메뉴 건너뛰기




Volumn 97, Issue 6, 2018, Pages 1284-1298.e7

Erratum: Tau Kinetics in Neurons and the Human Central Nervous System (Neuron (2018) 97(6) (1284–1298.e7)(S0896627318301363)(10.1016/j.neuron.2018.02.015));Tau Kinetics in Neurons and the Human Central Nervous System

Author keywords

Alzheimer's disease; amyloid; human; induced pluripotent stem cell; isoform; PET; phosphorylation; positron emission tomography; production rate; SILK; stable isotope labeling kinetics; tau

Indexed keywords

TAU PROTEIN; BIOLOGICAL MARKER;

EID: 85044160198     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2018.04.035     Document Type: Erratum
Times cited : (331)

References (80)
  • 4
    • 85044112838 scopus 로고    scopus 로고
    • Tau hyperphosphorylation on T217 in cerebrospinal fluid is specifically associated to amyloid-β pathology
    • Barthélemy, N.R., Bateman, R.J., Marin, P., Becher, F., Sato, C., Lehmann, S., Gabelle, A., Tau hyperphosphorylation on T217 in cerebrospinal fluid is specifically associated to amyloid-β pathology. bioRxiv, 2017, 10.1101/226977.
    • (2017) bioRxiv
    • Barthélemy, N.R.1    Bateman, R.J.2    Marin, P.3    Becher, F.4    Sato, C.5    Lehmann, S.6    Gabelle, A.7
  • 5
    • 33745920161 scopus 로고    scopus 로고
    • Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo
    • Bateman, R.J., Munsell, L.Y., Morris, J.C., Swarm, R., Yarasheski, K.E., Holtzman, D.M., Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo. Nat. Med. 12 (2006), 856–861.
    • (2006) Nat. Med. , vol.12 , pp. 856-861
    • Bateman, R.J.1    Munsell, L.Y.2    Morris, J.C.3    Swarm, R.4    Yarasheski, K.E.5    Holtzman, D.M.6
  • 7
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat, J., Gustke, N., Drewes, G., Mandelkow, E.M., Mandelkow, E., Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11 (1993), 153–163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 9
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278–284
    • Braak, H., Braak, E., Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16 (1995), 271–278 discussion 278–284.
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 13
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns, N.J., Bigio, E.H., Mackenzie, I.R.A., Neumann, M., Lee, V.M.-Y., Hatanpaa, K.J., White, C.L. 3rd, Schneider, J.A., Grinberg, L.T., Halliday, G., et al., Consortium for Frontotemporal Lobar Degeneration. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol. 114 (2007), 5–22.
    • (2007) Acta Neuropathol. , vol.114 , pp. 5-22
    • Cairns, N.J.1    Bigio, E.H.2    Mackenzie, I.R.A.3    Neumann, M.4    Lee, V.M.-Y.5    Hatanpaa, K.J.6    White, C.L.7    Schneider, J.A.8    Grinberg, L.T.9    Halliday, G.10
  • 14
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel, G., Mager, E.M., Binder, L.I., Kuret, J., The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 271 (1996), 32789–32795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 15
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • Chai, X., Dage, J.L., Citron, M., Constitutive secretion of tau protein by an unconventional mechanism. Neurobiol. Dis. 48 (2012), 356–366.
    • (2012) Neurobiol. Dis. , vol.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 16
    • 84973572645 scopus 로고    scopus 로고
    • Pathological conformations involving the amino terminus of tau occur early in Alzheimer's disease and are differentially detected by monoclonal antibodies
    • Combs, B., Hamel, C., Kanaan, N.M., Pathological conformations involving the amino terminus of tau occur early in Alzheimer's disease and are differentially detected by monoclonal antibodies. Neurobiol. Dis. 94 (2016), 18–31.
    • (2016) Neurobiol. Dis. , vol.94 , pp. 18-31
    • Combs, B.1    Hamel, C.2    Kanaan, N.M.3
  • 23
    • 80855138704 scopus 로고    scopus 로고
    • Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau)
    • Dickson, D.W., Kouri, N., Murray, M.E., Josephs, K.A., Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau). J. Mol. Neurosci. 45 (2011), 384–389.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 384-389
    • Dickson, D.W.1    Kouri, N.2    Murray, M.E.3    Josephs, K.A.4
  • 26
    • 0026047799 scopus 로고
    • Estrogen-enhanced neurite growth: evidence for a selective induction of Tau and stable microtubules
    • Ferreira, A., Caceres, A., Estrogen-enhanced neurite growth: evidence for a selective induction of Tau and stable microtubules. J. Neurosci. 11 (1991), 392–400.
    • (1991) J. Neurosci. , vol.11 , pp. 392-400
    • Ferreira, A.1    Caceres, A.2
  • 29
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R.L., Diamond, M.I., Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284 (2009), 12845–12852.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 30
    • 84940707250 scopus 로고    scopus 로고
    • Distinct therapeutic mechanisms of Tau antibodies: promoting microglial clearance versus blocking neuronal uptake
    • Funk, K.E., Mirbaha, H., Jiang, H., Holtzman, D.M., Diamond, M.I., Distinct therapeutic mechanisms of Tau antibodies: promoting microglial clearance versus blocking neuronal uptake. J. Biol. Chem. 290 (2015), 21652–21662.
    • (2015) J. Biol. Chem. , vol.290 , pp. 21652-21662
    • Funk, K.E.1    Mirbaha, H.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 33
    • 1642280378 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau protein alters its ability for self-aggregation
    • Haase, C., Stieler, J.T., Arendt, T., Holzer, M., Pseudophosphorylation of tau protein alters its ability for self-aggregation. J. Neurochem. 88 (2004), 1509–1520.
    • (2004) J. Neurochem. , vol.88 , pp. 1509-1520
    • Haase, C.1    Stieler, J.T.2    Arendt, T.3    Holzer, M.4
  • 35
    • 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., Anderton, B.H., New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J. Neurochem. 71 (1998), 2465–2476.
    • (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
  • 39
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • Iba, M., Guo, J.L., McBride, J.D., Zhang, B., Trojanowski, J.Q., Lee, V.M.-Y., Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J. Neurosci. 33 (2013), 1024–1037.
    • (2013) J. Neurosci. , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 40
    • 84938490181 scopus 로고    scopus 로고
    • C-terminally truncated forms of Tau, but not full-length Tau or its C-terminal fragments, are released from neurons independently of cell death
    • Kanmert, D., Cantlon, A., Muratore, C.R., Jin, M., O'Malley, T.T., Lee, G., Young-Pearse, T.L., Selkoe, D.J., Walsh, D.M., C-terminally truncated forms of Tau, but not full-length Tau or its C-terminal fragments, are released from neurons independently of cell death. J. Neurosci. 35 (2015), 10851–10865.
    • (2015) J. Neurosci. , vol.35 , pp. 10851-10865
    • Kanmert, D.1    Cantlon, A.2    Muratore, C.R.3    Jin, M.4    O'Malley, T.T.5    Lee, G.6    Young-Pearse, T.L.7    Selkoe, D.J.8    Walsh, D.M.9
  • 41
    • 84871141635 scopus 로고    scopus 로고
    • Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies
    • Karch, C.M., Jeng, A.T., Goate, A.M., Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies. J. Biol. Chem. 287 (2012), 42751–42762.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42751-42762
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 42
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of Tau aggregation by fibrillar species
    • Kfoury, N., Holmes, B.B., Jiang, H., Holtzman, D.M., Diamond, M.I., Trans-cellular propagation of Tau aggregation by fibrillar species. J. Biol. Chem. 287 (2012), 19440–19451.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 43
    • 0027534625 scopus 로고
    • Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease
    • Liu, W.-K., Moore, W.T., Williams, R.T., Hall, F.L., Yen, S.-H., Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease. J. Neurosci. Res. 34 (1993), 371–376.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 371-376
    • Liu, W.-K.1    Moore, W.T.2    Williams, R.T.3    Hall, F.L.4    Yen, S.-H.5
  • 45
    • 84964575878 scopus 로고    scopus 로고
    • Co-immunoprecipitation with Tau isoform-specific antibodies reveals distinct protein interactions and highlights a putative role for 2N Tau in disease
    • Liu, C., Song, X., Nisbet, R., Götz, J., Co-immunoprecipitation with Tau isoform-specific antibodies reveals distinct protein interactions and highlights a putative role for 2N Tau in disease. J. Biol. Chem. 291 (2016), 8173–8188.
    • (2016) J. Biol. Chem. , vol.291 , pp. 8173-8188
    • Liu, C.1    Song, X.2    Nisbet, R.3    Götz, J.4
  • 46
    • 84930966153 scopus 로고    scopus 로고
    • Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody
    • Luo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., Paul, S.M., Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody. Sci. Rep., 5, 2015, 11161.
    • (2015) Sci. Rep. , vol.5 , pp. 11161
    • Luo, W.1    Liu, W.2    Hu, X.3    Hanna, M.4    Caravaca, A.5    Paul, S.M.6
  • 48
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow, E.-M., Stamer, K., Vogel, R., Thies, E., Mandelkow, E., Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol. Aging 24 (2003), 1079–1085.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.-M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 52
    • 70350455151 scopus 로고    scopus 로고
    • Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway
    • Morita, T., Sobue, K., Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway. J. Biol. Chem. 284 (2009), 27734–27745.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27734-27745
    • Morita, T.1    Sobue, K.2
  • 53
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of Tau in the central nervous system
    • Papasozomenos, S.C., Binder, L.I., Phosphorylation determines two distinct species of Tau in the central nervous system. Cell Motil. Cytoskeleton 8 (1987), 210–226.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 55
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • Pooler, A.M., Phillips, E.C., Lau, D.H.W., Noble, W., Hanger, D.P., Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep. 14 (2013), 389–394.
    • (2013) EMBO Rep. , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.W.3    Noble, W.4    Hanger, D.P.5
  • 56
    • 84886509822 scopus 로고    scopus 로고
    • A role for tau at the synapse in Alzheimer's disease pathogenesis
    • Pooler, A.M., Noble, W., Hanger, D.P., A role for tau at the synapse in Alzheimer's disease pathogenesis. Neuropharmacology 76:Pt A (2014), 1–8.
    • (2014) Neuropharmacology , vol.76 , pp. 1-8
    • Pooler, A.M.1    Noble, W.2    Hanger, D.P.3
  • 60
    • 0031955835 scopus 로고    scopus 로고
    • Correction for partial volume effects in PET: principle and validation
    • Rousset, O.G., Ma, Y., Evans, A.C., Correction for partial volume effects in PET: principle and validation. J. Nucl. Med. 39 (1998), 904–911.
    • (1998) J. Nucl. Med. , vol.39 , pp. 904-911
    • Rousset, O.G.1    Ma, Y.2    Evans, A.C.3
  • 62
    • 84990061214 scopus 로고    scopus 로고
    • Human iPSC-derived neuronal model of Tau-A152T frontotemporal dementia reveals Tau-mediated mechanisms of neuronal vulnerability
    • Silva, M.C., Cheng, C., Mair, W., Almeida, S., Fong, H., Biswas, M.H.U., Zhang, Z., Huang, Y., Temple, S., Coppola, G., et al. Human iPSC-derived neuronal model of Tau-A152T frontotemporal dementia reveals Tau-mediated mechanisms of neuronal vulnerability. Stem Cell Reports 7 (2016), 325–340.
    • (2016) Stem Cell Reports , vol.7 , pp. 325-340
    • Silva, M.C.1    Cheng, C.2    Mair, W.3    Almeida, S.4    Fong, H.5    Biswas, M.H.U.6    Zhang, Z.7    Huang, Y.8    Temple, S.9    Coppola, G.10
  • 64
    • 84940664560 scopus 로고    scopus 로고
    • Developmental regulation of tau splicing is disrupted in stem cell-derived neurons from frontotemporal dementia patients with the 10 + 16 splice-site mutation in MAPT
    • Sposito, T., Preza, E., Mahoney, C.J., Setó-Salvia, N., Ryan, N.S., Morris, H.R., Arber, C., Devine, M.J., Houlden, H., Warner, T.T., et al. Developmental regulation of tau splicing is disrupted in stem cell-derived neurons from frontotemporal dementia patients with the 10 + 16 splice-site mutation in MAPT. Hum. Mol. Genet. 24 (2015), 5260–5269.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 5260-5269
    • Sposito, T.1    Preza, E.2    Mahoney, C.J.3    Setó-Salvia, N.4    Ryan, N.S.5    Morris, H.R.6    Arber, C.7    Devine, M.J.8    Houlden, H.9    Warner, T.T.10
  • 65
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: physiological and pathological consequences
    • Stoothoff, W.H., Johnson, G.V.W., Tau phosphorylation: physiological and pathological consequences. Biochim. Biophys. Acta 1739 (2005), 280–297.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.W.2
  • 68
    • 67649622427 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization
    • Sun, Q., Gamblin, T.C., Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization. Biochemistry 48 (2009), 6002–6011.
    • (2009) Biochemistry , vol.48 , pp. 6002-6011
    • Sun, Q.1    Gamblin, T.C.2
  • 69
    • 0027388775 scopus 로고
    • Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location
    • Szendrei, G.I., Lee, V.M.-Y., Otvos, L. Jr., Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location. J. Neurosci. Res. 34 (1993), 243–249.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 243-249
    • Szendrei, G.I.1    Lee, V.M.-Y.2    Otvos, L.3
  • 70
    • 33747195353 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors
    • Takahashi, K., Yamanaka, S., Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell 126 (2006), 663–676.
    • (2006) Cell , vol.126 , pp. 663-676
    • Takahashi, K.1    Yamanaka, S.2
  • 71
    • 84888201046 scopus 로고    scopus 로고
    • Longitudinal change in CSF Tau and Aβ biomarkers for up to 48 months in ADNI
    • Toledo, J.B., Xie, S.X., Trojanowski, J.Q., Shaw, L.M., Longitudinal change in CSF Tau and Aβ biomarkers for up to 48 months in ADNI. Acta Neuropathol. 126 (2013), 659–670.
    • (2013) Acta Neuropathol. , vol.126 , pp. 659-670
    • Toledo, J.B.1    Xie, S.X.2    Trojanowski, J.Q.3    Shaw, L.M.4
  • 73
    • 84951567833 scopus 로고    scopus 로고
    • Tau in physiology and pathology
    • Wang, Y., Mandelkow, E., Tau in physiology and pathology. Nat. Rev. Neurosci. 17 (2016), 5–21.
    • (2016) Nat. Rev. Neurosci. , vol.17 , pp. 5-21
    • Wang, Y.1    Mandelkow, E.2
  • 78
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T.E., Ma, S., Maloney, S.E., Wozniak, D.F., Diamond, M.I., Holtzman, D.M., Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 80 (2013), 402–414.
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1    Kfoury, N.2    Jiang, H.3    Mahan, T.E.4    Ma, S.5    Maloney, S.E.6    Wozniak, D.F.7    Diamond, M.I.8    Holtzman, D.M.9
  • 79
    • 85014531490 scopus 로고    scopus 로고
    • Shared genetic risk between corticobasal degeneration, progressive supranuclear palsy, and frontotemporal dementia
    • Yokoyama, J.S., Karch, C.M., Fan, C.C., Bonham, L.W., Kouri, N., Ross, O.A., Rademakers, R., Kim, J., Wang, Y., Höglinger, G.U., et al., International FTD-Genomics Consortium (IFGC). Shared genetic risk between corticobasal degeneration, progressive supranuclear palsy, and frontotemporal dementia. Acta Neuropathol. 133 (2017), 825–837.
    • (2017) Acta Neuropathol. , vol.133 , pp. 825-837
    • Yokoyama, J.S.1    Karch, C.M.2    Fan, C.C.3    Bonham, L.W.4    Kouri, N.5    Ross, O.A.6    Rademakers, R.7    Kim, J.8    Wang, Y.9    Höglinger, G.U.10
  • 80
    • 85025167025 scopus 로고    scopus 로고
    • Axodendritic sorting and pathological missorting of Tau are isoform-specific and determined by axon initial segment architecture
    • Zempel, H., Dennissen, F.J.A., Kumar, Y., Luedtke, J., Biernat, J., Mandelkow, E.-M., Mandelkow, E., Axodendritic sorting and pathological missorting of Tau are isoform-specific and determined by axon initial segment architecture. J. Biol. Chem. 292 (2017), 12192–12207.
    • (2017) J. Biol. Chem. , vol.292 , pp. 12192-12207
    • Zempel, H.1    Dennissen, F.J.A.2    Kumar, Y.3    Luedtke, J.4    Biernat, J.5    Mandelkow, E.-M.6    Mandelkow, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.