Tau and tauopathies

The evolution of Alzheimer's disease‐related cytoskeletal pathology in the human raphe nuclei

Rüb, U., Tredici, K. D., Schultz, C., Thal, D. R., Braak, E., & Braak, H. (2000) · Neuropathology and Applied Neurobiology · doi:10.1046/j.0305-1846.2000.00291.x · Cited by 134

Pick's disease associated with the novel Tau gene mutation K369I

Neumann, M., Schulz‐Schaeffer, W., Crowther, R. A., Smith, M. J., Spillantini, M. G., Goedert, M., & Kretzschmar, H. A. (2001) · Annals of Neurology · doi:10.1002/ana.1223 · Cited by 134

The influence of phospho-tau on dendritic spines of cortical pyramidal neurons in patients with Alzheimer’s disease

Merino-Serrais, P., Benavides-Piccione, R., Blazquez-Llorca, L., Kastanauskaite, A., Rábano, A., Avila, J., & DeFelipe, J. (2013) · Brain · doi:10.1093/brain/awt088 · Cited by 134

Insulin dysfunction and Tau pathology

Khoury, N. B. E., Gratuze, M., Papon, M.-A., Bretteville, A., & Planel, E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00022 · Cited by 133

Pre‐synaptic C‐terminal truncated tau is released from cortical synapses in Alzheimer's disease

Sokolow, S., Henkins, K. M., Bilousova, T., Gonzalez, B., Vinters, H. V., Miller, C. A., Cornwell, L., Poon, W. W., & Gylys, K. H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12991 · Cited by 133

Axonal Degeneration Induced by Targeted Expression of Mutant Human Tau in Oligodendrocytes of Transgenic Mice That Model Glial Tauopathies

Higuchi, M., Zhang, B., Forman, M. S., Yoshiyama, Y., Trojanowski, J. Q., & Lee, V. M. ‐. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2691-05.2005 · Cited by 133

Effect of Phosphorylation on α-Helix Stability as a Function of Position

Andrew, C. D., Warwicker, J., Jones, G. R., & Doig, A. J. (2002) · Biochemistry · doi:10.1021/bi0113216 · Cited by 133

Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38δ at Thr50 promotes microtubule assembly

Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M., & Cuenda, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.01655 · Cited by 133

Frontotemporal Lobar Degeneration: Epidemiology, Pathology, Diagnosis and Management

Seltman, R. E., & Matthews, B. R. (2012) · CNS Drugs · doi:10.2165/11640070-000000000-00000 · Cited by 132

Paired helical filament-like phosphorylation of tau, deposition of β/A4-amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A

Arendt, T., Holzer, M., Fruth, R., Brückner, M. K., & Gärtner, U. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00347-l · Cited by 132

Conversion of Serine to Aspartate Imitates Phosphorylation-induced Changes in the Structure and Function of Microtubule-associated Protein Tau

Léger, J. G., Kempf, M., Lee, G. S., & Brandt, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8441 · Cited by 131

Structural Impact of Tau Phosphorylation at Threonine 231

Schwalbe, M., Kadavath, H., Biernat, J., Ozenne, V., Blackledge, M. J., Mandelkow�, E., & Zweckstetter, M. (2015) · Structure · doi:10.1016/j.str.2015.06.002 · Cited by 130

NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss

Tackenberg, C., Grinschgl, S., Trutzel, A., Santuccione, A. C., Frey, M. C., Konietzko, U., Grimm, J., Brandt, R., & Nitsch, R. M. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.129 · Cited by 130

White Matter Tauopathy With Globular Glial Inclusions: A Distinct Sporadic Frontotemporal Lobar Degeneration

Kovács, G. G., Majtényi, K., Spina, S., Murrell, J. R., Gelpí, E., Höftberger, R., Fraser, G. M., Crowther, R. A., Goedert, M., Budka, H., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318187a80f · Cited by 130

Semantic dementia with ubiquitin-positive tau-negative inclusion bodies

Rossor, M. N., Révész, T., Lantos, P. L., & Warrington, E. K. (2000) · Brain · doi:10.1093/brain/123.2.267 · Cited by 130

Correlations between mental state and quantitative neuropathology in the Vienna Longitudinal Study on Dementia

Bancher, C., Jellinger, K., Lassmann, H., Fischer, P., & Leblhuber, F. (1996) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/bf02189115 · Cited by 130

Ki‐67 Immunoreactivity in Alzheimer's Disease and Other Neurodegenerative Disorders

Smith, T. W., & Lippa, C. (1995) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199505000-00002 · Cited by 129

Tau interaction with microtubules in vivo

Samsonov, A., Yu, J.-Z., Rasenick, M., & Popov, S. V. (2004) · Journal of Cell Science · doi:10.1242/jcs.01531 · Cited by 129

Characterization of the Inhibition of Protein Phosphatase-1 by DARPP-32 and Inhibitor-2

Huang, H.-B., Horiuchi, A., Watanabe, T., Shih, S.-R., Tsay, H.-J., Li, H., Greengard, P., & Nairn, A. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7870 · Cited by 129

Binding to the Minor Groove of the Double-Strand, Tau Protein Prevents DNA from Damage by Peroxidation

Wei, Y., Qu, M.-H., Wang, X.-S., Chen, L., Wang, D.-L., Liu, Y., Hua, Q., & He, R.-Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002600 · Cited by 129

Expression of microtubule-associated proteins MAP2 and tau in cultured rat brain oligodendrocytes

Müller, R., Heinrich, M., Heck, S., Blohm, D., & Richter-Landsberg, C. (1997) · Cell and Tissue Research · doi:10.1007/s004410050809 · Cited by 127

Divergent Pathways Mediate Spine Alterations and Cell Death Induced by Amyloid-β, Wild-Type Tau, and R406W Tau

Tackenberg, C., & Brandt, R. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3590-09.2009 · Cited by 127

Late onset of Huntington's disease.

Myers, R. H., Sax, D. S., Schoenfeld, M., Bird, E. D., Wolf, P. A., Vonsattel, J. P., White, R. F., & Martin, J. B. (1985) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.48.6.530 · Cited by 127

The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome

Gunawardana, C. G., Mehrabian, M., Wang, X., Mueller, I., Lubambo, I., Jonkman, J. E. N., Wang, H., & Schmitt‐Ulms, G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.050724 · Cited by 127

Pathogenesis of the Tauopathies

Goedert, M., & Spillantini, M. G. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9593-4 · Cited by 126

Dementia in a punch-drunk wife

Roberts, G. W., Whitwell, H., Acland, P. R., & Bruton, C. J. (1990) · The Lancet · doi:10.1016/0140-6736(90)90520-f · Cited by 126

Presence of tau in isolated nuclei from human brain

Rady, R. M., Zinkowski, R. P., & Binder, L. I. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00023-8 · Cited by 126

SUPRANUCLEAR OPHTHALMOPLEGIA, PSEUDOBULBAR PALSY, NUCHAL DYSTONIA AND DEMENTIA. A CLINICAL REPORT ON EIGHT CASES OF "HETEROGENOUS SYSTEM DEGENERATION".

Richardson, J. C., Steele, J. C., & Olszewski, J. (1963) · PubMed · Cited by 125

Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors

Wang, J., Gao, Q., Wang, Y., Lafyatis, R., Stamm, S., & Andreadis, A. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02232.x · Cited by 125

Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated .tau. proteins and inhibition of phosphorylation of .tau. proteins by protein kinase C

Baudier, J., Mochly‐Rosen, D., Newton, A. C., et al. (1987) · Biochemistry · doi:10.1021/bi00384a033 · Cited by 125

Missense and splice site mutations in tau associated with FTDP-17: Multiple pathogenic mechanisms

Hutton, M. L. (2001) · Neurology · doi:10.1212/wnl.56.suppl_4.s21 · Cited by 125

Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia

Stanford, P. M. (2003) · Brain · doi:10.1093/brain/awg090 · Cited by 125

Connecting the dots between tau dysfunction and neurodegeneration

Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124

Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer’s and Parkinson’s disease brains

Askanas, V., & Engel, W. K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0449-0 · Cited by 124

Somatodendritic localization of phosphorylated tau in neonatal and adult rat cerebral cortex

Tashiro, K., Hasegawa, M., Ihara, Y., & Iwatsubo, T. (1997) · Neuroreport · doi:10.1097/00001756-199708180-00029 · Cited by 123

The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian Hibernation

Stieler, J., Bullmann, T., Kohl, F., Tøien, Ø., Brückner, M. K., Härtig, W., Barnes, B. M., & Arendt, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014530 · Cited by 123

Starvation induces tau hyperphosphorylation in mouse brain: implications for Alzheimer's disease

Yanagisawa, M., Planel, E., Ishiguro, K., & Fujita, S. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01480-5 · Cited by 123

Membrane‐bound β‐amyloid oligomers are recruited into lipid rafts by a fyn‐dependent mechanism

Williamson, R., Usardi, A., Hanger, D. P., & Anderton, B. H. (2007) · The FASEB Journal · doi:10.1096/fj.07-9766com · Cited by 123

PTL-1, a microtubule-associated protein with tau-like repeats from the nematode Caenorhabditis elegans

Goedert, M., Baur, C.-P., Ahringer, J., Jakes, R., Hasegawa, M., Spillantini, M. G., Smith, M. J., & Hill, F. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.11.2661 · Cited by 123

Calmodulin binds to both microtubule-associated protein 2 and tau proteins.

Lee, Y. C., & Wolff, J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43592-7 · Cited by 122

Neurofibrillary degeneration in amyotrophic lateral sclerosis/parkinsonism-dementia complex of Guam. Immunochemical characterization of tau proteins.

Buée‐Scherrer, V., Buée, L., Hof, P. R., Leveugle, B., Mourton-Gilles, C., Loerzel, A. J., Perl, D. P., & Delacourte, A. (1995) · Europe PMC (PubMed Central) · Cited by 122

Cortical distribution of neurofibrillary tangles in Alzheimer's disease matches the pattern of neurons that retain their capacity of plastic remodelling in the adult brain

Arendt, T., Brückner, M. K., Gertz, H.-J., & Marcova, L. (1998) · Neuroscience · doi:10.1016/s0306-4522(97)00509-5 · Cited by 122

Quantitative neuropathologic analysis of Pick's disease cases: cortical distribution of Pick bodies and coexistence with Alzheimer's disease

Hof, P. R., Bouras, C., Perl, D. P., & Morrison, J. H. (1994) · Acta Neuropathologica · doi:10.1007/bf00296179 · Cited by 122

Direct evidence of phosphorylated neuronal intermediate filament proteins in neurofibrillary tangles (NFTs): phosphoproteomics of Alzheimer's NFTs

Rudrabhatla, P., Jaffe, H., & Pant, H. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-181297 · Cited by 121

Expression of the Small Heat-Shock Protein αB-Crystallin in Tauopathies with Glial Pathology

Dabir, D. V., Trojanowski, J. Q., Richter‐Landsberg, C., Lee, V. M. ‐., & Forman, M. S. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63106-9 · Cited by 120

Identification and characterization of the Drosophila tau homolog

Heidary, G., & Fortini, M. (2001) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00487-7 · Cited by 120

Thorn-shaped astrocytes: possibly secondarily induced tau-positive glial fibrillary tangles

Ikeda, K., Akiyama, H., Kondo, H., Haga, C., Tanno, E., Tokuda, T., & Ikeda, S. (1995) · Acta Neuropathologica · doi:10.1007/bf00318575 · Cited by 119

Effect of Pseudophosphorylation and Cross-linking by Lipid Peroxidation and Advanced Glycation End Product Precursors on Tau Aggregation and Filament Formation

Kuhla, B., Haase, C., Flach, K., Lüth, H.-J., Arendt, T., & Münch, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609521200 · Cited by 119

Glial Tau Pathology in Tauopathies: Functional Consequences

Kahlson, M. A., & Colodner, K. J. (2015) · Journal of Experimental Neuroscience · doi:10.4137/jen.s25515 · Cited by 119

Evaluating triggers and enhancers of tau fibrillization

Kuret, J., Congdon, E. E., Li, G., Yin, H., Yu, X., & Zhong, Q. (2005) · Microscopy Research and Technique · doi:10.1002/jemt.20187 · Cited by 119

Genetic Creutzfeldt-Jakob disease associated with the E200K mutation: characterization of a complex proteinopathy

Kovács, G. G., Seguin, J., Quadrio, I., Höftberger, R., Kapás, I., Streichenberger, N., Biacabé, A.-G., Meyronet, D., Sciot, R., Vandenberghe, R. R., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0713-y · Cited by 118

Familial presenile dementia with psychosis associated with cortical neurofibrillary tangles and degeneration of the amygdala

Sumi, S. M., Bird, T. D., Nochlin, D., & Raskind, M. A. (1992) · Neurology · doi:10.1212/wnl.42.1.120 · Cited by 118

A mutation affecting the sodium/proton exchanger, SLC9A6, causes mental retardation with tau deposition

Garbern, J. Y., Neumann, M., Trojanowski, J. Q., Lee, V. M. ‐., Feldman, G. L., Norris, J. W., Friez, M. J., Schwartz, C. E., Stevenson, R. E., & Sima, A. A. F. (2010) · Brain · doi:10.1093/brain/awq071 · Cited by 117

Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases

Sergeant, N., David, J.-P., Lefranc, D., Vermersch, P., Wattez, A., & Delacourte, A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00859-4 · Cited by 117

Corticonigral degeneration with neuronal achromasia and basal neurofibrillary tangles

Paulus, W., & Selim, M. (1990) · Acta Neuropathologica · doi:10.1007/bf00662643 · Cited by 117

Alzheimer's Disease: A Description of the Structural Lesions

Probst, A., Langui, D., & ULRICH, J. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00666.x · Cited by 117

Structural and Functional Implications of Tau Hyperphosphorylation: Information from Phosphorylation-Mimicking Mutated Tau Proteins

Eidenmüller, J., Fath, T., Hellwig, A., Reed, J., Sontag, E., & Brandt, R. (2000) · Biochemistry · doi:10.1021/bi001290z · Cited by 117

Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins

Kwon, Y., Huang, H.-B., Desdouits, F., Girault, J., Greengard, P., & Nairn, A. C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3536 · Cited by 117

Tau accumulation in astrocytes in progressive supranuclear palsy is a degenerative rather than a reactive process

Togo, T., & Dickson, D. W. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0569-x · Cited by 116

BAG-1 Associates with Hsc70·Tau Complex and Regulates the Proteasomal Degradation of Tau Protein

Elliott, E., Tsvetkov, P., & Ginzburg, I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706379200 · Cited by 116

Concurrent alterations of O‐GlcNAcylation and phosphorylation of tau in mouse brains during fasting

Li, X., Fen, L., Wang, J., & Gong, C. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04735.x · Cited by 116

Ultrastructural characteristics of tau filaments in tauopathies: Immuno‐electron microscopic demonstration of tau filaments in tauopathies

Arima, K. (2006) · Neuropathology · doi:10.1111/j.1440-1789.2006.00669.x · Cited by 115

Argyrophilic grain disease: widespread hyperphosphorylation of tau protein in limbic neurons

Tolnay, M., Spillantini, M. G., Goedert, M., ULRICH, J., Langui, D., & Probst, A. (1997) · Acta Neuropathologica · doi:10.1007/s004010050642 · Cited by 115

Familial amyotrophic lateral sclerosis and parkinsonism‐dementia complex of the Kii peninsula of Japan: Clinical and neuropathological study and tau analysis

Kuzuhara, S., Kokubo, Y., Sasaki, R., Narita, Y., Yabana, T., Hasegawa, M., & Iwatsubo, T. (2001) · Annals of Neurology · doi:10.1002/ana.100 · Cited by 115

Pathological overlap in cases of parkinsonism associated with neurofibrillary tangles

Geddes, J. F., Hughes, A. J., Lees, A. J., & Daniel, S. E. (1993) · Brain · doi:10.1093/brain/116.1.281 · Cited by 115

SnapShot: genetics of Alzheimer's disease.

Guerreiro, R., Bras, J., & Hardy, J. (2013) · Cell · doi:10.1016/j.cell.2013.10.037 · Cited by 114

Regional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementia

Holton, J. L., Ghiso, J., Lashley, T., Rostagno, A., Guerin, C. J., Gibb, G., Houlden, H., Ayling, H., Martinian, L., Anderton, B. H., et al. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63993-4 · Cited by 114

Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease

Luna‐Muñoz, J., García‐Sierra, F., Falcón, V., Menéndez, I., Chávez-Macías, L., & Mena, R. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8104 · Cited by 113

A new function of microtubule-associated protein tau: Involvement in chromosome stability

Rossi, G., Dalprà, L., Crosti, F., Lissoni, S., Sciacca, F. L., Catania, M., Mangieri, M., Giaccone, G., Croci, D., & Tagliavini, F. (2008) · Cell Cycle · doi:10.4161/cc.7.12.6012 · Cited by 113

Experimenting on the Past: The Enigma of von Economo's Encephalitis Lethargica

Reid, A. H., McCall, S. A., Henry, J. M., & Taubenberger, J. K. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.7.663 · Cited by 112

Site-specific Phosphorylation and Caspase Cleavage Differentially Impact Tau-Microtubule Interactions and Tau Aggregation

Ding, H., Matthews, T. A., & Johnson, G. V. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511697200 · Cited by 112

Essential role of tau phosphorylation in adult hippocampal neurogenesis

Hong, X., Peng, C., Wei, W., Tian, Q., Liu, Y., Yao, X., Zhang, Y., Cao, F., Wang, Q., & Wang, J. (2009) · Hippocampus · doi:10.1002/hipo.20712 · Cited by 112

The calmodulin‐binding protein in microtubules is tau factor

Sobue, K., Fujita, M., Muramoto, Y., & Kakiuchi, S. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80447-4 · Cited by 112

Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules

Aronov, S., Aranda, G., Behar, L., & Ginzburg, I. (2002) · Journal of Cell Science · doi:10.1242/jcs.00058 · Cited by 112

Tau and src family tyrosine kinases

Lee, G. S. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.002 · Cited by 111

MAP2c, but Not Tau, Binds and Bundles F-Actin via Its Microtubule Binding Domain

Roger, B., Al-Bassam, J., Dehmelt, L., Milligan, R. A., & Halpain, S. (2004) · Current Biology · doi:10.1016/j.cub.2004.01.058 · Cited by 110

Glycogen Synthase Kinase-3β Is Complexed with Tau Protein in Brain Microtubules

Sun, W., Qureshi, H. Y., Cafferty, P. W., Sobue, K., Agarwal-Mawal, A., Neufield, K. D., & Paudel, H. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107182200 · Cited by 110

Neurofibrillary degeneration and neuronal loss in alzheimer's disease

Bondareff, W., Mountjoy, C. Q., Roth, M., & Hauser, D. L. (1989) · Neurobiology of Aging · doi:10.1016/0197-4580(89)90007-9 · Cited by 109

Correlation Between Cortical θ Activity and Hippocampal Volumes in Health, Mild Cognitive Impairment, and Mild Dementia

Grunwald, M., Busse, F. P., Hensel, A., Kruggel, F., Riedel-Heller, S. G., Wolf, H., Arendt, T., & Gertz, H.-J. (2001) · Journal of Clinical Neurophysiology · doi:10.1097/00004691-200103000-00010 · Cited by 109

Prevalence, incidence and duration of Braak's stages in the general population: can we know?

Duyckaerts, C., & Hauw, J.-J. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00047-x · Cited by 109

Integrated phylogeny of the primate brain, with special reference to humans and their diseases

Rapoport, S. I. (1990) · Brain Research Reviews · doi:10.1016/0165-0173(90)90004-8 · Cited by 108

An immunohistochemical study of cases of sporadic and inherited frontotemporal lobar degeneration using 3R- and 4R-specific tau monoclonal antibodies

de Silva, R., Lashley, T., Strand, C., Shiarli, A.-M., Shi, J., Tian, J., Bailey, K. L., Davies, P., Bigio, E. H., Arima, K., et al. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0048-x · Cited by 108

Astrocytic inclusions in progressive supranuclear palsy and corticobasal degeneration

Yoshida, M. (2014) · Neuropathology · doi:10.1111/neup.12143 · Cited by 107

Immunoreactive Epidermal Growth Factor Receptors in Neuritic Plaques from Patients with Alzheimer's Disease

Birecree, E., Whetsell, W. O., Stoscheck, C. M., King, L. E., & Nanney, L. B. (1988) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198809000-00006 · Cited by 107

An in vitro perspective on the molecular mechanisms underlying mutant huntingtin protein toxicity

Cisbani, G., & Cicchetti, F. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.121 · Cited by 107

Structural correlates of mild cognitive impairment

Wolf, H., Hensel, A., Kruggel, F., Riedel-Heller, S. G., Arendt, T., Wahlund, L., & Gertz, H. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.006 · Cited by 107

LRRK2 phosphorylates novel tau epitopes and promotes tauopathy

Bailey, R. M., Covy, J. P., Melrose, H. L., Rousseau, L., Watkinson, R., Knight, J. A., Miles, S., Farrer, M. J., Dickson, D. W., Giasson, B. I., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1188-4 · Cited by 107

Tau Phosphorylated at Tyrosine 394 is Found in Alzheimer's Disease Tangles and can be a Product of the Abl-Related Kinase, Arg

Tremblay, M. A., Acker, C. M., & Davies, P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1271 · Cited by 106

Tau as a nucleolar protein in human nonneural cells in vitro and in vivo

Thurston, V. C., Zinkowski, R. P., & Binder, L. I. (1996) · Chromosoma · doi:10.1007/bf02510035 · Cited by 106

Pooled-DNA sequencing identifies novel causative variants in PSEN1, GRN and MAPT in a clinical early-onset and familial Alzheimer's disease Ibero-American cohort

Jin, S. C., Pástor, P., Cooper, B., Cervantes, S., Benítez, B. A., Razquín, C., Goate, A., Ibero-American Alzheimer Disease Genetics Group Researchers, & Cruchaga, C. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt137 · Cited by 106

Post-mortem Interval Effects on the Phosphorylation of Signaling Proteins

Li, J., Gould, T. D., Yuan, P., Manji, H. K., & Chen, G. (2002) · Neuropsychopharmacology · doi:10.1038/sj.npp.1300112 · Cited by 105

Phosphoproteome Profiling of Human Skin Fibroblast Cells in Response to Low- and High-Dose Irradiation

Yang, F., Stenoien, D. L., Strittmatter, E. F., Wang, J., Ding, L., Lipton, M. S. W., Monroe, M. E., Nicora, C., Gristenko, M. A., Tang, K., et al. (2006) · Journal of Proteome Research · doi:10.1021/pr060028v · Cited by 105

Phylogenetic diversity of the expression of the microtubule-associated protein tau: implications for neurodegenerative disorders

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Are Tangles as Toxic as They Look?

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