메뉴 건너뛰기




Volumn 2011, Issue , 2011, Pages

A window into the heterogeneity of human cerebrospinal fluid Aβ peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-12]; AMYLOID BETA PROTEIN[1-13]; AMYLOID BETA PROTEIN[1-14]; AMYLOID BETA PROTEIN[1-15]; AMYLOID BETA PROTEIN[1-16]; AMYLOID BETA PROTEIN[1-17]; AMYLOID BETA PROTEIN[1-18]; AMYLOID BETA PROTEIN[1-19]; AMYLOID BETA PROTEIN[1-20]; AMYLOID BETA PROTEIN[1-27]; AMYLOID BETA PROTEIN[1-28]; AMYLOID BETA PROTEIN[1-29]; AMYLOID BETA PROTEIN[1-30]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[10-40]; AMYLOID BETA PROTEIN[11-30]; AMYLOID BETA PROTEIN[11-34]; AMYLOID BETA PROTEIN[11-40]; AMYLOID BETA PROTEIN[11-42]; AMYLOID BETA PROTEIN[11-43]; AMYLOID BETA PROTEIN[12-43]; AMYLOID BETA PROTEIN[2-14]; AMYLOID BETA PROTEIN[2-17]; AMYLOID BETA PROTEIN[3-17]; AMYLOID BETA PROTEIN[3-44]; AMYLOID BETA PROTEIN[6-27]; AMYLOID BETA PROTEIN[6-34]; AMYLOID BETA PROTEIN[6-35]; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 80053492393     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/697036     Document Type: Review
Times cited : (17)

References (113)
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J., Selkoe D. J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 2002 297 5580 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid- immunotherapy?
    • Lemere C. A., Masliah E., Can Alzheimer disease be prevented by amyloid- immunotherapy? Nature Reviews Neurology 2010 6 2 108 119
    • (2010) Nature Reviews Neurology , vol.6 , Issue.2 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 5
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct -amyloid peptide species, A N3(pE), in senile plaques
    • Saido T. C., Iwatsubo T., Mann D. M. A., Shimada H., Ihara Y., Kawashima S., Dominant and differential deposition of distinct -amyloid peptide species, A N3(pE), in senile plaques Neuron 1995 14 2 457 466
    • (1995) Neuron , vol.14 , Issue.2 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.A.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 6
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid-β(1-42(43)) and amino-terminally modified and truncated amyloid-β42(43) deposit in diffuse plaques
    • Iwatsubo T., Saido T. C., Mann D. M. A., Lee V. M. Y., Trojanowski J. Q., Full-length amyloid- (1-42(43)) and amino-terminally modified and truncated amyloid- 42(43) deposit in diffuse plaques American Journal of Pathology 1996 149 6 1823 1830 (Pubitemid 26415203)
    • (1996) American Journal of Pathology , vol.149 , Issue.6 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.A.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 7
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid β-peptide in Alzheimer's disease and Down's syndrome brains
    • DOI 10.1016/S0014-5793(97)00564-4, PII S0014579397005644
    • Russo C., Saido T. C., DeBusk L. M., Tabaton M., Gambetti P., Teller J. K., Heterogeneity of water-soluble amyloid -peptide in Alzheimer's disease and Down's syndrome brains FEBS Letters 1997 409 3 411 416 (Pubitemid 27285896)
    • (1997) FEBS Letters , vol.409 , Issue.3 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    DeBusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 10
    • 0035118308 scopus 로고    scopus 로고
    • Identification of amino-terminally and phospotyrosine-modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain
    • DOI 10.1006/nbdi.2000.0357
    • Russo C., Salis S., Dolcini V., Amino-terminal modification and tyrosine phosphorylation of carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain Neurobiology of Disease 2001 8 1 173 180 (Pubitemid 32171829)
    • (2001) Neurobiology of Disease , vol.8 , Issue.1 , pp. 173-180
    • Russo, C.1    Salis, S.2    Dolcini, V.3    Venezia, V.4    Song, X.5    Teller, J.K.6    Schettini, G.7
  • 12
    • 33947305482 scopus 로고    scopus 로고
    • Characterization of Abeta11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: Implication of N-terminally truncated Abeta species in the pathogenesis of Alzheimer's disease
    • Liu K., Solano I., Mann D., Lemere C., Mercken M., Trojanowski J. Q., Lee V. M., Characterization of Abeta11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Abeta species in the pathogenesis of Alzheimer's disease Acta neuropathologica 2006 112 2 163 174
    • (2006) Acta Neuropathologica , vol.112 , Issue.2 , pp. 163-174
    • Liu, K.1    Solano, I.2    Mann, D.3    Lemere, C.4    Mercken, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 15
    • 0037022828 scopus 로고    scopus 로고
    • Glu11 site cleavage and N-terminally truncated Aβ production upon BACE overexpression
    • DOI 10.1021/bi015800g
    • Liu K., Doms R. W., Lee V. M. Y., Glu11 site cleavage and N-terminally truncated A production upon BACE overexpression Biochemistry 2002 41 9 3128 3136 (Pubitemid 34184644)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3128-3136
    • Liu, K.1    Doms, R.W.2    Lee, V.M.-Y.3
  • 17
    • 42149123761 scopus 로고    scopus 로고
    • ε-secretase: Reduction of amyloid precursor protein ε-site cleavage in Alzheimer's disease
    • DOI 10.2174/156720508783954776
    • Kametani F., -secretase: reduction of amyloid precursor protein -site cleavage in Alzheimer's disease Current Alzheimer Research 2008 5 2 165 171 (Pubitemid 351536341)
    • (2008) Current Alzheimer Research , vol.5 , Issue.2 , pp. 165-171
    • Kametani, F.1
  • 19
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA work group under the auspices of Department of Health and Human Services Task Force on Alzheimer's disease
    • McKhann G., Drachman D., Folstein M., Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA work group under the auspices of Department of Health and Human Services Task Force on Alzheimer's disease Neurology 1984 34 7 939 944 (Pubitemid 14076461)
    • (1984) Neurology , vol.34 , Issue.7 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3
  • 32
    • 0033975837 scopus 로고    scopus 로고
    • Plasma and cerebrospinal fluid levels of amyloid β proteins 1-40 and 1- 42 in Alzheimer disease
    • Mehta P. D., Pirttil T., Mehta S. P., Sersen E. A., Aisen P. S., Wisniewski H. M., Plasma and cerebrospinal fluid levels of amyloid proteins 1-40 and 1- 42 in Alzheimer disease Archives of Neurology 2000 57 1 100 105 (Pubitemid 30027637)
    • (2000) Archives of Neurology , vol.57 , Issue.1 , 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
  • 33
    • 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., Mizuno T., Mori S., Nakajima K., Fushiki S., Yanagisawa K., Age-dependent change in the levels of A 40 and A 42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of A 42 to A 40 level in cerebrospinal fluid from Alzheimer's disease patients European Neurology 2000 43 3 155 160 (Pubitemid 30189537)
    • (2000) European Neurology , vol.43 , Issue.3 , pp. 155-160
    • Fukuyama, R.1    Mizuno, T.2    Mizuno, T.3    Mori, S.4    Nakajima, K.5    Fushiki, S.6    Yanagisawa, K.7
  • 35
  • 37
    • 80052868367 scopus 로고    scopus 로고
    • Amyloid- 42 is associated with cognitive impairment in healthy elderly and subjective cognitive impairment
    • In press
    • Rolstad S., Berg A. I., Bjerke M., Amyloid- 42 is associated with cognitive impairment in healthy elderly and subjective cognitive impairment. Journal of Alzheimers Disease,. In press
    • Journal of Alzheimers Disease
    • Rolstad, S.1    Berg, A.I.2    Bjerke, M.3
  • 38
    • 72149104756 scopus 로고    scopus 로고
    • Biomarkers for Alzheimer's disease and other forms of dementia: Clinical needs, limitations and future aspects
    • Cedazo-Minguez A., Winblad B., Biomarkers for Alzheimer's disease and other forms of dementia: clinical needs, limitations and future aspects Experimental Gerontology 2010 45 1 5 14
    • (2010) Experimental Gerontology , vol.45 , Issue.1 , pp. 5-14
    • Cedazo-Minguez, A.1    Winblad, B.2
  • 41
    • 42049121409 scopus 로고    scopus 로고
    • Amyloid-related biomarkers for Alzheimer's disease
    • DOI 10.2174/092986708783955572
    • Andreasen N., Zetterberg H., Amyloid-related biomarkers for Alzheimer's disease Current Medicinal Chemistry 2008 15 8 766 771 (Pubitemid 351516792)
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.8 , pp. 766-771
    • Andreasen, N.1    Zetterberg, H.2
  • 45
    • 23844551164 scopus 로고    scopus 로고
    • Amino-terminally truncated Aβ peptide species are the main component of cotton wool plaques
    • DOI 10.1021/bi0508237
    • Miravalle L., Calero M., Takao M., Roher A. E., Ghetti B., Vidal R., Amino-terminally truncated A peptide species are the main component of cotton wool plaques Biochemistry 2005 44 32 10810 10821 (Pubitemid 41153641)
    • (2005) Biochemistry , vol.44 , Issue.32 , pp. 10810-10821
    • Miravalle, L.1    Calero, M.2    Takao, M.3    Roher, A.E.4    Ghetti, B.5    Vidal, R.6
  • 47
    • 33645775230 scopus 로고    scopus 로고
    • Determination of -amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry
    • Portelius E., Westman-Brinkmalm A., Zetterberg H., Blennow K., Determination of -amyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry Journal of Proteome Research 2006 5 4 1010 1016
    • (2006) Journal of Proteome Research , vol.5 , Issue.4 , pp. 1010-1016
    • Portelius, E.1    Westman-Brinkmalm, A.2    Zetterberg, H.3    Blennow, K.4
  • 48
    • 36348970121 scopus 로고    scopus 로고
    • Characterization of amyloid β peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry
    • DOI 10.1021/pr0703627
    • Portelius E., Tran A. J., Andreasson U., Persson R., Brinkmann G., Zetterberg H., Blennow K., Westman-Brinkmalm A., Characterization of amyloid peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry Journal of Proteome Research 2007 6 11 4433 4439 (Pubitemid 350158518)
    • (2007) Journal of Proteome Research , vol.6 , Issue.11 , pp. 4433-4439
    • Portelius, E.1    Tran, A.J.2    Andreasson, U.3    Persson, R.4    Brinkmann, G.5    Zetterberg, H.6    Blennow, K.7    Westman-Brinkmalm, A.8
  • 53
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • DOI 10.1111/j.1471-4159.1993.tb09841.x
    • Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D. B., Characterization of -amyloid peptide from human cerebrospinal fluid Journal of Neurochemistry 1993 61 5 1965 1968 (Pubitemid 23317227)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.5 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 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
    • DOI 10.1046/j.1471-4159.2002.00818.x
    • Wiltfang J., Esselmann H., Bibl M., Smirnov A., Otto M., Paul S., Schmidt B., Klafki H. W., Maler M., Dyrks T., Bienert M., Beyermann M., Rther E., Kornhuber J., Highly conserved and disease-specific patterns of carboxyterminally truncated A peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation Journal of Neurochemistry 2002 81 3 481 496 (Pubitemid 34809327)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.3 , pp. 481-496
    • Wiltfang, J.1    Esselmann, H.2    Bibl, M.3    Smirnov, A.4    Otto, M.5    Paul, S.6    Schmidt, B.7    Klafki, H.-W.8    Maler, M.9    Dyrks, T.10    Bienert, M.11    Beyermann, M.12    Ruther, E.13    Kornhuber, J.14
  • 58
    • 1542722311 scopus 로고    scopus 로고
    • Amyloid β peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: Evidence of novel biomarkers in Alzheimer's disease
    • DOI 10.1016/j.biopsych.2003.10.014, PII S0006322303011259
    • Lewczuk P., Esselmann H., Groemer T. W., Bibl M., Maler J. M., Steinacker P., Otto M., Kornhuber J., Wiltfang J., Amyloid peptides in cerebrospinal fluid as profiled with surface enhanced laser desorption/ionization time-of-flight mass spectrometry: evidence of novel biomarkers in Alzheimer's disease Biological Psychiatry 2004 55 5 524 530 (Pubitemid 38338541)
    • (2004) Biological Psychiatry , vol.55 , Issue.5 , pp. 524-530
    • Lewczuk, P.1    Esselmann, H.2    Groemer, T.W.3    Bibl, M.4    Maler, J.M.5    Steinacker, P.6    Otto, M.7    Kornhuber, J.8    Wiltfang, J.9
  • 59
    • 77953418604 scopus 로고    scopus 로고
    • A novel abeta isoform pattern in CSF reflects gamma-secretase inhibition in Alzheimer disease
    • Portelius E., Dean R. A., Gustavsson M. K., A novel abeta isoform pattern in CSF reflects gamma-secretase inhibition in Alzheimer disease Alzheimers Research Theraphy 2010 2 7 1 7
    • (2010) Alzheimers Research Theraphy , vol.2 , Issue.7 , pp. 1-7
    • Portelius, E.1    Dean, R.A.2    Gustavsson, M.K.3
  • 60
    • 34248190279 scopus 로고    scopus 로고
    • A oligomersa decade of discovery
    • Walsh D. M., Selkoe D. J., A oligomersa decade of discovery Journal of Neurochemistry 2007 101 5 1172 1184
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 61
    • 60549107033 scopus 로고    scopus 로고
    • A specific enzyme-linked immunosorbent assay for measuring -amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer Disease
    • Xia W., Yang T., Shankar G., Smith I. M., Shen Y., Walsh D. M., Selkoe D. J., A specific enzyme-linked immunosorbent assay for measuring -amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer Disease Archives of Neurology 2009 66 2 190 199
    • (2009) Archives of Neurology , vol.66 , Issue.2 , pp. 190-199
    • Xia, W.1    Yang, T.2    Shankar, G.3    Smith, I.M.4    Shen, Y.5    Walsh, D.M.6    Selkoe, D.J.7
  • 63
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D. M., Walsh D. M., Ye C. P., Diehl T., Vasquez S., Vassilev P. M., Teplow D. B., Selkoe D. J., Protofibrillar intermediates of amyloid -protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons Journal of Neuroscience 1999 19 20 8876 8884 (Pubitemid 30226709)
    • (1999) Journal of Neuroscience , vol.19 , Issue.20 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 64
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • DOI 10.1074/jbc.C400260200
    • Kayed R., Sokolov Y., Edmonds B., McIntire T. M., Milton S. C., Hall J. E., Glabe C. G., Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases Journal of Biological Chemistry 2004 279 45 46363 46366 (Pubitemid 39518276)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 67
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh D. M., Klyubin I., Fadeeva J. V., Cullen W. K., Anwyl R., Wolfe M. S., Rowan M. J., Selkoe D. J., Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo Nature 2002 416 6880 535 539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 70
    • 80051665699 scopus 로고    scopus 로고
    • Cognitive effects of cell-derived and synthetically derived Abeta oligomers
    • Reed M. N., Hofmeister J. J., Jungbauer L., Cognitive effects of cell-derived and synthetically derived Abeta oligomers Neurobiology of Aging 2011 32 10 1784 1794
    • (2011) Neurobiology of Aging , vol.32 , Issue.10 , pp. 1784-1794
    • Reed, M.N.1    Hofmeister, J.J.2    Jungbauer, L.3
  • 71
    • 79955769953 scopus 로고    scopus 로고
    • Soluble a oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors
    • Li S., Jin M., Koeglsperger T., Shepardson N. E., Shankar G. M., Selkoe D. J., Soluble a oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors Journal of Neuroscience 2011 31 18 6627 6638
    • (2011) Journal of Neuroscience , vol.31 , Issue.18 , pp. 6627-6638
    • Li, S.1    Jin, M.2    Koeglsperger, T.3    Shepardson, N.E.4    Shankar, G.M.5    Selkoe, D.J.6
  • 72
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheirner's patients by fluorescence correlation spectroscopy
    • DOI 10.1038/nm0798-832
    • Pitschke M., Prior R., Haupt M., Riesner D., Detection of single amyloid -protein aggregates in the cerebrospinal fluid of Alzheirner's patients by fluorescence correlation spectroscopy Nature Medicine 1998 4 7 832 834 (Pubitemid 28331026)
    • (1998) Nature Medicine , vol.4 , Issue.7 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 79
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed R., Head E., Thompson J. L., McIntire T. M., Milton S. C., Cotman C. W., Glabel C. G., Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 2003 300 5618 486 489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , 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    Glabel, C.G.7
  • 83
    • 62049083728 scopus 로고    scopus 로고
    • Direct in vivo intracellular selection of conformation-sensitive antibody domains targeting Alzheimer's amyloid- oligomers
    • Meli G., Visintin M., Cannistraci I., Cattaneo A., Direct in vivo intracellular selection of conformation-sensitive antibody domains targeting Alzheimer's amyloid- oligomers Journal of Molecular Biology 2009 387 3 584 606
    • (2009) Journal of Molecular Biology , vol.387 , Issue.3 , pp. 584-606
    • Meli, G.1    Visintin, M.2    Cannistraci, I.3    Cattaneo, A.4
  • 84
    • 67651236366 scopus 로고    scopus 로고
    • Common key-signals in learning and neurodegeneration: Focus on excito-amino acids, -amyloid peptides and -synuclein
    • Agnati L. F., Leo G., Genedani S., Piron L., Rivera A., Guidolin D., Fuxe K., Common key-signals in learning and neurodegeneration: focus on excito-amino acids, -amyloid peptides and -synuclein Journal of Neural Transmission 2009 116 8 953 974
    • (2009) Journal of Neural Transmission , vol.116 , Issue.8 , pp. 953-974
    • Agnati, L.F.1    Leo, G.2    Genedani, S.3    Piron, L.4    Rivera, A.5    Guidolin, D.6    Fuxe, K.7
  • 85
    • 0034588755 scopus 로고    scopus 로고
    • Volume transmission as a key feature of information handling in the central nervous system possible new interpretative value of the Turing's B-type machine
    • DOI 10.1016/S0079-6123(00)25003-6
    • Agnati L. F., Fuxe K., Volume transmission as a key feature of information handling in the central nervous system possible new interpretative value of the Turing's B-type machine Progress in Brain Research 2000 125 3 19 (Pubitemid 35460791)
    • (2000) Progress in Brain Research , vol.125 , pp. 3-19
    • Agnati, L.F.1    Fuxe, K.2
  • 86
    • 42749092828 scopus 로고    scopus 로고
    • Itinerant exosomes: Emerging roles in cell and tissue polarity
    • Lakkaraju A., Rodriguez-Boulan E., Itinerant exosomes: emerging roles in cell and tissue polarity Trends in Cell Biology 2008 18 5 199 209
    • (2008) Trends in Cell Biology , vol.18 , Issue.5 , pp. 199-209
    • Lakkaraju, A.1    Rodriguez-Boulan, E.2
  • 88
    • 67949097489 scopus 로고    scopus 로고
    • Exosomesvesicular carriers for intercellular communication
    • Simons M., Raposo G., Exosomesvesicular carriers for intercellular communication Current Opinion in Cell Biology 2009 21 4 575 581
    • (2009) Current Opinion in Cell Biology , vol.21 , Issue.4 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 89
    • 70350445977 scopus 로고    scopus 로고
    • Hen or egg? Some thoughts on tunneling nanotubes
    • Rustom A., Hen or egg? Some thoughts on tunneling nanotubes Annals of the New York Academy of Sciences 2009 1178 129 136
    • (2009) Annals of the New York Academy of Sciences , vol.1178 , pp. 129-136
    • Rustom, A.1
  • 90
    • 33845898715 scopus 로고    scopus 로고
    • Aβ peptides as one of the crucial volume transmission signals in the trophic units and their interactions with homocysteine. Physiological implications and relevance for Alzheimer's disease
    • DOI 10.1007/s00702-006-0564-9, Intramembrane receptor-receptor interactions and volume transmission
    • Agnati L. F., Genedani S., Leo G., Forni A., Woods A. S., Filaferro M., Franco R., Fuxe K., A peptides as one of the crucial volume transmission signals in the trophic units and their interactions with homocysteine. Physiological implications and relevance for Alzheimer's disease Journal of Neural Transmission 2007 114 1 21 31 (Pubitemid 46018672)
    • (2007) Journal of Neural Transmission , vol.114 , Issue.1 , pp. 21-31
    • Agnati, L.F.1    Genedani, S.2    Leo, G.3    Forni, A.4    Woods, A.S.5    Filaferro, M.6    Franco, R.7    Fuxe, K.8
  • 91
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis K., Ye Z., Qiu W. Q., Walsh D., Hartley D., Chesneau V., Rosner M. R., Selkoe D. J., Neurons regulate extracellular levels of amyloid -protein via proteolysis by insulin-degrading enzyme Journal of Neuroscience 2000 20 5 1657 1665 (Pubitemid 30220363)
    • (2000) Journal of Neuroscience , vol.20 , Issue.5 , pp. 1657-1665
    • Vekrellis, K.1    Ye, Z.2    Qiu, W.Q.3    Walsh, D.4    Hartley, D.5    Chesneau, V.6    Rosner, M.R.7    Selkoe, D.J.8
  • 93
    • 67149145265 scopus 로고    scopus 로고
    • Detection of amyloid- aggregates in body fluids: A suitable method for early diagnosis of Alzheimer's disease?
    • Funke S. A., Birkmann E., Willbold D., Detection of amyloid- aggregates in body fluids: a suitable method for early diagnosis of Alzheimer's disease? Current Alzheimer Research 2009 6 3 285 289
    • (2009) Current Alzheimer Research , vol.6 , Issue.3 , pp. 285-289
    • Funke, S.A.1    Birkmann, E.2    Willbold, D.3
  • 94
    • 33845591072 scopus 로고    scopus 로고
    • Quantitative analysis of amyloid β peptides in cerebrospinal fluid of Alzheimer's disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography/negative electrospray ionization tandem mass spectrometry
    • DOI 10.1002/rcm.2787
    • Oe T., Ackermann B. L., Inoue K., Berna M. J., Garner C. O., Gelfanova V., Dean R. A., Siemers E. R., Holtzman D. M., Farlow M. R., Blair I. A., Quantitative analysis of amyloid peptides in cerebrospinal fluid of Alzheimer's disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography/negative electrospray ionization tandem mass spectrometry Rapid Communications in Mass Spectrometry 2006 20 24 3723 3735 (Pubitemid 44935325)
    • (2006) Rapid Communications in Mass Spectrometry , vol.20 , Issue.24 , pp. 3723-3735
    • Oe, T.1    Ackermann, B.L.2    Inoue, K.3    Berna, M.J.4    Garner, C.O.5    Gelfanova, V.6    Dean, R.A.7    Siemers, E.R.8    Holtzman, D.M.9    Farlow, M.R.10    Blair, I.A.11
  • 97
    • 43249087541 scopus 로고    scopus 로고
    • Inhibition of γ-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes
    • DOI 10.1096/fj.07-9357com
    • Sharples R. A., Vella L. J., Nisbet R. M., Naylor R., Perez K., Barnham K. J., Masters C. L., Hill A. F., Inhibition of -secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes The Journal of the Federation of American Societies for Experimental Biology 2008 22 5 1469 1478 (Pubitemid 351656787)
    • (2008) FASEB Journal , vol.22 , Issue.5 , pp. 1469-1478
    • Sharples, R.A.1    Vella, L.J.2    Nisbet, R.M.3    Naylor, R.4    Perez, K.5    Barnham, K.J.6    Masters, C.L.7    Hill, A.F.8
  • 98
    • 43049160705 scopus 로고    scopus 로고
    • Exosomes: The Trojan horses of neurodegeneration
    • Ghidoni R., Benussi L., Binetti G., Exosomes: the Trojan horses of neurodegeneration Medical Hypotheses 2008 70 6 1226 1227
    • (2008) Medical Hypotheses , vol.70 , Issue.6 , pp. 1226-1227
    • Ghidoni, R.1    Benussi, L.2    Binetti, G.3
  • 100
    • 77953330985 scopus 로고    scopus 로고
    • A new hypothesis of pathogenesis based on the divorce between mitochondria and their host cells: Possible relevance for alzheimer's disease
    • Agnati L. F., Guidolin D., Baluka F., Leo G., Barlow P. W., Carone C., Genedani S., A new hypothesis of pathogenesis based on the divorce between mitochondria and their host cells: possible relevance for alzheimer's disease Current Alzheimer Research 2010 7 4 307 322
    • (2010) Current Alzheimer Research , vol.7 , Issue.4 , pp. 307-322
    • Agnati, L.F.1    Guidolin, D.2    Baluka, F.3    Leo, G.4    Barlow, P.W.5    Carone, C.6    Genedani, S.7
  • 101
    • 33847076858 scopus 로고    scopus 로고
    • Ganglioside GM1-mediated amyloid-beta fibrillogenesis and membrane disruption
    • Chi E. Y., Frey S. L., Lee K. Y. C., Ganglioside GM1-mediated amyloid-beta fibrillogenesis and membrane disruption Biochemistry 2007 46 7 1913 1924
    • (2007) Biochemistry , vol.46 , Issue.7 , pp. 1913-1924
    • Chi, E.Y.1    Frey, S.L.2    Lee, K.Y.C.3
  • 102
    • 41149088714 scopus 로고    scopus 로고
    • Accelerated release of exosome-associated GM1 ganglioside (GM1) by endocytic pathway abnormality: Another putative pathway for GM1-induced amyloid fibril formation
    • DOI 10.1111/j.1471-4159.2007.05128.x
    • Yuyama K., Yamamoto N., Yanagisawa K., Accelerated release of exosome-associated GM1 ganglioside (GM1) by endocytic pathway abnormality: another putative pathway for GM1-induced amyloid fibril formation Journal of Neurochemistry 2008 105 1 217 224 (Pubitemid 351441638)
    • (2008) Journal of Neurochemistry , vol.105 , Issue.1 , pp. 217-224
    • Yuyama, K.1    Yamamoto, N.2    Yanagisawa, K.3
  • 103
    • 69249159945 scopus 로고    scopus 로고
    • Senescence, apoptosis, and stem cell biology: The rationale for an expanded view of intracrine action
    • Re R. N., Cook J. L., Senescence, apoptosis, and stem cell biology: the rationale for an expanded view of intracrine action American Journal of Physiology, Heart and Circulatory Physiology 2009 297 3 H893 H901
    • (2009) American Journal of Physiology, Heart and Circulatory Physiology , vol.297 , Issue.3
    • Re, R.N.1    Cook, J.L.2
  • 104
    • 79251550418 scopus 로고    scopus 로고
    • Mechanisms of amyloid-beta peptide uptake by neurons: The role of lipid rafts and lipid raft-associated proteins
    • Lai A. Y., McLaurin J., Mechanisms of amyloid-beta peptide uptake by neurons: the role of lipid rafts and lipid raft-associated proteins International Journal of Alzheimer's Disease 2011 2011 11
    • (2011) International Journal of Alzheimer's Disease , vol.2011 , pp. 11
    • Lai, A.Y.1    McLaurin, J.2
  • 105
    • 33746809372 scopus 로고    scopus 로고
    • Physiological roles for amyloid peptides
    • Pearson H. A., Peers C., Physiological roles for amyloid peptides Journal of Physiology 2006 575 1 5 10
    • (2006) Journal of Physiology , vol.575 , Issue.1 , pp. 5-10
    • Pearson, H.A.1    Peers, C.2
  • 109
    • 0022272278 scopus 로고
    • The effects of the fibre environment on the paths taken by regenerating optic nerve fibres in Xenopus
    • Taylor J. S., Gaze R. M., The effects of the fibre environment on the paths taken by regenerating optic nerve fibres in Xenopus Journal of Embryology and Experimental Morphology 1985 89 383 401 (Pubitemid 16211100)
    • (1985) Journal of Embryology and Experimental Morphology , vol.VOL. 89 , pp. 383-401
    • Taylor, J.S.H.1    Gaze, R.M.2
  • 110
    • 0026641612 scopus 로고
    • Neuronal plasticity and ageing processes in the frame of the 'Red Queen Theory'
    • Agnati L. F., Zoli M., Biagini G., Fuxe K., Neuronal plasticity and ageing processes in the frame of the 'Red Queen Theory' Acta Physiologica Scandinavica 1992 145 4 301 309
    • (1992) Acta Physiologica Scandinavica , vol.145 , Issue.4 , pp. 301-309
    • Agnati, L.F.1    Zoli, M.2    Biagini, G.3    Fuxe, K.4
  • 111
    • 0038730942 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor/TrkB signaling in memory processes
    • Yamada K., Nabeshima T., Brain-derived neurotrophic factor/TrkB signaling in memory processes Journal Pharmacological Sciences 2003 91 4 267 270 (Pubitemid 36581946)
    • (2003) Journal Pharmacological Sciences , vol.91 , Issue.4 , pp. 267-270
    • Yamada, K.1    Nabeshima, T.2
  • 112
    • 37849050242 scopus 로고    scopus 로고
    • Neurotrophic factors in Alzheimer's disease: Role of axonal transport
    • Schindowski K., Belarbi K., Buée L., Neurotrophic factors in Alzheimer's disease: role of axonal transport Genes, Brain and Behavior 2008 7 1 43 56
    • (2008) Genes, Brain and Behavior , vol.7 , Issue.1 , pp. 43-56
    • Schindowski, K.1    Belarbi, K.2    Buée, L.3
  • 113
    • 4944258716 scopus 로고    scopus 로고
    • The role of inflammation in Alzheimer's disease
    • DOI 10.1016/j.biocel.2004.07.009, PII S1357272504002699
    • Tuppo E. E., Arias H. R., The role of inflammation in Alzheimer's disease International Journal of Biochemistry and Cell Biology 2005 37 2 289 305 (Pubitemid 39330191)
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , Issue.2 , pp. 289-305
    • Tuppo, E.E.1    Arias, H.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.