Ver registro no DEDALUS
Exportar registro bibliográfico

Metrics


Metrics:

Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation (2013)

  • Authors:
  • USP affiliated authors: GRINBERG, LEA TENENHOLZ - FM
  • USP Schools: FM
  • DOI: 10.1007/s00401-013-1080-2
  • Subjects: AUTÓPSIA; IMUNOHISTOQUÍMICA; ANTICORPOS MONOCLONAIS; SISTEMA NERVOSO CENTRAL
  • Language: Inglês
  • Imprenta:
  • Source:
  • Acesso online ao documento

    Online accessDOI or search this record in
    Informações sobre o DOI: 10.1007/s00401-013-1080-2 (Fonte: oaDOI API)
    • Este periódico é de assinatura
    • Este artigo é de acesso aberto
    • URL de acesso aberto
    • Cor do Acesso Aberto: green
    Versões disponíveis em Acesso Aberto do: 10.1007/s00401-013-1080-2 (Fonte: Unpaywall API)

    Título do periódico: Acta Neuropathologica

    ISSN: 0001-6322,1432-0533

    • Melhor URL em Acesso Aberto:


    • Outras alternativas de URLs em Acesso Aberto:


        • Página do artigo
        • Evidência: oa repository (via pmcid lookup)
        • Licença:
        • Versão: acceptedVersion
        • Tipo de hospedagem: repository


    Informações sobre o Citescore
  • Título: Acta Neuropathologica

    ISSN: 0001-6322

    Citescore - 2017: 11.82

    SJR - 2017: 7.589

    SNIP - 2017: 3.347


  • Exemplares físicos disponíveis nas Bibliotecas da USP
    BibliotecaCód. de barrasNúm. de chamada
    FM2348441-10BCSEP 176 2013
    How to cite
    A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas

    • ABNT

      GRINBERG, Lea Tenenholz; WANG, Xuehua; WANG, Chao; et al. Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation. Acta Neuropathologica, Berlin, v. 125, n. 4, p. 581-593, 2013. Disponível em: < http://link.springer.com/content/pdf/10.1007%2Fs00401-013-1080-2.pdf > DOI: 10.1007/s00401-013-1080-2.
    • APA

      Grinberg, L. T., Wang, X., Wang, C., Sohn, P. D., Theofilas, P., Sidhu, M., et al. (2013). Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation. Acta Neuropathologica, 125( 4), 581-593. doi:10.1007/s00401-013-1080-2
    • NLM

      Grinberg LT, Wang X, Wang C, Sohn PD, Theofilas P, Sidhu M, Arevalo JB, Heinsen H, Huang EJ, Rosen H, Miller BL, Gan L, Seeley WW. Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation [Internet]. Acta Neuropathologica. 2013 ; 125( 4): 581-593.Available from: http://link.springer.com/content/pdf/10.1007%2Fs00401-013-1080-2.pdf
    • Vancouver

      Grinberg LT, Wang X, Wang C, Sohn PD, Theofilas P, Sidhu M, Arevalo JB, Heinsen H, Huang EJ, Rosen H, Miller BL, Gan L, Seeley WW. Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation [Internet]. Acta Neuropathologica. 2013 ; 125( 4): 581-593.Available from: http://link.springer.com/content/pdf/10.1007%2Fs00401-013-1080-2.pdf

    Referências citadas na obra
    Ahmed Z, Doherty KM, Silveira-Moriyama L, Bandopadhyay R, Lashley T, Mamais A et al (2011) Globular glial tauopathies (GGT) presenting with motor neuron disease or frontotemporal dementia: an emerging group of 4-repeat tauopathies. Acta Neuropathol 122:28–415
    Ballatore C, Lee VM, Trojanowski JQ (2007) Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders. Nat Rev Neurosci 8:663–672
    Berg L, McKeel DW Jr, Miller JP, Storandt M, Rubin EH, Morris JC et al (1998) Clinicopathologic studies in cognitively healthy aging and Alzheimer’s disease: relation of histologic markers to dementia severity, age, sex, and apolipoprotein E genotype. Arch Neurol 55:326–335
    Braak H, Braak E (1989) Cortical and subcortical argyrophilic grains characterize a disease associated with adult onset dementia. Neuropathol Appl Neurobiol 15:13–26
    Braak H, Thal DR, Ghebremedhin E, Del Tredici K (2011) Stages of the pathologic process in Alzheimer disease: age categories from 1 to 100 years. J Neuropathol Exp Neurol 70:960–969
    Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Rev 33:95–130
    Buee L, Delacourte A (1999) Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick’s disease. Brain Pathol 9:681–693
    Cairns NJ, Bigio EH, Mackenzie IR, Neumann M, Lee VM, Hatanpaa KJ et al (2007) Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol 114:5–22
    Cohen P, Frame S (2001) The renaissance of GSK3. Nat Rev Mol Cell Biol 2:769–776
    Cohen TJ, Guo JL, Hurtado DE, Kwong LK, Mills IP, Trojanowski JQ et al (2011) The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun 2:252
    Duyckaerts C (2004) Looking for the link between plaques and tangles. Neurobiol Aging 25:735–739
    Ferrer I, Barrachina M, Tolnay M, Rey MJ, Vidal N, M Carmona et al (2003) Phosphorylated protein kinases associated with neuronal and glial tau deposits in argyrophilic grain disease. Brain Pathol 13:62–78
    Ferrer I, Santpere G, van Leeuwen FW (2008) Argyrophilic grain disease. Brain 131:1416–1432
    Giannakopoulos P, Gold G, Kovari E, von Gunten A, Imhof A, Bouras C et al (2007) Assessing the cognitive impact of Alzheimer disease pathology and vascular burden in the aging brain: the Geneva experience. Acta Neuropathol 113:1–12
    Goedert M (2001) The significance of tau and alpha-synuclein inclusions in neurodegenerative diseases. Curr Opin Genet Dev 11:343–351
    Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron 3:519–526
    Goedert M, Spillantini MG, Potier MC, Ulrich J, Crowther RA (1989) Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J 8:393–399
    Goode BL, Denis PE, Panda D, Radeke MJ, Miller HP, L Wilson et al (1997) Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly. Mol Biol Cell 8:353–365
    Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (1998) New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer’s disease brain using nanoelectrospray mass spectrometry. J Neurochem 71:2465–2476
    Hodges JR, Davies RR, Xuereb JH, Casey B, Broe M, Bak TH et al (2004) Clinicopathological correlates in frontotemporal dementia. Ann Neurol 56:399–406
    Ilieva EV, Kichev A, Naudi A, Ferrer I, Pamplona R, Portero-Otin M (2011) Mitochondrial dysfunction and oxidative and endoplasmic reticulum stress in argyrophilic grain disease. J Neuropathol Exp Neurol 70:253–263
    Irwin DJ, Cohen TJ, Grossman M, Arnold SE, Xie SX, Lee VM et al (2012) Acetylated tau, a novel pathological signature in Alzheimer’s disease and other tauopathies. Brain 135:807–818
    Jicha GA, Petersen RC, Knopman DS, Boeve BF, Smith GE, Geda YE et al (2006) Argyrophilic grain disease in demented subjects presenting initially with amnestic mild cognitive impairment. J Neuropathol Exp Neurol 65:602–609
    Knopman DS, Parisi JE, Salviati A, Floriach-Robert M, Boeve BF, Ivnik RJ et al (2003) Neuropathology of cognitively normal elderly. J Neuropathol Exp Neurol 62:1087–1095
    Kovacs GG, Majtenyi K, Spina S, Murrell JR, Gelpi E, Hoftberger R et al (2008) White matter tauopathy with globular glial inclusions: a distinct sporadic frontotemporal lobar degeneration. J Neuropathol Exp Neurol 67:963–975
    Lee G, Neve RL, Kosik KS (1989) The microtubule binding domain of tau protein. Neuron 2:1615–1624
    Mandelkow EM, Mandelkow E (2012) Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb Perspect Med 2:a006247
    Maurage CA, Sergeant N, Schraen-Maschke S, Lebert F, Ruchoux MM, Sablonniere B et al (2003) Diffuse form of argyrophilic grain disease: a new variant of four-repeat tauopathy different from limbic argyrophilic grain disease. Acta Neuropathol 106:575–583
    Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, Seeley WW et al (2010) Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67:953–966
    Petersen RC, Parisi JE, Dickson DW, Johnson KA, Knopman DS, Boeve BF et al (2006) Neuropathologic features of amnestic mild cognitive impairment. Arch Neurol 63:665–672
    Steuerwald GM, Baumann TP, Taylor KI, Mittag M, Adams H, Tolnay M et al (2007) Clinical characteristics of dementia associated with argyrophilic grain disease. Dement Geriatr Cogn Disord 24:229–234
    Thal DR, Schultz C, Botez G, Del Tredici K, Mrak RE, Griffin WS et al (2005) The impact of argyrophilic grain disease on the development of dementia and its relationship to concurrent Alzheimer’s disease-related pathology. Neuropathol Appl Neurobiol 31:270–279
    Tolnay M, Clavaguera F (2004) Argyrophilic grain disease: a late-onset dementia with distinctive features among tauopathies. Neuropathology 24:269–283
    Tolnay M, Schwietert M, Monsch AU, Staehelin HB, Langui D, Probst A (1997) Argyrophilic grain disease: distribution of grains in patients with and without dementia. Acta Neuropathol 94:353–358
    Tolnay M, Sergeant N, Ghestem A, Chalbot S, De Vos RA, Jansen Steur EN et al (2002) Argyrophilic grain disease and Alzheimer’s disease are distinguished by their different distribution of tau protein isoforms. Acta Neuropathol 104:425–434