, M.J.2    McDonald, S.R.3
  • 55
    • 34347356554 scopus 로고    scopus 로고
    • Oxidized proteins in astrocytes generated in a hyperbaric atmosphere induce neuronal apoptosis
    • Mori, H., Oikawa, M., Tamagami, T. et al. (2007) Oxidized proteins in astrocytes generated in a hyperbaric atmosphere induce neuronal apoptosis, J Alzheimers Dis 11:165-74.
    • (2007) J Alzheimers Dis , vol.11 , pp. 165-174
    • Mori, H.1    Oikawa, M.2    Tamagami, T.3
  • 56
    • 4444242850 scopus 로고    scopus 로고
    • Proteomic identification of brainstem cytosolic proteins in a neuropathic pain model
    • Alzate, O., Hussain, S. R., Goettl, V. M. et al. (2004) Proteomic identification of brainstem cytosolic proteins in a neuropathic pain model, Brain Res Mol Brain Res 128:193-200.
    • (2004) Brain Res Mol Brain Res , vol.128 , pp. 193-200
    • Alzate, O.1    Hussain, S.R.2    Goettl, V.M.3
  • 57
    • 42149136185 scopus 로고    scopus 로고
    • Identification of new regional marker proteins to map mouse brain by 2-D difference gel electrophoresis screening
    • Jacobs, S., Van de Plas, B., Van der Gucht, E. et al. (2008) Identification of new regional marker proteins to map mouse brain by 2-D difference gel electrophoresis screening, Electrophoresis 29:1518-24.
    • (2008) Electrophoresis , vol.29 , pp. 1518-1524
    • Jacobs, S.1    Van de Plas, B.2    van der Gucht, E.3
  • 58
    • 40949085263 scopus 로고    scopus 로고
    • Profiling of experience-regulated proteins in the songbird auditory forebrain using quantitative proteomics
    • Pinaud, R., Osorio, C., Alzate, O. and Jarvis, E. D. (2008) Profiling of experience-regulated proteins in the songbird auditory forebrain using quantitative proteomics, Eur J Neurosci 27:1409-22.
    • (2008) Eur J Neurosci , vol.27 , pp. 1409-1422
    • Pinaud, R.1    Osorio, C.2    Alzate, O.3    Jarvis, E.D.4
  • 59
    • 1542344981 scopus 로고    scopus 로고
    • Protein profiling of human postmortem brain using 2-dimensional fluorescence difference gel electrophoresis (2-D DIGE)
    • Swatton, J. E., Prabakaran, S., Karp, N. A., Lilley, K. S. and Bahn, S. (2004) Protein profiling of human postmortem brain using 2-dimensional fluorescence difference gel electrophoresis (2-D DIGE), Mol Psychiatry 9:128-43.
    • (2004) Mol Psychiatry , vol.9 , pp. 128-143
    • Swatton, J.E.1    Prabakaran, S.2    Karp, N.A.3    Lilley, K.S.4    Bahn, S.5
  • 60
    • 46249114406 scopus 로고    scopus 로고
    • Non-covalent and covalent protein labeling in two-dimensional gel electrophoresis
    • Riederer, B. M. (2008) Non-covalent and covalent protein labeling in two-dimensional gel electrophoresis, J Proteomics 71:231-44.
    • (2008) J Proteomics , vol.71 , pp. 231-244
    • Riederer, B.M.1
  • 61
    • 42449149436 scopus 로고    scopus 로고
    • Striatal proteomic analysis suggests that first L-dopa dose equates to chronic exposure
    • Scholz, B., Svensson, M., Alm, H. et al. (2008) Striatal proteomic analysis suggests that first L-dopa dose equates to chronic exposure, PLoS ONE 3:e1589.
    • (2008) PLoS ONE , vol.3 , pp. e1589
    • Scholz, B.1    Svensson, M.2    Alm, H.3
  • 62
    • 34347394970 scopus 로고    scopus 로고
    • Proteomics strategy based on liquid-phase IEF and 2-D DIGE:Application to bone marrow mesenchymal progenitor cells
    • Seshi, B. (2007) Proteomics strategy based on liquid-phase IEF and 2-D DIGE:Application to bone marrow mesenchymal progenitor cells, Proteomics 7:1984-99.
    • (2007) Proteomics , vol.7 , pp. 1984-1999
    • Seshi, B.1
  • 63
    • 20544442753 scopus 로고    scopus 로고
    • Rapid discovery of putative protein biomarkers of traumatic brain injury by SDS-PAGE-capillary liquid chromatography- tandem mass spectrometry
    • Haskins, W. E., Kobeissy, F. H., Wolper, R. A. et al. (2005) Rapid discovery of putative protein biomarkers of traumatic brain injury by SDS-PAGE-capillary liquid chromatography- tandem mass spectrometry, J Neurotrauma 22:629-44.
    • (2005) J Neurotrauma , vol.22 , pp. 629-644
    • Haskins, W.E.1    Kobeissy, F.H.2    Wolper, R.A.3
  • 64
    • 43449089715 scopus 로고    scopus 로고
    • Psychoproteomic analysis of rat cortex following acute methamphetamine exposure
    • Kobeissy, F. H., Warren, M. W., Ottens, A. K. et al. (2008) Psychoproteomic analysis of rat cortex following acute methamphetamine exposure, J Proteome Res 7:1971-83.
    • (2008) J Proteome Res , vol.7 , pp. 1971-1983
    • Kobeissy, F.H.1    Warren, M.W.2    Ottens, A.K.3
  • 65
    • 23044442338 scopus 로고    scopus 로고
    • A multidimensional differential proteomic platform using dual-phase ion-exchange chromatography-polyacrylamide gel electrophoresis/reversed-phase liquid chromatography tandem mass spectrometry
    • Ottens, A. K., Kobeissy, F. H., Wolper, R. A. et al. (2005) A multidimensional differential proteomic platform using dual-phase ion-exchange chromatography-polyacrylamide gel electrophoresis/reversed-phase liquid chromatography tandem mass spectrometry, Anal Chem 77:4836-45.
    • (2005) Anal Chem , vol.77 , pp. 4836-4845
    • Ottens, A.K.1    Kobeissy, F.H.2    Wolper, R.A.3
  • 67
    • 65949120001 scopus 로고    scopus 로고
    • Two-dimensional protein separation in microfluidic devices
    • Chen, H. and Fan, Z. H. (2009) Two-dimensional protein separation in microfluidic devices, Electrophoresis 30:758-65.
    • (2009) Electrophoresis , vol.30 , pp. 758-765
    • Chen, H.1    Fan, Z.H.2
  • 68
    • 33747876882 scopus 로고    scopus 로고
    • An integrated digital microfluidic chip for multiplexed proteomic sample preparation and analysis by MALDI-MS
    • Moon, H., Wheeler, A. R., Garrell, R. L., Loo, J. A. and Kim, C. J. (2006) An integrated digital microfluidic chip for multiplexed proteomic sample preparation and analysis by MALDI-MS, Lab Chip 6:1213-9.
    • (2006) Lab Chip , vol.6 , pp. 1213-1219
    • Moon, H.1    Wheeler, A.R.2    Garrell, R.L.3    Loo, J.A.4    Kim, C.J.5
  • 70
    • 58249092145 scopus 로고    scopus 로고
    • Protein techniques: Immunoprecipitation, in vitro kinase assays, and Western blotting
    • Dickson, C. (2008) Protein techniques: Immunoprecipitation, in vitro kinase assays, and Western blotting, Methods Mol Biol 461:735-44.
    • (2008) Methods Mol Biol , vol.461 , pp. 735-744
    • Dickson, C.1
  • 72
    • 3242670023 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis for analysis of protein complexes
    • Barnouin, K. (2004) Two-dimensional gel electrophoresis for analysis of protein complexes, Methods Mol Biol 261:479-98.
    • (2004) Methods Mol Biol , vol.261 , pp. 479-498
    • Barnouin, K.1
  • 73
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. (2003) Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system, Nat Neurosci 6:231-42.
    • (2003) Nat Neurosci , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 74
    • 33744922423 scopus 로고    scopus 로고
    • A human protein atlas based on antibody proteomics
    • Persson, A., Hober, S. and Uhlen, M. (2006) A human protein atlas based on antibody proteomics, Curr Opin Mol Ther 8:185-90.
    • (2006) Curr Opin Mol Ther , vol.8 , pp. 185-190
    • Persson, A.1    Hober, S.2    Uhlen, M.3
  • 78
    • 0342503024 scopus 로고
    • The macromolecular properties of bloodgroup substances. Sedimentation-velocity and viscosity measurements
    • Creeth, J. M. and Knight, C. G. (1967) The macromolecular properties of bloodgroup substances. Sedimentation-velocity and viscosity measurements, Biochem J 105:1135-45.
    • (1967) Biochem J , vol.105 , pp. 1135-1145
    • Creeth, J.M.1    Knight, C.G.2
  • 79
    • 0014035554 scopus 로고
    • The determination of molecular weights of biological macromolecules by ultracentrifuge methods
    • Creeth, J. M. and Pain, R. H. (1967) The determination of molecular weights of biological macromolecules by ultracentrifuge methods, Prog Biophys Mol Biol 17:217-87.
    • (1967) Prog Biophys Mol Biol , vol.17 , pp. 217-287
    • Creeth, J.M.1    Pain, R.H.2
  • 80
    • 0015823837 scopus 로고
    • Characterization of proteins by sedimentation equilibrium in the analytical ultracentrifuge
    • Teller, D. C. (1973) Characterization of proteins by sedimentation equilibrium in the analytical ultracentrifuge, Methods Enzymol 27:346-441.
    • (1973) Methods Enzymol , vol.27 , pp. 346-441
    • Teller, D.C.1
  • 81
    • 33749523387 scopus 로고    scopus 로고
    • The impact of protein characterization in structural proteomics
    • Geerlof, A., Brown, J., Coutard, B. et al. (2006) The impact of protein characterization in structural proteomics, Acta Crystallogr D Biol Crystallogr 62:1125-36.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1125-1136
    • Geerlof, A.1    Brown, J.2    Coutard, B.3
  • 82
    • 62649089303 scopus 로고    scopus 로고
    • Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation
    • Stafford, W. F., 3rd (2009) Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation, Methods Mol Biol 490:83-113.
    • (2009) Methods Mol Biol , vol.490 , pp. 83-113
    • Stafford, W.F.1
  • 83
    • 45749124039 scopus 로고    scopus 로고
    • Mining the oncoproteome and studying molecular interactions for biomarker development by 2DE, ChIP and SPR technologies
    • Ahmed, F. E. (2008) Mining the oncoproteome and studying molecular interactions for biomarker development by 2DE, ChIP and SPR technologies, Expert Rev Proteomics 5:469-96.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 469-496
    • Ahmed, F.E.1
  • 84
    • 0026045194 scopus 로고
    • Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology
    • Jonsson, U., Fagerstam, L., Ivarsson, B. et al. (1991) Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology, Biotechniques 11:620-7.
    • (1991) Biotechniques , vol.11 , pp. 620-627
    • Jonsson, U.1    Fagerstam, L.2    Ivarsson, B.3
  • 85
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Myszka, D. G. (1997) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors, Curr Opin Biotechnol 8:50-7.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 50-57
    • Myszka, D.G.1
  • 86
    • 45749101309 scopus 로고    scopus 로고
    • Surface plasmon resonance mass spectrometry in proteomics
    • Visser, N. F. and Heck, A. J. (2008) Surface plasmon resonance mass spectrometry in proteomics, Expert Rev Proteomics 5:425-33.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 425-433
    • Visser, N.F.1    Heck, A.J.2
  • 87
    • 15344344813 scopus 로고    scopus 로고
    • Proteomic applications of surface plasmon resonance biosensors: Analysis of protein arrays
    • Yuk, J. S. and Ha, K. S. (2005) Proteomic applications of surface plasmon resonance biosensors: Analysis of protein arrays, Exp Mol Med 37:1-10.
    • (2005) Exp Mol Med , vol.37 , pp. 1-10
    • Yuk, J.S.1    Ha, K.S.2
  • 88
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. (2006) Using circular dichroism spectra to estimate protein secondary structure, Nat Protoc 1:2876-90.
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 89
    • 4444370179 scopus 로고    scopus 로고
    • How does parkin ligate ubiquitin to Parkinson’s disease?
    • Kahle, P. J. and Haass, C. (2004) How does parkin ligate ubiquitin to Parkinson’s disease? EMBO Rep 5:681-5.
    • (2004) EMBO Rep , vol.5 , pp. 681-685
    • Kahle, P.J.1    Haass, C.2
  • 90
    • 45549091524 scopus 로고    scopus 로고
    • The stress rheostat: An interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration
    • Matus, S., Lisbona, F., Torres, M. et al. (2008) The stress rheostat: An interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration, Curr Mol Med 8:157-72.
    • (2008) Curr Mol Med , vol.8 , pp. 157-172
    • Matus, S.1    Lisbona, F.2    Torres, M.3
  • 91
    • 58049214009 scopus 로고    scopus 로고
    • Tau oligomerization: A role for tau aggregation intermediates linked to neurodegeneration
    • Sahara, N., Maeda, S. and Takashima, A. (2008) Tau oligomerization: A role for tau aggregation intermediates linked to neurodegeneration, Curr Alzheimer Res 5:591-8.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 591-598
    • Sahara, N.1    Maeda, S.2    Takashima, A.3
  • 92
    • 34247098374 scopus 로고    scopus 로고
    • Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders
    • Uehara, T. (2007) Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders, Antioxid Redox Signal 9:597-601.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 597-601
    • Uehara, T.1
  • 93
    • 55949092886 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and neurodegenerative diseases
    • Uversky, V. N. (2008) Alpha-synuclein misfolding and neurodegenerative diseases, Curr Protein Pept Sci 9:507-40.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 507-540
    • Uversky, V.N.1
  • 95
    • 34249862316 scopus 로고    scopus 로고
    • The role of tau phosphorylation and cleavage in neuronal cell death
    • Chun, W. and Johnson, G. V. (2007) The role of tau phosphorylation and cleavage in neuronal cell death, Front Biosci 12:733-56.
    • (2007) Front Biosci , vol.12 , pp. 733-756
    • Chun, W.1    Johnson, G.V.2
  • 96
    • 48449090669 scopus 로고    scopus 로고
    • Brain banks:Benefits, limitations and cautions concerning the use of post-mortem brain tissue for molecular studies
    • Ferrer, I., Martinez, A., Boluda, S., Parchi, P. and Barrachina, M. (2008) Brain banks:Benefits, limitations and cautions concerning the use of post-mortem brain tissue for molecular studies, Cell Tissue Bank 9:181-94.
    • (2008) Cell Tissue Bank , vol.9 , pp. 181-194
    • Ferrer, I.1    Martinez, A.2    Boluda, S.3    Parchi, P.4    Barrachina, M.5
  • 98
    • 57149098589 scopus 로고    scopus 로고
    • Systems biology perspectives on cerebellar long-term depression
    • Ogasawara, H., Doi, T. and Kawato, M. (2008) Systems biology perspectives on cerebellar long-term depression, Neurosignals 16:300-17.
    • (2008) Neurosignals , vol.16 , pp. 300-317
    • Ogasawara, H.1    Doi, T.2    Kawato, M.3
  • 99
    • 39949083958 scopus 로고    scopus 로고
    • The substrate for long-lasting memory: If not protein synthesis, then what?
    • Routtenberg, A. (2008) The substrate for long-lasting memory: If not protein synthesis, then what? Neurobiol Learn Mem 89:225-33.
    • (2008) Neurobiol Learn Mem , vol.89 , pp. 225-233
    • Routtenberg, A.1
  • 100
    • 46249117435 scopus 로고    scopus 로고
    • The role of post-translational modifications for learning and memory formation
    • Sunyer, B., Diao, W. and Lubec, G. (2008) The role of post-translational modifications for learning and memory formation, Electrophoresis 29:2593-2602.
    • (2008) Electrophoresis , vol.29 , pp. 2593-2602
    • Sunyer, B.1    Diao, W.2    Lubec, G.3
  • 101
    • 60549103853 scopus 로고    scopus 로고
    • Complex brain networks: Graph theoretical analysis of structural and functional systems
    • Bullmore, E. and Sporns, O. (2009) Complex brain networks: Graph theoretical analysis of structural and functional systems, Nat Rev Neurosci 10:186-98.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 186-198
    • Bullmore, E.1    Sporns, O.2
  • 102
    • 0010697803 scopus 로고    scopus 로고
    • Proteomics of multiprotein complexes: Answering fundamental questions in neuroscience
    • Grant, S. G. and Husi, H. (2001) Proteomics of multiprotein complexes: Answering fundamental questions in neuroscience, Trends Biotechnol 19:S49-54.
    • (2001) Trends Biotechnol , vol.19 , pp. S49-S54
    • Grant, S.G.1    Husi, H.2
  • 103
    • 33751395622 scopus 로고    scopus 로고
    • The value of high quality protein-protein interaction networks for systems biology
    • Stelzl, U. and Wanker, E. E. (2006) The value of high quality protein-protein interaction networks for systems biology, Curr Opin Chem Biol 10:551-8.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 551-558
    • Stelzl, U.1    Wanker, E.E.2
  • 104
    • 51049123818 scopus 로고    scopus 로고
    • Protein cooperation: From neurons to networks
    • Volonte, C., D’Ambrosi, N. and Amadio, S. (2008) Protein cooperation: From neurons to networks, Prog Neurobiol 86:61-71.
    • (2008) Prog Neurobiol , vol.86 , pp. 61-71
    • Volonte, C.1    D’Ambrosi, N.2    Amadio, S.3
  • 105
    • 58149305794 scopus 로고    scopus 로고
    • An empirical framework for binary interactome mapping
    • Venkatesan, K., Rual, J. F., Vazquez, A. et al. (2009) An empirical framework for binary interactome mapping, Nat Methods 6:83-90.
    • (2009) Nat Methods , vol.6 , pp. 83-90
    • Venkatesan, K.1    Rual, J.F.2    Vazquez, A.3
  • 106
    • 53349117774 scopus 로고    scopus 로고
    • High-quality binary protein interaction map of the yeast interactome network
    • Yu, H., Braun, P., Yildirim, M. A. et al. (2008) High-quality binary protein interaction map of the yeast interactome network, Science 322:104-10.
    • (2008) Science , vol.322 , pp. 104-110
    • Yu, H.1    Braun, P.2    Yildirim, M.A.3
  • 107
    • 1842580761 scopus 로고    scopus 로고
    • Functional and topological characterization of protein interaction networks
    • Yook, S. H., Oltvai, Z. N. and Barabasi, A. L. (2004) Functional and topological characterization of protein interaction networks, Proteomics 4:928-42.
    • (2004) Proteomics , vol.4 , pp. 928-942
    • Yook, S.H.1    Oltvai, Z.N.2    Barabasi, A.L.3
  • 108
    • 0141484611 scopus 로고    scopus 로고
    • Evolutionary conservation of motif constituents in the yeast protein interaction network
    • Wuchty, S., Oltvai, Z. N. and Barabasi, A. L. (2003) Evolutionary conservation of motif constituents in the yeast protein interaction network, Nat Genet 35:176-9.
    • (2003) Nat Genet , vol.35 , pp. 176-179
    • Wuchty, S.1    Oltvai, Z.N.2    Barabasi, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.