The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments
Open accessAbstract
The axonal microtubule-associated phosphoprotein tau interacts with neural plasma membrane (PM) components during neuronal development (Brandt, R., Léger, J., and Lee, G. (1995) J. Cell Biol. 131, 1327-1340). To analyze the mechanism and potential regulation of tau's PM association, a method was developed to isolate PM-associated tau using microsphere separation of surface-biotinylated cells. We show that tau's PM association requires an intact membrane cortex and that PM-associated tau and cytosolic tau are differentially phosphorylated at sites detected by several Alzheimer's disease (AD) diagnostic antibodies (Ser(199)/Ser(202), Thr(231), and Ser(396)/Ser(404)). In polar neurons, the association of endogenous tau phosphoisoforms with the membrane cortex correlates with an enrichment in the axonal compartment. To test for a direct effect of AD-specific tau modifications in determining tau's interactions, a phosphomutant that simulates an AD-like hyperphosphorylation of tau was produced by site-directed mutagenesis of Ser/Thr residues to negatively charged amino acids (Glu). These mutations completely abolish tau's association with the membrane cortex; however, the construct retains its capability to bind to microtubules. The data suggest that a loss of tau's association with the membrane cortex as a result of phosphorylation at sites that are modified during disease contributes to somatodendritic tau accumulation, axonal microtubule disintegration, and neuronal death characteristic for AD.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Prior to initiating the screen, the robustness of the protocol was examined using two well characterized tau kinases, CDK5 (13) and GSK3 𝛃 (18), as well as GFP, the negative control.”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [18]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Assay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Bialojan, C., & Takai, A. (1988) · Biochemical Journal · doi:10.1042/bj2560283 · Cited by 1,689
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588
Okadaic acid: a new probe for the study of cellular regulation
Cohen, P., Holmes, C. F. B., & Tsukitani, Y. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90192-e · Cited by 1,373
Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037
Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 1,011
A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification
Hopp, T. P., Prickett, K. S., Price, V. L., Libby, R. T., March, C. J., Cerretti, D. P., Urdal, D. L., & Conlon, P. J. (1988) · Nature Biotechnology · doi:10.1038/nbt1088-1204 · Cited by 959
Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.
Kilmartin, J. V., Wright, B., & Milstein, C. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.93.3.576 · Cited by 942
Flagged first, then by citations
Research works printed but not linked: 1
- Prickett, 1989, BioTechniques, 7, 580
Cited by
Sorted by citations
Items 101–200 of 225
Utton, M. A., Connell, J. W., Asuni, A. A., van Slegtenhorst, M., Hutton, M. L., de Silva, R., Lees, A. J., Miller, C. C. J., & Anderton, B. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06394.2002 · Cited by 66
Hahn, I., Voelzmann, A., Liew, Y.-T., Costa-Gomes, B., & Prokop, A. (2019) · Neural Development · doi:10.1186/s13064-019-0134-0 · Cited by 66
Impact of Tau on Neurovascular Pathology in Alzheimer's Disease
Canepa, E., & Fossati, S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.573324 · Cited by 67
Farah, C. A., Nguyen, M. D., Julien, J., & Leclerc, N. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01505.x · Cited by 64
Intracellular and Extracellular Roles for Tau in Neurodegenerative Disease
Hanger, D. P., Lau, D. H. W., Phillips, E. C., Bondulich, M. K., Guo, T., Woodward, B. W., Pooler, A. M., & Noble, W. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132054 · Cited by 66
Niewidok, B., Igaev, M., Sündermann, F., Janning, D., Bakota, L., & Brandt, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0402 · Cited by 62
Self-citationRole of the Lipid Membrane and Membrane Proteins in Tau Pathology
Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61
Rodríguez, L. C. D. L. C., Mohamed, N., Desjardins, A., Lippé, R., Fon, E. A., & Leclerc, N. M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13994 · Cited by 66
Croft, C. L., Wade, M. A., Kurbatskaya, K., Mastrandreas, P., Hughes, M. M., Phillips, E. C., Pooler, A. M., Perkinton, M. S., Hanger, D. P., & Noble, W. J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.97 · Cited by 62
Curcumin Labeling of Neuronal Fibrillar Tau Inclusions in Human Brain Samples
Mohorko, N., Repovš, G., Popović, M., Kovács, G. G., & Bresjanac, M. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181d709eb · Cited by 60
Roles of Cholesterol and Lipids in the Etiopathogenesis ofAlzheimer′s Disease
Rojo, L. E., Sjöberg-Herrera, M. K., Hernández, P., Zambrano, C. A., & Maccioni, R. B. (2006) · BioMed Research International · doi:10.1155/jbb/2006/73976 · Cited by 57
Sarnat, H. B., Flores‐Sarnat, L., Crino, P. B., Hader, W. J., & Bello‐Espinosa, L. E. (2012) · Folia Neuropathologica · doi:10.5114/fn.2012.32363 · Cited by 52
Florenzano, F., Corsetti, V., Ciasca, G., Ciotti, M. T., Pittaluga, A., Olivero, G., Feligioni, M., Iannuzzi, F., Latina, V., Sciacca, M. F. M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17371 · Cited by 54
Cytoskeletal mechanisms of neuronal degeneration
Brandt, R. (2001) · Cell and Tissue Research · doi:10.1007/s004410000334 · Cited by 52
Self-citationRahman, A., Khan, K. M., Al‐Khaledi, G., Khan, I., & Al-Shemary, T. E. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.02.014 · Cited by 49
Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 51
Smith, M. J., Crowther, R. A., & Goedert, M. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02169-4 · Cited by 49
Expression of Tau40 Induces Activation of Cultured Rat Microglial Cells
Wang, L., Jiang, Q., Chu, J., Lin, L., Li, X.-G., Chai, G.-S., Wang, Q., Wang, J.-Z., & Tian, Q. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076057 · Cited by 47
Sontag, J., Nunbhakdi‐Craig, V., & Sontag, E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490102 · Cited by 47
Platt, T. L., Reeves, V. L., & Murphy, M. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.017 · Cited by 48
Gauthier‐Kemper, A., Igaev, M., Sündermann, F., Janning, D., Brühmann, J., Moschner, K., Reyher, H.-J., Junge, W., Glebov, K., Walter, J., et al. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-12-0737 · Cited by 45
Self-citationPress‐Sandler, O., & Miller, Y. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.014 · Cited by 45
Is membrane homeostasis the missing link between inflammation and neurodegenerative diseases?
de Groot, N. S., & Torrent, M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2038-4 · Cited by 45
Visualizing the microtubule-associated protein tau in the nucleus
Lu, J. N., Li, T., He, R., Bartlett, P. F., & Götz, J. (2014) · Science China Life Sciences · doi:10.1007/s11427-014-4635-0 · Cited by 43
Hyperosmotic stress‐induced apoptosis and tau phosphorylation in human neuroblastoma cells
Stoothoff, W. H., & Johnson, G. V. W. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1187 · Cited by 43
Golovyashkina, N., Penazzi, L., Ballatore, C., Smith, A. B., Bakota, L., & Brandt, R. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0049-0 · Cited by 41
Self-citationNatale, G. D., Sabatino, G., Sciacca, M. F. M., Tosto, R., Milardi, D., & Pappalardo, G. (2022) · Molecules · doi:10.3390/molecules27165066 · Cited by 41
Mari, S. A., Wegmann, S., Tepper, K., Hyman, B. T., Mandelkow, E., Mandelkow�, E., & Müller, D. J. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b01085 · Cited by 39
Sahara, N., Murayama, M., Higuchi, M., Suhara, T., & Takashima, A. (2014) · Frontiers in Neurology · doi:10.3389/fneur.2014.00026 · Cited by 37
Beharry, C., Alaniz, M. E., & Alonso, A. D. C. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130617 · Cited by 39
HERNANDEZ, F. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.002 · Cited by 41
Is Tau Aggregation Toxic or Protective: A Sensible Question in the Absence of Sensitive Methods?
Götz, J., Ittner, L. M., Fändrich, M., & Schönrock, N. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14410 · Cited by 37
Homchaudhuri, L., Polverini, E., Gao, W., Harauz, G., & Boggs, J. M. (2009) · Biochemistry · doi:10.1021/bi8022587 · Cited by 36
Interaction of Tau with Fe65 links tau to APP
Barbato, C., Canu, N., Zambrano, N., Serafino, A., Minopoli, G., Ciotti, M. T., Amadoro, G., Russo, T., & Calissano, P. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.10.011 · Cited by 36
Xu, M., Dong, Y., Wan, S., Yan, T., Cao, J., Wu, L., Bi, K., & Jia, Y. (2016) · Physiology & Behavior · doi:10.1016/j.physbeh.2016.09.018 · Cited by 36
Tau phosphorylation during apoptosis of human SH-SY5Y neuroblastoma cells
Mookherjee, P., & Johnson, G. V. W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)03074-8 · Cited by 36
Zhong, L., Liu, H., Zhang, W., Liu, X., Jiang, B., Fei, H., & Sun, Z. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6860 · Cited by 34
How it all Started: Tau and Protein Phosphatase 2A
Liu, C., & Götz, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130503 · Cited by 38
Inhibition of PMCA activity by tau as a function of aging and Alzheimer's neuropathology
Berrocal, M., Corbacho‐Cuello, I., Vázquez-Hernández, M., Ávila, J., Sepúlveda, M. R., & Mata, A. M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.007 · Cited by 34
Pharmacological Modulators of Tau Aggregation and Spreading
Dominguez‐Meijide, A., Vasili, E., & Outeiro, T. F. (2020) · Brain Sciences · doi:10.3390/brainsci10110858 · Cited by 36
Piontek, J., & Brandt, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306749200 · Cited by 33
Self-citationBakota, L., Ussif, A. M., Jeserich, G., & Brandt, R. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.003 · Cited by 33
Self-citationAdministration of the benzodiazepine midazolam increases tau phosphorylation in the mouse brain
Whittington, R. A., Virág, L., Gratuze, M., Lewkowitz-Shpuntoff, H. M., Cheheltanan, M., Petry, F. R., Poitras, I., Morin, F., & Planel, E. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.027 · Cited by 32
Connecting the dots: Neuronal senescence, stress granules, and neurodegeneration
Ma, Y., & Farny, N. G. (2023) · Gene · doi:10.1016/j.gene.2023.147437 · Cited by 30
Lénárt, N., Szegedi, V., Juhász, G., Kasztner, A., Horváth, J., Bereczki, E., Tóth, M. E., Penke, B., & Sántha, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046007 · Cited by 27
The Power and Richness of Modelling Tauopathies in Drosophila
Papanikolopoulou, K., & Skoulakis, E. M. C. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8193-1 · Cited by 29
Tau and HMW tau phosphorylation and compartmentalization in apoptotic neuronal PC12 cells
Shelton, S. B., & Johnson, G. V. W. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1212 · Cited by 27
Altered phosphorylation but no neurodegeneration in a mouse model of tau hyperphosphorylation
Hundelt, M., Fath, T., Selle, K., Oesterwind, K., Jordan, J., Schultz, C., Götz, J., von Engelhardt, J., Monyer, H., Lewejohann, L., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.06.007 · Cited by 28
Self-citationMaintenance of Synaptic Stability Requires Calcium-Independent Phospholipase A2Activity
Allyson, J., Bi, X., Baudry, M., & Massicotte, G. (2012) · Neural Plasticity · doi:10.1155/2012/569149 · Cited by 25
Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tau knockin mice
Gilley, J., Ando, K., Seereeram, A., Rodríguez-Martín, T., Pooler, A. M., Sturdee, L., Anderton, B. H., Brion, J., Hanger, D. P., & Coleman, M. P. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.11.028 · Cited by 26
Changes in tau phosphorylation in hibernating rodents
León‐Espinosa, G., García, E., García‐Escudero, V., Hernández, F., DeFelipe, J., & Ávila, J. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23220 · Cited by 24
Yeast as a Model for Alzheimer’s Disease: Latest Studies and Advanced Strategies
Verduyckt, M., Vignaud, H., Bynens, T., den Brande, J. V., Franssens, V., Cullin, C., & Winderickx, J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2627-5_11 · Cited by 24
Chen, N.-Y., Liu, C., Wei, L., Ding, Y., Bian, Z., Huang, L., Huang, H., Yu, K., Chen, S., Sun, Y., et al. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/4757520 · Cited by 24
Mitochondrial defects: An emerging theranostic avenue towards Alzheimer's associated dysregulations
Mani, S., Swargiary, G., Singh, M., Agarwal, S., Dey, A., Ojha, S. K., & Jha, N. K. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119985 · Cited by 24
Tau Protein as Therapeutic Target for Cancer? Focus on Glioblastoma
Hedna, R., Kovacic, H., Pagano, A., Peyrot, V., Robin, M., Devred, F., & Breuzard, G. (2022) · Cancers · doi:10.3390/cancers14215386 · Cited by 25
New insights into clinical trial for colostrinin™ in Alzheimer's disease
Szaniszlo, P., Germán, P., Hajas, G., Saenz, D. N., Kruzel, M. L., & Boldogh, I. R. (2009) · The journal of nutrition health & aging · doi:10.1007/s12603-009-0065-2 · Cited by 23
Blockade of NR2A-Containing NMDA Receptors Induces Tau Phosphorylation in Rat Hippocampal Slices
Allyson, J., Dontigny, E., Auberson, Y. P., Cyr, M., & Massicotte, G. (2010) · Neural Plasticity · doi:10.1155/2010/340168 · Cited by 21
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
The Co-chaperone BAG2 Mediates Cold-Induced Accumulation of Phosphorylated Tau in SH-SY5Y Cells
de Paula, C. A. D., Santiago, F. E., Oliveira, A. S., Oliveira, F. A., Almeida, M. C., & Carrettiero, D. C. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0239-x · Cited by 21
Hanger, D. P., Goniotaki, D., & Noble, W. J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_9 · Cited by 23
Spears, W. E., Furgerson, M., Sweetnam, J. M. C., Evans, P. T., Gearing, M., Fechheimer, M., & Furukawa, R. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-74 · Cited by 19
Recent advances in experimental modeling of the assembly of tau filaments
Ko, L., Deture, M. A., Sahara, N., Chihab, R., Vega, I. E., & Yen, S.-H. C. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.004 · Cited by 19
Piontek, J., Régnier‐Vigouroux, A., & Brandt, R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10094 · Cited by 18
Self-citationInteraction of Tau construct K18 with model lipid membranes
Azouz, M., Feuillie, C., Lafleur, M., Molinari, M., & Lecomte, S. (2021) · Nanoscale Advances · doi:10.1039/d1na00055a · Cited by 16
Ke, Y. D., Chan, G., Stefanoska, K., Au, C. G., Bi, M., Müller, J., Przybyla, M., Feiten, A., Prikas, E., Halliday, G. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005263 · Cited by 16
Microtubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?
Soliman, A., Bakota, L., & Brandt, R. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211201101020 · Cited by 19
Self-citationTau–Mitochondria Interactions in Neurodegeneration: Mechanisms and Therapeutic Potential
Castillo-Casaña, Y., Arias, C., & Coria, R. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01634-1 · Cited by 20
Tau Protein Alterations Induced by Hypobaric Hypoxia Exposure
Pena, E., Martin-Salamanca, R. S., Alam, S. E., Flores, K., & Arriaza, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020889 · Cited by 16
Recent advances in the development of immunotherapies for tauopathies
Ubhi, K. K., & Masliah, E. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.10.007 · Cited by 16
The Role ofα-Synuclein and LRRK2 in Tau Phosphorylation
Kawakami, F., & Ichikawa, T. (2015) · Parkinson s Disease · doi:10.1155/2015/734746 · Cited by 15
Rández‐Gil, F., Bojunga, L., Estruch, F., Winderickx, J., Poeta, M. D., & Prieto, J. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.592159 · Cited by 14
Modeling tauopathy: a range of complementary approaches
Hall, G. F., & Yao, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.002 · Cited by 14
Monitoring Cytoskeletal Dynamics in Living Neurons Using Fluorescence Photoactivation
Gauthier‐Kemper, A., Weissmann, C., Reyher, H.-J., & Brandt, R. (2012) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-388448-0.00009-7 · Cited by 13
Self-citationKitamura, C., Shirai, K., Inoue, M., & Tashiro, T. (2006) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-006-9117-x · Cited by 13
Ruan, Y., Zhai, W., Shi, X., Zhang, L., & Hu, Y. (2016) · Metabolic Brain Disease · doi:10.1007/s11011-016-9857-3 · Cited by 13
Beyond microtubule regulation: the multifaceted roles of tau in neuronal function and dysfunction
Bakota, L., Tulva, K., Trushina, N. I., & Brandt, R. (2026) · Translational Psychiatry · doi:10.1038/s41398-026-03947-1 · Cited by 12
Self-citationMicrotubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?
Soliman, A., Bakota, L., & Brandt, R. (2022) · UCL Discovery (University College London) · Cited by 12
Self-citationZhang, Z., Zhao, R., Tang, Y., Wen, S., Wang, D., & Qi, J. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0405-6 · Cited by 11
RetractedMethylation at a conserved lysine residue modulates tau assembly and cellular functions
Shams, H., Matsunaga, A., Ma, Q., Mofrad, M. R. K., & Didonna, A. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103707 · Cited by 10
Effects of Colostrinin™ on gene expression-transcriptomal network analysis
Szaniszlo, P., Germán, P., Hajas, G., Saenz, D. N., Woodberry, M. W., Kruzel, M. L., & Boldogh, I. R. (2008) · International Immunopharmacology · doi:10.1016/j.intimp.2008.10.022 · Cited by 10
Amyloids on Membrane Interfaces: Implications for Neurodegeneration
Mahakud, A. K., Shaikh, J., Iqbal, V. V. R., Gupta, A., Tiwari, A., & Saleem, M. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00245-x · Cited by 8
Kammula, S. V., Tripathi, S., Wang, N., Dawson, V. L., Dawson, T. M., & Mao, X. (2023) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2023.20 · Cited by 9
Vos, A. D., Bynens, T., Rosseels, J., Coun, C., Ring, J., Madeo, F., Galas, M., Winderickx, J., & Franssens, V. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.2.144 · Cited by 10
Zhang, Z., Zhao, R., Tang, Y., Wen, S., Wang, D., & Qi, J. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0721-5 · Cited by 9
RetractedAndrés‐Benito, P., Íñigo-Marco, I., Brullas, M., Carmona, M., del Rı́o, J. A., Fernández‐Irigoyen, J., Santamaría, E., Povedano, M., & Ferrer, I. (2023) · Aging · doi:10.18632/aging.204698 · Cited by 8
Regulation of Neurodegeneration-associated Protein Fragments by the N-degron Pathways
Eldeeb, M. A., Ragheb, M. A., Soliman, M. H., & Fahlman, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-021-00396-0 · Cited by 9
Villemagne, V. L., Okamura, N., & Rowe, C. C. (2016) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2016.05.001 · Cited by 7
The mitotic tensegrity guardian tau protects mammary epithelia from katanin-like1-induced aneuploidy
Sudo, H., & Nakajima, K. (2016) · Oncotarget · doi:10.18632/oncotarget.10728 · Cited by 6
Alpaugh, M., Lantero‐Rodriguez, J., Benedet, A. L., Manseau, U., Boutin, M., Maiuri, M., Denis, H. L., Masnata, M., Fazal, S. V., Chouinard, S., et al. (2025) · Journal of Neurology · doi:10.1007/s00415-025-12966-9 · Cited by 7
Role of Tau Protein Hyperphosphorylation in Diabetic Retinal Neurodegeneration
Mu, J., Zhang, Z., Jiang, C., Geng, H., & Duan, J. (2025) · Journal of Ophthalmology · doi:10.1155/joph/3278794 · Cited by 5
[Phosphorylation of tau and Alzheimer's disease].
García, T., & Jay, D. (2004) · PubMed · Cited by 4
Regulation of Microtubule: Current Concepts and Relevance to Neurodegenerative Diseases
Ghosh, A., & Singh, S. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666210728144043 · Cited by 6
Disentangling the role of tau pathology in autism spectrum disorders
Villavicencio-Tejo, F., Olesen, M. A., Moya, M. L., & Quintanilla, R. A. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111496 · Cited by 4
Tau Phosphorylation in Myotilinopathies and Desminopathies~!2010-01-09~!2010-02-04~!2010-03-18~!
Janué, A., Olivé, M., & Ferrer, I. (2010) · The Open Pathology Journal · doi:10.2174/1874375701004010001 · Cited by 3
Cytoskeletal mechanisms of neuronal morphogenesis
Brandt, R. (2001) · Zoology · doi:10.1078/0944-2006-00027 · Cited by 3
Self-citationKöhler, C. N., Fuhr, V., & Dinekov, M. (2017) · Brain Research · doi:10.1016/j.brainres.2017.08.029 · Cited by 2
Padilla-Zambrano, H., García-Ballestas, E., Quiñones-Ossa, G. A., Sibaja-Perez, A. E., Agrawal, A., Moscote‐Salazar, L. R., & Menéndez‐González, M. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666201204164220 · Cited by 2
Tau Protein: Targets And Development Against Alzheimer’s Disease
Dubey, S., & Mahesh, A. R. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815136142123010010 · Cited by 1
Lanning, J. D., & Meredith, S. C. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_14 · Cited by 1
Traits and Trammels of Tau Tracer Imaging
Villemagne, V. L., Lopresti, B. J., Doré, V., Minhas, D. S., Gogola, A., Nadkarni, N. K., Mason, N. S., Bourgeat, P., López, O. L., Ikonomović, M. D., et al. (2023) · Springer eBooks · doi:10.1007/978-3-031-35098-6_6 · Cited by 1
Metadata
- Authors
- Maas, T., Eidenmüller, J., & Brandt, R.
- Affiliations
- Heidelberg University (DE)
- Corresponding author
- Brandt, Roland
- ORCID
- Brandt, Roland
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 21
- Pages
- 15733-15740
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2061655823
- Cited by
- 226
- References
- 50
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 6 · 2022: 9 · 2021: 9 · 2020: 9 · 2019: 10 · 2018: 10 · 2017: 14 · 2016: 7 · 2015: 17 · 2014: 18 · 2013: 11 · 2012: 14
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 31 7)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau phosphorylation, paired helical filaments, Alzheimer's disease, plasma membrane association, axonal microtubules, tau hyperphosphorylation, neuronal cell death
- MeSH terms
- Actins, Alzheimer Disease, Animals, Cell Membrane, Cytosol, Immunohistochemistry, Microscopy, Electron, Microspheres, Microtubules, Neurons, Phosphorylation, Protein Binding, Transfection, Mutagenesis, Site-Directed, PC12 Cells, tau Proteins, Microscopy, Confocal, Okadaic Acid, Biotinylation, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review