Phosphorylation determines two distinct species of tau in the central nervous system

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.76.9.4350 · Cited by 51,421 · see citing works

Continuous cultures of fused cells secreting antibody of predefined specificity

Köhler, G., & Milstein, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,200 · see citing works

Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii

Voth, D. E., & Heinzen, R. A. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00901.x · Cited by 11,773 · see citing works

THE UNLABELED ANTIBODY ENZYME METHOD OF IMMUNOHISTOCHEMISTRY PREPARATION AND PROPERTIES OF SOLUBLE ANTIGEN-ANTIBODY COMPLEX (HORSERADISH PEROXIDASE-ANTIHORSERADISH PEROXIDASE) AND ITS USE IN IDENTIFICATION OF SPIROCHETES

Sternberger, L. A., Hardy, P. H., Cuculis, J. J., & Meyer, H. G. (1970) · Journal of Histochemistry & Cytochemistry · doi:10.1177/18.5.315 · Cited by 5,042 · see citing works

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works

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 · see citing works

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 · see citing works

Derivation of specific antibody‐producing tissue culture and tumor lines by cell fusion

Köhler, G., & Milstein, C. (1976) · European Journal of Immunology · doi:10.1002/eji.1830060713 · Cited by 1,927 · see citing works

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 · see citing works

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 1,462 · see citing works

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881 · see citing works

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works

Tau protein function in living cells.

Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works

Microtubule-Associated Proteins

Olmsted, J. B. (1986) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.02.110186.002225 · Cited by 565 · see citing works

The periodic association of MAP2 with brain microtubules in vitro.

Kim, H. W., Binder, L. I., & Rosenbaum, J. L. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.80.2.266 · Cited by 510 · see citing works

Microtubule-associated proteins and the stimulation of tubulin assembly in vitro

Sloboda, R. D., Dentler, W. L., & Rosenbaum, J. L. (1976) · Biochemistry · doi:10.1021/bi00665a026 · Cited by 437 · see citing works

Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: a difference between dendritic and axonal cytoskeletons

Bernhardt, R., & Matus, A. (1984) · Journal of Comparative Neurology · doi:10.1002/cne.902260205 · Cited by 421 · see citing works

Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence

De Camilli, P., Miller, P. E., Navone, F., Theurkauf, W. E., & Vallee, R. B. (1984) · Neuroscience · doi:10.1016/0306-4522(84)90194-5 · Cited by 381 · see citing works

Biochemical and immunological analyses of cytoskeletal domains of neurons.

Peng, I., Binder, L. I., & Black, M. M. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.1.252 · Cited by 230 · see citing works

Differential Localization of MAP‐2 and Tau in Mammalian Neurons in Situ a

Binder, L. I., Frankfurter, A. J., & Rebhun, L. I. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38392.x · Cited by 210 · see citing works

Separation and characterization of microtubule proteins from calf brain

Berkowitz, S. A., Katagiri, J., Binder, H. K., & Williams, R. C. (1977) · Biochemistry · doi:10.1021/bi00644a035 · Cited by 200 · see citing works

Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes.

Drubin, D. G., Caput, D., & Kirschner, M. W. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.98.3.1090 · Cited by 164 · see citing works

Heterogeneity of Microtubule‐Associated Proteins and Brain Development

Francon, J., Lennon, A. M., Fellous, A., Mareck, A., Pierre, M., & Nunez, J. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb07072.x · Cited by 155 · see citing works

Microtubule-associated protein 2 within axons of spinal motor neurons: associations with microtubules and neurofilaments in normal and beta,beta'-iminodipropionitrile-treated axons.

Papasozomenos, S. C., Binder, L. I., Bender, P. K., & Payne, M. R. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.74 · Cited by 90 · see citing works

Monoclonal antibodies to the glycoprotein of vesicular stomatitis virus: comparative neutralizing activity

Volk, W. A., Synder, R. M., Benjamin, D. C., et al. (1982) · Journal of Virology · doi:10.1128/jvi.42.1.220-227.1982 · Cited by 88 · see citing works

Microtubule-associated protein 2 (MAP2) is present in astrocytes of the optic nerve but absent from astrocytes of the optic tract

Papasozomenos, S. C., & Binder, L. (1986) · Journal of Neuroscience · doi:10.1523/jneurosci.06-06-01748.1986 · Cited by 50 · see citing works

The Binding of MAP‐2 and Tau on Brain Microtubules in Vitro: Implications for Microtubule Structurea

Kim, H., Jensen, C. G., & Rebhun, L. I. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38396.x · Cited by 46 · see citing works

Analysis of the relationship of bovine high molecular weight protein-2 and tau protein using radioimmunoassay

Bender, P. K., Rebhun, L. I., & Benjamin, D. C. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90215-1 · Cited by 10 · see citing works

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works

Tau Kinetics in Neurons and the Human Central Nervous System

Sato, C., Barthélemy, N. R., Mawuenyega, K. G., Patterson, B. W., Gordon, B. A., Jockel-Balsarotti, J., Sullivan, M., Crisp, M. J., Kasten, T., Kirmess, K. M., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.015 · Cited by 586 · see citing works

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10369 · Cited by 388 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313 · see citing works

Tau isoform profile and phosphorylation state in dementia pugilistica recapitulate Alzheimer's disease

Schmidt, M., Zhukareva, V., Newell, K., Lee, V., & Trojanowski, J. (2001) · Acta Neuropathologica · doi:10.1007/s004010000330 · Cited by 230 · see citing works

Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.

Litersky, J. M., & Johnson, G. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45982-0 · Cited by 201 · see citing works

Pathological tau promotes neuronal damage by impairing ribosomal function and decreasing protein synthesis

Meier, S., Bell, M., Lyons, D. N., Rodriguez-Rivera, J., Ingram, A., Fontaine, S. N., Mechas, E., Chen, J., Wolozin, B., LeVine, H., et al. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.3029-15.2016 · Cited by 190 · see citing works

Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons.

Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179 · see citing works

Acetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment

Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works

Nuclear Tau and Its Potential Role in Alzheimer’s Disease

Bukar Maina, M., Al-Hilaly, Y., & Serpell, L. (2016) · Biomolecules · doi:10.3390/biom6010009 · Cited by 161 · see citing works

Proteolysis of tau by calpain

Johnson, G. V. W., Jope, R. S., & Binder, L. I. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91150-9 · Cited by 161 · see citing works

Sorting mechanisms of Tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding

Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144 · see citing works

Tau drives translational selectivity by interacting with ribosomal proteins

Koren, S. A., Hamm, M. J., Meier, S. E., Weiss, B. E., Nation, G. K., Chishti, E. A., Arango, J. P., Chen, J., Zhu, H., Blalock, E. M., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01970-9 · Cited by 122 · see citing works

Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges

Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110 · see citing works

Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00572 · Cited by 102 · see citing works

Tau‐66: evidence for a novel tau conformation in Alzheimer's disease

Ghoshal, N., García‐Sierra, F., Fu, Y., Beckett, L. A., Mufson, E. J., Kuret, J., Berry, R. W., & Binder, L. I. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00346.x · Cited by 97 · see citing works

Microtubule-Stimulated Phosphorylation of tau at Ser202 and Thr205 by cdk5 Decreases Its Microtubule Nucleation Activity

Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., & Hisanaga, S.-I. (1998) · Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022174 · Cited by 58 · see citing works

Tau acts as a mediator for<scp>A</scp>lzheimer's disease‐related synaptic deficits

Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53 · see citing works

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 · see citing works

Regulation and differential expression of tau mRNA isoforms as oligodendrocytes mature in vivo: Implications for myelination

Lopresti, P. (2002) · Glia · doi:10.1002/glia.10035 · Cited by 33 · see citing works

Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy

Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28 · see citing works

Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside

Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25 · see citing works

Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease

Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684

Rotational diffusion of Escherichia coli ribosomes

Pochon, F., Amand, B., & Lavalette, D. (1977) · Biochimie · doi:10.1016/s0300-9084(77)80208-3 · Cited by 5 · see citing works

Ribosomes from HeLa cells

Winckelmans, D., Hill, M., & Errera, M. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects · doi:10.1016/0926-6550(64)90197-5 · Cited by 14 · see citing works

Dissociation of Ribosomes on Polypeptide Chain Termination and Origin of Single Ribosomes

Kaempfer, R. O. R. (1970) · Nature · doi:10.1038/228534a0 · Cited by 70 · see citing works

Stability of free ribosomes, derived ribosomes and polysomes of the sea urchin

Infante, A. A., & Graves, P. N. (1971) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(71)90075-x · Cited by 32 · see citing works

Polyribosome metabolism in bacteriophage T4 infected Escherichia coli

Walsh, M. L., & Cohen, P. S. (1974) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(74)90195-7 · Cited by 4 · see citing works