The microtubule binding domain of tau protein

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

DNA sequencing with chain-terminating inhibitors

Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572

A new method for sequencing DNA.

Maxam, A. M., & Gilbert, W. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.2.560 · Cited by 7,929

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

Ultrasensitive Stain for Proteins in Polyacrylamide Gels Shows Regional Variation in Cerebrospinal Fluid Proteins

Merril, C. R., Goldman, D. A., Sedman, S. A., & Ebert, M. H. (1981) · Science · doi:10.1126/science.6162199 · Cited by 2,933

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

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

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

A rapid single-stranded cloning strategy for producing a sequential series of overlapping clones for use in DNA sequencing: Application to sequencing the corn mitochondrial 18 S rDNA

Dale, R. M. K., McClure, B., & Houchins, J. P. (1985) · Plasmid · doi:10.1016/0147-619x(85)90053-8 · Cited by 1,043

Disordered proteins in dementia

Ingelsson, M., & Hyman, B. T. (2002) · Annals of Medicine · doi:10.1080/078538902320322529 · Cited by 20

DeveIopmentalIy ReguIated Alternative SpIicing of mRNAs encoding N‐Terminal Tau Variants in the Rat Hippocampus: Structural and Functional Implications

Collet, J., Ferhat, L., Pollard, H., de Pouplana, L. R., Charton, G., Bernard, A., Moreau, J., Ben‐Ari, Y., & Khrestchatisky, M. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01701.x · Cited by 19

Differential compartmental processing and phosphorylation of pathogenic human tau and native mouse tau in the line 66 model of frontotemporal dementia

Lemke, N., Melis, V., Lauer, D., Magbagbeolu, M., Neumann, B., Harrington, C. R., Riedel, G., Wischik, C. M., Theuring, F., & Schwab, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014890 · Cited by 15

Probing modifications of the neuronal cytoskeleton

Doering, L. C. (1993) · Molecular Neurobiology · doi:10.1007/bf02769179 · Cited by 18

Tau isoform–specific stabilization of intermediate states during microtubule assembly and disassembly

Best, R. L., LaPointe, N. E., Liang, J., Ruan, K., Shade, M. F., Wilson, L., & Feinstein, S. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009124 · Cited by 20

Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin‐binding repeats of the τ protein reveal structural features of paired helical filament assembly

Hoffmann, R., Dawson, N. F., Wade, J. D., & Ötvös, L. (1997) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1997.tb01178.x · Cited by 17

Interaction 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

Phosphorylation Pattern of tau Associated with Distinct Changes of the Growth Cone Cytoskeleton

Šimić, G., Diana, A., & Hof, P. R. (2003) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-55557-2_2 · Cited by 17

The effect of multivalent cations and Tau on paclitaxel-stabilized microtubule assembly, disassembly, and structure

Safinya, C. R., Chung, P. J., Song, C., Li, Y., Ewert, K. K., & Choi, M. C. (2015) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2015.11.002 · Cited by 16

Solution structure of the microtubule‐targeting COS domain of MID1

Wright, K. M., Du, H., Dagnachew, M., & Massiah, M. A. (2016) · FEBS Journal · doi:10.1111/febs.13795 · Cited by 16

Optimization of in vitro conditions to study the arachidonic acid induction of 4R isoforms of the microtubule-associated protein tau

Mutreja, Y., & Gamblin, T. C. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.007 · Cited by 17

Discovery of Compounds That Will Prevent Tau Pathology

Kosik, K. S., Ahn, J. S., Stein, R. L., & Yeh, L.-A. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:261 · Cited by 16

Atypical role of proximal caspase-8 in truncated Tau-induced neurite regression and neuronal cell death.

Chung, C., Hong, Y.-M., Song, S.-M., Woo, H.-N., Choi, Y.-H., Rohn, T., & Jung, Y.-K. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.08.017 · Cited by 18

The Genetics of Frontotemporal Dementia

Haugarvoll, K., Wszołek, Z. K., & Hutton, M. L. (2007) · Neurologic Clinics · doi:10.1016/j.ncl.2007.03.002 · Cited by 16

Carboxyl terminal sequences of ?-tubulin involved in the interaction of HMW-MAPs. Studies using site-specific antibodies

Cross, D. C., Far�as, G. A., Dom�nguez, J., Ávila, J., & Maccioni, R. B. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf00925677 · Cited by 16

A conserved microtubule-binding region in Xanthomonas XopL is indispensable for induced plant cell death reactions

Ortmann, S., Marx, J., Lampe, C., Handrick, V., Ehnert, T.-M., Zinecker, S., Reimers, M., Bonas, U., & Erickson, J. L. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011263 · Cited by 15

Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles

Kohl, P. A., Song, C., Fletcher, B. J., Best, R. L., Tchounwou, C. K., Arceo, X. G., Chung, P. J., Miller, H. P., Wilson, L., Choi, M. C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46438-x · 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

Identification of Parkinson’s disease candidate genes using CAESAR and screening of MAPT and SNCAIP in South African Parkinson’s disease patients

Keyser, R. J., Oppon, E., Carr, J. A., & Bardien, S. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0591-z · Cited by 15

Microtubule-Tau Interaction as a Therapeutic Target for Alzheimer’s Disease

Ivashko‐Pachima, Y., Zhou, L.-Y., Lei, P., & Gozes, I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0715-x · Cited by 15

Neurofibrillary tangles mediated human neuronal tauopathies: insights from fly models

Sarkar, S. (2018) · Journal of Genetics · doi:10.1007/s12041-018-0962-4 · Cited by 15

Tau-Like Proteins in the Nervous System of Goldfish

Liu, Y., Xia, J., Ma, D., Faber, D. S., & Fischer, I. (1997) · Neurochemical Research · doi:10.1023/a:1021914830872 · Cited by 14

Relationship between microtubule-binding repeats and morphology of neurofibrillary tangle in Alzheimer's disease

Kitamura, T., Sugimori, K., Sudo, S., & Kobayashi, K. (2005) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2005.00488.x · Cited by 14

Implications of the sequence similarities between tau and myelin basic protein

Karthigasan, J., Inouye, H., & Kirschner, D. A. (1995) · Medical Hypotheses · doi:10.1016/0306-9877(95)90111-6 · 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

Development of an Assay to Screen for Inhibitors of Tau Phosphorylation by Cdk5

Ahn, J. S., Musacchio, A., Mapelli, M., Ni, J., Scinto, L. F. M., Stein, R. L., Kosik, K. S., & Yeh, L.-A. (2004) · SLAS DISCOVERY · doi:10.1177/1087057103260594 · Cited by 13

Alzheimer’s Disease and Alzheimer’s Disease-Related Dementias in African Americans: Focus on Caregivers

Kopel, J. J., Sehar, U., Choudhury, M., & Reddy, P. H. (2023) · Healthcare · doi:10.3390/healthcare11060868 · Cited by 15

The murine coronavirus as a model of trafficking and assembly of viral proteins in neural tissue

Kalicharran, K., & Dales, S. (1996) · Trends in Microbiology · doi:10.1016/0966-842x(96)10045-7 · Cited by 13

Review: Recent progress in frontotemporal lobar degeneration

Pickering-Brown, S. M. (2009) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2009.01045.x · Cited by 13

A Novel mRNA Binding Protein Complex Promotes Localized Plasminogen Activator Inhibitor-1 Accumulation at the Myoendothelial Junction

Heberlein, K. R., Han, J., Straub, A. C., Best, A. K., Kaun, C., Wojta, J., & Isakson, B. E. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.246371 · Cited by 13

Molecular neuropathology of Alzheimer's disease:In situ hybridization studies

Goedert, M., & Spillantini, M. G. (1990) · Cellular and Molecular Neurobiology · doi:10.1007/bf00733642 · Cited by 13

Changes in cytoskeletal organization in polyoma middle T antigen-transformed fibroblasts: Involvement of protein phosphatase 2A andsrc tyrosine kinases

da Costa, S. R., Wang, Y., Vilalta, P. M., Schönthal, A. H., & Hamm‐Alvarez, S. F. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/1097-0169(200012)47:4 · Cited by 11

Neurofibrillary Tangles, Dystrophic IMeurites (Curly Fibers), and Abnormal Phosphorylation of Tau

Mori, H., & Ihara, Y. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00670.x · 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

Oligodendrocyte Dysfunction in Tauopathy: A Less Explored Area in Tau-Mediated Neurodegeneration

Majumder, M., & Dutta, D. (2024) · Cells · doi:10.3390/cells13131112 · Cited by 14

Unknown roles of tau pathology in neurological disorders. Challenges and new perspectives

Olesen, M. A., Villavicencio-Tejo, F., Cuevas-Espinoza, V., & Quintanilla, R. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102594 · Cited by 12

Tau Proteins Harboring Neurodegeneration-Linked Mutations Impair Kinesin Translocation in vitro

Yu, D., LaPointe, N. E., Guzman, E., Pessino, V., Wilson, L., Feinstein, S. C., & Valentine, M. T. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131274 · Cited by 12

The role of the cellular prion protein in the uptake and toxic signaling of pathological neurodegenerative aggregates

Scialò, C., & Legname, G. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.008 · Cited by 12

N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding

Makwana, K. M., Sarnowski, M. P., Miao, J., Lin, Y., & Valle, J. R. D. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00528 · Cited by 12

C-H ... interplay between Ile308 and Tyr310 residues in the third repeat of microtubule binding domain is indispensable for self-assembly of three- and four-repeat tau

Sogawa, K., Okuda, R., In, Y., Ishida, T., Taniguchi, T., Minoura, K., & Tomoo, K. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs061 · Cited by 13

Assembly and bundling of marginal band microtubule protein: Role of tau

Sánchez, I., & Cohen, W. (1994) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970290106 · Cited by 12

Use of a heat-stable microtubule-associated protein class-specific antibody to investigate the mechanism of microtubule binding.

Dingus, J., Obar, R. A., Hyams, J. S., Goedert, M., & Vallee, R. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55142-5 · Cited by 12

Differentiating Progressive Supranuclear Palsy and Corticobasal Syndrome: Insights from Cerebrospinal Fluid Biomarkers—A Narrative Review

Giannakis, A., Konitsiotis, S., & Sioka, C. (2025) · Medicina · doi:10.3390/medicina61040701 · Cited by 12

Age-related Changes in Tau Expression in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis

Barańczyk‐Kuźma, A., Usarek, E., Kuźma‐Kozakiewicz, M., Kaźmierczak, B., Gajewska, B., Schwalenstöcker, B., & Ludolph, A. C. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9242-4 · Cited by 11

Les aspects génétiques de la maladie d’Alzheimer (Revue)

Kadmiri, N. E., Hamzi, K., Moutawakil, B. E., Slassi, I., & Nadifi, S. (2013) · Pathologie Biologie · doi:10.1016/j.patbio.2013.04.001 · Cited by 20

A 26–30 kDa developmentally‐regulated tauisoform localized within nuclei of mitotic humanneuroblastoma cells

Shea, T. B., & Cressman, C. M. (1998) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(97)00044-0 · Cited by 11

Alzheimer's disease: Recent advances in molecular pathology and genetics

McLoughlin, D. M., & Lovestone, S. (1994) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.930090602 · Cited by 11

Tau Lysine Pseudomethylation Regulates Microtubule Binding and Enhances Prion-like Tau Aggregation

Xia, Y., Bell, B. M., & Giasson, B. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098286 · Cited by 11

Re-Arranging the Puzzle between the Amyloid-Beta and Tau Pathology: An APP-Centric Approach

Haut, F., Argyrousi, E. K., & Arancio, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010259 · Cited by 11

Role of Oxygen Radicals in Alzheimer’s Disease: Focus on Tau Protein

Atlante, A., Valenti, D., Latina, V., & Amadoro, G. (2021) · Oxygen · doi:10.3390/oxygen1020010 · Cited by 11

Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein

Alhadidy, M. M., & Kanaan, N. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230596 · Cited by 10

Mice with Mutation in Dynein Heavy Chain 1 Do Not Share the Same Tau Expression Pattern with Mice with SOD1-Related Motor Neuron Disease

Kuźma‐Kozakiewicz, M., Usarek, E., Ludolph, A. C., & Barańczyk‐Kuźma, A. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0436-z · Cited by 9

Structure of puromycin-sensitive aminopeptidase and polyglutamine binding

Madabushi, S., Chow, K. M., Song, E. S., Goswami, A., Hersh, L. B., & Rodgers, D. W. (2023) · PLOS ONE · doi:10.1371/journal.pone.0287086 · Cited by 9

Pathogenic MAPT mutations Q336H and Q336R have isoform‐dependent differences in aggregation propensity and microtubule dysfunction

Xia, Y., Nasif, L. H., & Giasson, B. I. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15358 · Cited by 9

Clinical and Molecular Aspects of Frontotemporal Dementia

Froelich-Fabre, S., Skoglund, L., Ostojic, J., Kilander, L., Lindau, M. P., Glaser, A., Basun, H., & Lannfelt, L. (2004) · Neurodegenerative Diseases · doi:10.1159/000080989 · Cited by 9

The 77-kDa Echinoderm Microtubule-Associated Protein (EMAP) Shares Epitopes with the Mammalian Brain MAPs, MAP-2 and Tau

Li, Q., Callaghan, M., & Suprenant, K. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9271 · Cited by 9

Developmental regulation and PKC dependence of Alzheimer's-type tau phosphorylations in cultured fetal rat hippocampal neurons

Combs, C. K., Coleman, P. D., & O’Banion, M. K. (1998) · Developmental Brain Research · doi:10.1016/s0165-3806(98)00019-4 · Cited by 9

Chemically synthesized 182–235 segment of tau protein and analogue peptides are efficient in vitro microtubule assembly inducers of low apparent sequence specificity

Novella, I. S., Andreu, J. M., & Andreu, D. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81110-8 · Cited by 9

Transcriptional programs mediating neuronal toxicity and altered glial–neuronal signaling in a Drosophila knock-in tauopathy modelPreprint

Bukhari, H., Nithianandam, V., Battaglia, R. A., Cicalo, A., Sarkar, S., Comjean, A., Hu, Y., Leventhal, M. J., Dong, X., & Feany, M. Β. (2024) · Genome Research · doi:10.1101/gr.278576.123 · Cited by 11

Cellular model of Alzheimer's disease — Relevance to therapeutic testing

Marwarha, G., & Ghribi, O. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.11.011 · Cited by 8

The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease

Bhaskar, K., & Lamb, B. T. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_5 · Cited by 8

Tau-based therapies for Alzheimer’s disease: Promising novel neuroprotective approaches

Sayas, C. L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814037-6.00005-7 · Cited by 9

Cytoskeleton in abiotic stress signaling

Quezada-Rodríguez, E. H., Arthikala, M., & Nanjareddy, K. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90568-8.00016-x · Cited by 8

Tau Isoforms Expression in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis

Usarek, E., Kuźma‐Kozakiewicz, M., Schwalenstöcker, B., Kaźmierczak, B., Münch, C., Ludolph, A. C., & Barańczyk‐Kuźma, A. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9057-3 · Cited by 8

Secondary structures transition of tau protein with intrinsically disordered proteins specific force field

Dan, A., & Chen, H. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13407 · Cited by 8

Localization of tau and other proteins of isolated marginal bands

Sánchez, I., & Cohen, W. (1994) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970270407 · Cited by 8

Tau Phosphorylation

Buée, L., & Delacourte, A. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50023-8 · Cited by 8

Structural and functional implications of SLC13A3 and SLC9A6 mutations: an in silico approach to understanding intellectual disability

Hussain, S. I., Muhammad, N., Shah, S. U. D., Fardous, F., Khan, S. A., Khan, N., Rehman, A. U., Siddique, M., Wasan, S. A., Niaz, R., et al. (2023) · BMC Neurology · doi:10.1186/s12883-023-03397-y · Cited by 7

Unravelling the Proteinopathic Engagement of α-Synuclein, Tau, and Amyloid Beta in Parkinson’s Disease: Mitochondrial Collapse as a Pivotal Driver of Neurodegeneration

Sahoo, T. A., Chand, J., Kandy, A. T., Shanish Antony, A., & Subramanian, G. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04399-7 · Cited by 9

Development of a Cellular Tau Enzyme-Linked Immunosorbent Assay Method for Screening GSK-3β Inhibitors

Cho, G., Noh, M., Kang, B. Y., Ku, I.-W., Park, J., Hong, Y., Kim, M., & Kim, S. H. (2011) · Assay and Drug Development Technologies · doi:10.1089/adt.2010.0343 · Cited by 7

Selective dimerization of cysteines in glycopeptides and phosphopeptides

Hoffmann, R., & Ötvös, L. (1997) · Letters in Peptide Science · doi:10.1007/bf00127968 · Cited by 7

Minireview - Microtubules and Tubulin Oligomers: Shape Transitions and Assembly by Intrinsically Disordered Protein Tau and Cationic Biomolecules

Safinya, C. R., Chung, P. J., Song, C., Li, Y., Miller, H. P., Choi, M. C., Raviv, U., Ewert, K. K., Wilson, L., & Feinstein, S. C. (2019) · Langmuir · doi:10.1021/acs.langmuir.9b02208 · Cited by 7

Molecular dynamics simulations reveal the disruption mechanism of a 2,4‐thiazolidinedione derivative C30 against tau hexapeptide ( PHF6 ) oligomer

Liu, H., Zhong, H., Liu, H., & Yao, X. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26196 · Cited by 7

Alternative Splicing of Amino-Terminal Tau mRNA in Rat Spinal Cord during Development and Following Axonal Injury

Halverson, R. A., Chambers, C. B., & Muma, N. A. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7637 · Cited by 7

Functional domains on chemically modified tau protein

Far�as, G. A., Vial, C., & Maccioni, R. B. (1993) · Cellular and Molecular Neurobiology · doi:10.1007/bf00735373 · Cited by 7

The Biology and Pathobiology of Tau Protein

Hall, G. F. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_15 · Cited by 6

An emerging role for the gut microbiome in tauopathy

Zhu, Y., Self, W. K., & Holtzman, D. M. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00423 · Cited by 6

Insight into Atomic Resolution of the Cross‐Seeding between Tau/Mutated Tau and Amyloid‐β in Neurodegenerative Diseases

Atsmon‐Raz, Y., & Miller, Y. (2015) · Israel Journal of Chemistry · doi:10.1002/ijch.201400162 · Cited by 6

Traveling the tau pathway: A personal account

Kosik, K. S. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s327 · Cited by 6

The Role of Glycogen Synthase Kinase-3 (GSK-3) in Alzheimer’s Disease

Medina, M., & Avil, J. (2011) · InTech eBooks · doi:10.5772/16879 · Cited by 7

Missense and Splice Site Mutations in Tau Associated with FTDP-17 Multiple Pathogenic Mechanisms

Hutton, M. L., Lovestone, S., Heutink, P., Pickering-Brown, S. M., & Yen, S. H. (2000) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-662-04056-0_4 · Cited by 6

Introduction to the Tauopathies

Goedert, M. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch13 · Cited by 6

Synthesis and preclinical evaluation of diarylamine derivative as Tau-PET radiotracer for Alzheimer's Disease

Liu, T., Ren, C., Guo, W., Zhang, X., Li, Y., Wang, Y., Zhang, Q., Chen, B., Dai, J., Yan, X., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117046 · Cited by 6

Implications of Mucin-Type O-Glycosylation in Alzheimer’s Disease

Navarro, N. V., Mundim, G. D. N., & Čudić, M. (2025) · Molecules · doi:10.3390/molecules30091895 · Cited by 5

MAPT Mutations V337M and N297K Alter Organelle Trafficking in Frontotemporal Dementia Patient-Specific Motor Neurons

Hartmann, C., Anskat, M., Ehrlich, M., Sterneckert, J. L., Pal, A., & Hermann, A. (2024) · Biomedicines · doi:10.3390/biomedicines12030641 · Cited by 5

Development of a Fluorescent High Throughput Assay for Tau Aggregation

Liu, M., Ni, J., Kosik, K. S., & Yeh, L.-A. (2004) · Assay and Drug Development Technologies · doi:10.1089/adt.2004.2.609 · Cited by 5

The neuronal cytoskeleton

Bush, M. S., Eagles, P. A. M., & Gordon‐Weeks, P. R. (1996) · The Cytoskeleton · doi:10.1016/s1874-6020(96)80009-7 · Cited by 5

Identification of a microtubule-binding domain sequence in pancreatic messenger RNAs

Neuville, P., Michalik, L., & Launay, J. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(93)90038-3 · Cited by 5

The contribution of N-terminally modified amyloid beta to the etiology of Alzheimer's disease

Wittnam, J. L. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3182 · Cited by 5

GSK-3β coordinates axonal microtubule organisation through Shot and TauPreprint

Voelzmann, A., Nuhu-Soso, L., Roof, A., Patel, S., Bennett, H. J., Adamson, A. D., Bentley, M., Evans, G. J. O., & Hahn, I. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.08.611864 · Cited by 5

Ptprd deficiency promotes tau hyperphosphorylation and impairs cognitive function in aged mice

Foncea-Bitrán, A., Franchini, N., Tobar, I., Thienel, S., Retamal, I. N., Cancino, G. I., & Cornejo, F. (2025) · Biological Research · doi:10.1186/s40659-025-00607-4 · Cited by 4

Mixtures of Intrinsically Disordered Neuronal Protein Tau and Anionic Liposomes Reveal Distinct Anionic Liposome-Tau Complexes Coexisting with Tau Liquid–Liquid Phase-Separated Coacervates

Tchounwou, C. K., Jobanputra, A. J., Lasher, D., Fletcher, B. J., Jacinto, J., Bhaduri, A., Best, R. L., Fisher, W. S., Ewert, K. K., Li, Y., et al. (2024) · Langmuir · doi:10.1021/acs.langmuir.4c02471 · Cited by 4

Passive Immunotherapy in Alzheimer’s Disease

Dolan, P. J., & Zago, W. M. (2018) · InTech eBooks · doi:10.5772/intechopen.76299 · Cited by 4

[Phosphorylation of tau and Alzheimer's disease].

García, T., & Jay, D. (2004) · PubMed · Cited by 4

Molecular Pathobiology of Alzheimer’s Disease

Harrington, C. R., & Wischik, C. M. (1994) · Springer eBooks · doi:10.1007/978-1-4615-6805-6_13 · Cited by 4

A Novel Correlation Between the Levels of β‐Amyloid Protein Precursor and τ Transcripts in the Aged Human Brain

Oyama, F., Shimada, H., Oyama, R., Titani, K., & Ihara, Y. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08354.x · Cited by 4

Cytoplasmic domains of the myelin-associated glycoprotein

Kursula, P. (2000) · Cited by 4

Tau seeding activity in the cerebrospinal fluid of Alzheimer disease patients predicts short-term cognitive decline

Houzé, L., Dhénain, M., Lam, S., Petit, F., Haı̈k, S., Mouton‐Liger, F., Hugon, J., Dam, J., Paquet, C., Jockers, R., et al. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01792-w · Cited by 3

Flavonoid-Based Derivatives for Modulating Various Targets of Alzheimer’s Disease

Pandey, J. (2023) · Springer eBooks · doi:10.1007/978-981-99-6038-5_11 · Cited by 3

Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context

Bali, S., Wydorski, P. M., Singh, R., Nuland, N. E. V., Wosztyl, A., Morgan, N., Perez, V. A., Chen, D., Chen, J., Rizo, J., et al. (2025) · Structure · doi:10.1016/j.str.2025.11.009 · Cited by 3

Microtubule-Associated Protein MAP2 Shares a Microtubule Binding Motif with Tau Protein

Lewis, S. A., Wang, D. H., & Cowan, N. J. (1988) · Science · doi:10.1126/science.3142041 · Cited by 483

Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains

Himmler, A., Drechsel, D. N., Kirschner, M. W., & Martin, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1381-1388.1989 · Cited by 555

Probing Structural Features of Tau Binding to Tubulin and Microtubules

Fung, H. Y. J., & Rhoades, E. R. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2018.11.1392

The “Jaws” of the Tau-Microtubule Interaction

Mukrasch, M. D., von Bergen�, M., Biernat, J., Fischer, D., Griesinger, C., Mandelkow�, E., & Zweckstetter, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607159200 · Cited by 203

The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease

Crowther, R. A., Olesen, O. F., Jakes, R., & Goedert, M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81094-3 · Cited by 167