Cited by 916Microtubule and mitosis dynamicsAlzheimer's disease research and treatmentsCancer Treatment and Pharmacology

The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Cleveland, Don W., Hwo, Shu-Ying, Kirschner, Marc W.·1977·Journal of Molecular Biology

DOI 10.1016/0022-2836(77)90213-3

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1016/0022-2836(77)90213-3

Cites

18 of 18 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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 316,394
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
Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations
Weisenberg, R. C. (1972) · Science · doi:10.1126/science.177.4054.1104 · Cited by 1,216
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
Self-citation
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 444
PURIFICATION OF TUBULIN AND ASSOCIATED HIGH MOLECULAR WEIGHT PROTEINS FROM PORCINE BRAIN AND CHARACTERIZATION OF MICROTUBULE ASSEMBLY IN VITRO*
Borisy, G. G., Marcum, J. M., Olmsted, J. B., Murphy, D. B., & Johnson, K. A. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb19196.x · Cited by 424
Nucleated Assembly of Microtubules in Porcine Brain Extracts
Borisy, G. G., & Olmsted, J. B. (1972) · Science · doi:10.1126/science.177.4055.1196 · Cited by 322
Ultrastructural localization of the high molecular weight proteins associated with in vitro-assembled brain microtubules
Dentler, W., Granett, S. E., & Rosenbaum, J. L. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.65.1.237 · Cited by 261
Identity and polymerization-stimulatory activity of the nontubulin proteins associated with microtubules
Murphy, D. B., Vallee, R. B., & Borisy, G. G. (1977) · Biochemistry · doi:10.1021/bi00631a004 · Cited by 186
Properties of the depolymerization products of microtubules from mammalian brain
Weingarten, M., Suter, M. M., Littman, D. R., & Kirschner, M. W. (1974) · Biochemistry · doi:10.1021/bi00724a012 · Cited by 170
Self-citation

Show all 18 references

Research works printed but not linked: 6

Kirschner, 1974, 71, 1159
Murphy, 1975, 72, 2696
Shelanski, 1973, 70, 765
Sloboda, 1975, 72, 177
Weingarten, 1975, 72, 1858
Witman, 1976, 73, 4070

Sorted by citations

Items 701–800 of 916

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
Exploring the Therapeutic Potential of Phosphorylated Cis-Tau Antibody in a Pig Model of Traumatic Brain Injury
Shin, S. S., Mazandi, V. M., Schneider, A. L. C., Morton, S., Starr, J. P., Weeks, M. K., Widmann, N. J., Jang, D. H., Kao, S.-H., Ahlijanian, M. K., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11071807 · Cited by 5
“Tau proteins are highly expressed in neurons as well as astroglia and oligodendroglia [1] and play an important role in maintaining the stability of axonal microtubules [2].”
Background
Transfection of Human Neuroblastoma Cells with Alzheimer’s Disease Brain Hallmarks as a Promising Strategy to Investigate the Role of Neurosteroidogenesis in Neuroprotection
Patte‐Mensah, C., Meyer, L., Schaeffer, V., Eckert, A., & Mensah‐Nyagan, A. G. (2012) · BioValley monographs · doi:10.1159/000339189 · Cited by 6
Protein Conformational Dynamics upon Association with the Surfaces of Lipid Membranes and Engineered Nanoparticles: Insights from Electron Paramagnetic Resonance Spectroscopy
Georgieva, E. R. (2020) · Molecules · doi:10.3390/molecules25225393 · Cited by 7
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
The Role of Tau Protein in Diseases
Das Bhaskar, C. (2018) · Annals of Advances in Chemistry · doi:10.29328/journal.aac.1001010 · Cited by 6
Evolution of research on cellular motility over five decades
Pollard, T. D. (2018) · Biophysical Reviews · doi:10.1007/s12551-018-0473-9 · Cited by 6
“…complex (Zheng et al. 1995)), stabilize minus ends (CAMSAPs (Akhmanova and Steinmetz 2015)), stabilize the wall of the microtubule (MAP2/tau family (Cleveland et al. 1977)), kinesins that promote dissociation of subunits from the ends (kinesin 8, kinesin 13, and kinesin 14 (Howard and Hyman…”
Background
The effects of nerve growth factor and dibutyryl cyclic AMP on cytoskeletal densities in cultured sensory ganglia
Doane, K. J., Roisen, F. J., & Wilson, F. J. (1992) · Tissue and Cell · doi:10.1016/0040-8166(92)90053-a · Cited by 6
The Calcium Sensitivity of MAP‐2 and Tau Microtubules in the Presence of Calmodulina
Bender, P. K., & Rebhun, L. I. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38408.x · Cited by 6
High molecular weight tau distribution and microtubule stability in neuroblastoma N115 cells
Gache, Y., Guilleminot, J., & Nunez, J. (1994) · Experimental Brain Research · doi:10.1007/bf00227196 · Cited by 6
“1984; Couchie and Nunez 1985) which are replaced by five to six variants of 5065 kDa in adulthood (Cleveland et al. 1977).”
Background
Biochemistry of the Ca2+- and Calmodulin-Dependent Regulation of the Cytoskeleton
Kakiuchi, S. (1985) · Springer eBooks · doi:10.1007/978-3-642-70070-5_11 · Cited by 6
Control of microtubule polymerization and stability
Ávila, J., & Díaz‐Nido, J. (1995) · The Cytoskeleton · doi:10.1016/s1874-6020(06)80005-4 · Cited by 6
Synthesis of azido tubulin: a photoaffinity label for tubulin-binding proteins
Balczon, R., & Brinkley, B. R. (1989) · Biochemistry · doi:10.1021/bi00447a033 · Cited by 6
Purification of bovine adrenocortical and brain tubulin A comparative study
Ray, P., Strott, C. A., & Nath, J. (1979) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(79)90223-x · Cited by 6
Solubilization of SV40 Plasma‐Membrane‐Associated Large Tumor Antigen Using Single‐Phase Concentrations of 1‐Butanol
Maxwell, S. A., Santos, M., Wong, C., Rasmussen, G., & Butel, J. S. (1989) · Molecular Carcinogenesis · doi:10.1002/mc.2940020607 · Cited by 6
Tubulin
Wallin, M., & Deinum, J. (1983) · Springer eBooks · doi:10.1007/978-1-4899-4555-6_4 · Cited by 6
The role of microtubule-associated protein tau in netrin-1 attractive signaling
Huang, H., Majumder, T., Khot, B., Suriyaarachchi, H., Yang, T., Shao, Q., Tirukovalluru, S., & Liu, G. (2024) · Journal of Cell Science · doi:10.1242/jcs.261244 · Cited by 5
3D-QSAR, design, molecular docking and dynamics simulation studies of novel 6-hydroxybenzothiazole-2-carboxamides as potentially potent and selective monoamine oxidase B inhibitors
Xie, D., Tian, Y., Cao, L., Guo, P., Cai, Z., & Zhou, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1545791 · Cited by 5
Microtubule-Associated Proteins and Microtubule-Interacting Proteins
Kavallaris, M., Don, S., & Verrills, N. M. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_4 · Cited by 5
In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas.
Neuville, P., Vanier, M. T., Michalik, L., & Launay, J. F. (1995) · PubMed · Cited by 5
Huntingtin and Other Neurodegeneration-Associated Proteins in the Development of Intracellular Pathologies: Potential Target Search for Therapeutic Intervention
Churkina, A. S., Shakhov, A. S., Kotlobay, A. A., & Alieva, I. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415533 · Cited by 5
“It turned out that this protein can stimulate the assembly of microtubules [34].”
Background
Animal models in Alzheimer's disease: Biological plausibility and mood disorders
Castillo-Rangel, C., Marín, G., Díaz-Chiguer, D. L., Zarate-Calderon, C., Viveros-Martínez, I., Salazar, F., Torres-Pasillas, J. G., Hernández-Contreras, K. A., Vega-Quesada, L. A., Cano-Ortega, Y., et al. (2023) · Neurology Perspectives · doi:10.1016/j.neurop.2023.100110 · Cited by 5
Biochemical and Anthropometric Parameters for the Early Recognition of the Intrauterine Growth Restriction and Preterm Neonates at Risk of Impaired Neurodevelopment
Aisa, M. C., Cappuccini, B., Favilli, A., Datti, A., Nardicchi, V., Coata, G., & Gerli, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411549 · Cited by 5
“Tau, the tubulin-associated unit protein, is a highly soluble microtubule assembly molecule present in both the neurons of the central nervous system and oligodendrocytes [27,28].”
Background
Genetics of Frontotemporal Dementia
Heetveld, S., Rizzu, P., & Heutink, P. (2015) · Springer eBooks · doi:10.1007/978-3-319-17223-1_5 · Cited by 5
Comparison of the neuropsychological mechanisms of 2,6-diisopropylphenol and N-methyl-D-aspartate receptor antagonist against electroconvulsive therapy-induced learning and memory impairment in depressed rats
LIU, G., Liu, C., & NING-ZHANG, X. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3803 · Cited by 5
“These repeats are involved in the microtubule-associated region of the Tau proteins, promoting the assembly and stabilisation of axon microtubules (9), maintaining the space between microtubules (10), affecting the axonal material transport of nerve cells, promoting neuronal Comparison of the neuropsychological mechan…”
Induction of lysosomal abnormalities and tau hyperphosphorylation in human neuroblastoma cells by colchicine and okadaic acid: Evidence that microtubule disruption contributes to Alzheimer neurodegeneration
Shea, T. B. (1996) · Neuroscience Research Communications · doi:10.1002/(sici)1520-6769(199607)19:1 · Cited by 5
Is tau a suitable therapeutical target in tauopathies?
de Barreda, E. G. (2010) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v1.i5.81 · Cited by 5
Antibodies directed against microtubule proteins from Drosophila melanogaster cross react with similar proteins in the rat brain
Alcantara, A. A., Srinivasan, S., Reilein, A. R., & Karr, T. L. (1995) · Brain Research · doi:10.1016/0006-8993(95)00953-x · Cited by 5
Control of Growth by Cytokinin: An Examination of Tubulin Synthesis During Cytokinin — Induced Growth in Cultured Cells of Paul’s Scarlet Rose
Fosket, D. E., Morejohn, L. C., & Westerling, K. E. (1981) · Proceedings in life sciences · doi:10.1007/978-3-642-68035-9_18 · Cited by 5
Quick purification of recombinant human truncated tau proteins for immunoanalysis
Kontseková, E., Cattaneo, A., & Novák, M. (1995) · Journal of Immunological Methods · doi:10.1016/0022-1759(95)00120-y · Cited by 5
Maturation of cerebellar granule cells is delayed in cultures derived from ethanol‐treated chick embryos: Survival and proliferation studies
Srivastava, N., & Vernadakis, A. (1995) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(95)00031-b · Cited by 5
Strongly basic polypeptides among microtubule associated proteins
Bärmann, M., Mann, K., & Fasold, H. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91484-x · Cited by 5
Structure and mechanism of microtubule stabilization and motor regulation by MAP9Preprint
Çetin, B., Taheri, A., Gölcük, M., Monroy, B. Y., Fernandes, J., Ori-McKenney, K. M., Gür, M., Nogales, E., & Yıldız, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.17.688911 · Cited by 5
“These results contrast with earlier reports of the MT stabilization role of tau and MAP7 2, 22, 23 , and are more consistent with recent studies showing that tau does not significantly affect MT stabilization in neurons 24 .”
Mitochondrial Quality Control in Alzheimer’s Disease: Insights from Caenorhabditis elegans Models
Ganguly, U., Carroll, T., Nehrke, K. W., & Johnson, G. V. W. (2024) · Antioxidants · doi:10.3390/antiox13111343 · Cited by 5
20 years of taxane therapy in prostate cancer — the past, present and future
Carceles‐Cordon, M., Rodríguez-Bravo, V., Petrylak, D. P., & Domenech, J. M. D. (2025) · Nature Reviews Urology · doi:10.1038/s41585-025-01104-9 · Cited by 4
“48) or tau 49,50 .”
Tau and Alzheimer’s Disease: Molecular Mechanisms and Treatment Approaches
Reiss, A. B., Muhieddine, D., Leon, A. Z. D., Voloshyna, I., Gomolin, I. H., & Pinkhasov, A. (2021) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-021-01092-y · 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
Tau from SPAM Transgenic Mice Exhibit Potent Strain-Specific Prion-Like Seeding Properties Characteristic of Human Neurodegenerative Diseases
Smith, E. D., Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2025) · NeuroMolecular Medicine · doi:10.1007/s12017-025-08850-4 · Cited by 7
“Tau has long been recognized as a microtubule-associated protein that stabilizes microtubules (Cleveland et al., 1977a, 1977b; Drubin & Kirschner, 1986; Gustke et al., 1994; Weingarten et al., 1975).”
R ole of Tau, a microtubule associated protein, in Drosophila photoreceptor morphogenesis
Nam, S. (2016) · genesis · doi:10.1002/dvg.22966 · Cited by 4
“Because Tau has been known as a microtubule associated protein (Cleveland et al., 1977; Doerflinger et al., 2003), it is expected to colocalize with microtubule cytoskeletons.”
Background
In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas
Neuville, P., Vanier, M. T., Michalik, L., & Launay, J. F. (1995) · The Histochemical Journal · doi:10.1007/bf02388454 · Cited by 4
Prospects and Challenges for Alzheimer Therapeutics
Wolfe, M. S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00023-x · Cited by 5
Proximity Ligation Assay: A Tool to Study Endogenous Interactions Between Tau and Its Neuronal Partners
Bretteville, A., Demiautte, F., & Chapuis, J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_18 · Cited by 4
“Polymerization and stabilization of microtubules are its main described functions [1, 2], which are mediated through interaction of Tau with tubulin via the binding of three or four microtubule binding domains, depending on the Tau isoform considered (for review [3]).”
Background
Generation of a monoclonal antibody to the carboxy-terminal domain of tau by immunization with the amino-terminal domain of the amyloid precursor protein
Philippe, B., Brion, J., Coppens, E., & Octave, J. (1996) · Journal of Neuroscience Research · doi:10.1002/jnr.490460602 · Cited by 4
Molecular Aspects of Memory Dysfunction in Alzheimer’s Disease
Chin, J., Roberson, E. D., & Mucke, L. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00015-2 · Cited by 5
Potential neuroprotective strategies against tauopathy
Wheeler, J. M., Guthrie, C. R., & Kraemer, B. C. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120017 · Cited by 4
Minimalistic in vitro systems for investigating tau pathology
Hallinan, G. I., Pitera, A. P., Patel, P., West, J. J., & Deinhardt, K. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.09.032 · Cited by 4
Modulation of poly(A)(+)mRNA-metabolizing and transporting systems under special consideration of microtubule protein and actin
Müller, W. E. G., Bernd, A., & Schröder, H. C. (1983) · Springer eBooks · doi:10.1007/978-1-4613-3879-6_12 · Cited by 4
Microtubules in the Nervous System
Soifer, D., & Mack, K. (1984) · Springer eBooks · doi:10.1007/978-1-4684-4586-2_10 · Cited by 4
Similarities and differences between tau protein and chromobindin A
Sternberg, H., Baudier, J., Akizuki, K., Cole, G. M., Martin, W. H., Creutz, C. E., Timiras, P. S., & Cole, R. D. (1988) · Neurochemistry International · doi:10.1016/0197-0186(88)90050-2 · Cited by 4
Animal models of neurodegenerative dementing disorders other than Alzheimer's disease
Giasson, B. I., Lee, V. M. ‐., & Trojanowski, J. Q. (2004) · Clinical Neuroscience Research · doi:10.1016/j.cnr.2004.04.008 · Cited by 4
Brain-derived neurotrophic factor : generation and characterization of adult mice lacking BDNF in the adult brain
Rauskolb, S. (2008) · edoc (University of Basel) · doi:10.5451/unibas-004587325 · Cited by 4
The neuronal cytoskeleton: an insight for neurosurgeons
Fitzpatrick, M. O., Dewar, D., Teasdale, G. M., & Graham, D. I. (1996) · British Journal of Neurosurgery · doi:10.1080/02688699647122 · 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
Calmodulin and Cytoskeleton
Kakiuchi, S., Sobue, K., Fujita, M., Muramoto, Y., Kanda, K., & Morimoto, K. (1982) · Springer eBooks · doi:10.1007/978-1-4684-4328-8_12 · Cited by 4
FRACTIONATION AND ELECTROPHORETIC ANALYSIS OF MICROTUBULE PROTEINS FROM RAT BRAIN
Kobayashi, T. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-615080-3.50010-0 · Cited by 4
Post-translational modifications as a regulatory code for tau function in health and disease
Nordbeck, A. J., Sharma, B., Garcia, C. A., & Tseng, J. (2026) · Frontiers in Dementia · doi:10.3389/frdem.2026.1834737 · Cited by 3
“In healthy neurons, tau dynamically associates with microtubules to regulate axonal stability, intracellular transport, and neuronal polarity (Weingarten et al., 1975; Cleveland et al., 1977; Wang and Mandelkow, 2016).”
Actin assembly mediated by a nucleation promoting factor WASH is involved in MTOC–TMA formation during Xenopus oocyte maturation
Yamagishi, Y., & Abe, H. (2017) · Cytoskeleton · doi:10.1002/cm.21428 · Cited by 3
“MTs were purified from porcine brain following the method of Cleveland et al. (1977) with slight modification.”
Method
A mathematical model on the propagation of tau pathology in neurodegenerative diseases
Chen, C., Tseng, Y.-H., & Ward, J. (2024) · Journal of Mathematical Biology · doi:10.1007/s00285-024-02101-z · Cited by 4
“8 nmol/daycm 3 , where we have assumed the molecular mass of a monomer tau protein to be 55kDa (Cleveland et al. 1977).”
Presenilin 1 mutations increase amyloid precursor protein production and proteolysis in Xenopus laevis oocytes
Heyn, S. N., & Vulliet, P. R. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02312-5 · Cited by 3
Controlled Tau Cleavage in Cells Reveals Abnormal Localizations of Tau Fragments
Fourest‐Lieuvin, A., Vinit, A., Blot, B., Perrot, A., Denarier, É., Saudou, F., & Arnal, I. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.08.016 · Cited by 3
“Tau is a neuronal protein initially identified as a microtubule-associated protein (MAP) able to stabilize and bundle microtubules (Weingarten et al., 1975; Cleveland et al., 1977a; 1977b; Chen et al., 1992; Kanai et al., 1992; Takemura et al., 1992; Samsonov et al., 2004; Prezel et al., 2018).”
Background
Therapeutic Contribution of Tau-Binding Thiazoloflavonoid Hybrid Derivatives Against Glioblastoma Using Pharmacological Approach in 3D Spheroids
Relave, E. T., Hedna, R., Maio, A. D., Devred, F., Kovacic, H., Robin, M., & Breuzard, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111785 · Cited by 3
“The discovery of the Tau protein and its crucial role in tubulin assembly dates back to the 1970s [1,23,24].”
Background
Frontotemporal dementia with parkinsonism linked to Chromosome 17
Forman, M. S., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Cambridge University Press eBooks · doi:10.1017/cbo9780511544873.036 · Cited by 3
A Phosphorylated Tau Species Is Transiently Present in Developing Cortical Neurons and Is Not Associated with Stable Microtubules
Brion, J., Couck, A. M., Conreur, J.-L., & Octave, J. N. (1995) · Springer eBooks · doi:10.1007/978-3-642-79423-0_13 · Cited by 3
Selected genetically engineered models relevant to human neurodegenerative disease
Price, D. L., Borchelt, D., Lee, M. K., & Wong, P. C. (2005) · Cambridge University Press eBooks · doi:10.1017/cbo9780511544873.016 · Cited by 3
Neurofilament-Like Immunoreactivity in the Sea Anemone Condylactis gigantea (Cnidaria: Anthozoa)
Dellacorte, C., Anderson, D. S., McClure, W. O., & Kalinoski, D. L. (1994) · Biological Bulletin · doi:10.2307/1542242 · Cited by 3
Disruption of tubulin polymerization and cell proliferation by 1‐naphthylarsonic acid
Mahinpour, R., Riazi, G. H., Shokrgozar, M. A., Sarbolouki, M. N., Ahmadian, S., Douraghi, M., Hadi‐Alijanvand, H., Azadmanesh, K., Heidari, M., Gheshlaghi, Z. N., et al. (2012) · Cell Biology International · doi:10.1042/cbi20100603 · Cited by 3
“Several classes of MAPs act by stabilizing microtubules (Sloboda et al., 1976; Cleveland et al., 1977; Parysek et al., 1984; Wiche et al., 1991).”
Background
Propofol can Protect Against the Impairment of Learning-memory Induced by Electroconvulsive Shock via Tau Protein Hyperphosphorylation in Depressed Rats
Liu, W.-F., & Liu, C. (2015) · Chinese Medical Sciences Journal · doi:10.1016/s1001-9294(15)30020-1 · Cited by 3
Development of the Axonal and Dendritic Cytoskeleton
Riederer, B. M. (1995) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60261-1 · Cited by 3
Tau and beta-amyloid in Alzheimer’s Disease: Theories, treatments strategies, and future directions
Colautti, J., & Nagales, K. (2020) · The Meducator · doi:10.15173/m.v1i37.2502 · Cited by 3
Influence of Phospholipids and Sequential Kinase Activities on Tau in Vitro
SHEA, T. B., & Ekinci, F. J. (1998) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4869-0_11 · Cited by 3
Systems of Microtubules
Bershadsky, A. D., & Vasiliev, J. M. (1988) · Springer eBooks · doi:10.1007/978-1-4684-5278-5_3 · Cited by 3
Purification of a stimulator of microtubule assembly from bovine thyroid.
Berk, B. C., & Hinkle, P. M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68485-1 · Cited by 3
Biochemical characterization of related microtubule proteins in Drosophila melanogaster and adult rat brain
Srinivasan, S., & Karr, T. L. (1995) · Brain Research · doi:10.1016/0006-8993(95)00952-8 · Cited by 3
Comparative study of shark and beef brain microtubules
Langford, G. M. (1981) · Biosystems · doi:10.1016/0303-2647(81)90032-0 · Cited by 3
Tubulin Synthesis during the Cell Cycle
Bird, R. C., Zimmerman, S. B., & Zimmerman, A. M. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-747750-3.50013-2 · Cited by 3
A novel pThr217 tau monoclonal antibody reveals neuropathological heterogeneity in tauopathies
Paterno, G., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Prokop, S., & Giasson, B. I. (2025) · Scientific Reports · doi:10.1038/s41598-025-04291-y · Cited by 2
Tau Axonal Sorting and Interaction With Synaptic Plasticity Modulators Is Domain‐ and Isoform‐Dependent in Human iPSC ‐Derived Neurons
Bell‐Simons, M., Breuer, H., Wunderlich, L., Chmes, H., Adam, D., Klimek, J., Buchholz, S., & Zempel, H. (2025) · Aging Cell · doi:10.1111/acel.70215 · Cited by 2
The discovery of tau protein
Kirschner, M. W. (2023) · Cytoskeleton · doi:10.1002/cm.21796 · Cited by 2
“It was not a single band on a gel but rather a set of about four or five proteins that migrated just a bit slower than tubulin on an SDS gel (Cleveland et al., 1977a).”
BackgroundSelf-citation
Structure and function of Full-length Tau
Vallés‐Saiz, L., Domene-Serrano, I., Picher, Á. J., Pérez, M., García‐Escudero, V., Hernández, F., & Ávila, J. (2025) · PLoS ONE · doi:10.1371/journal.pone.0335251 · Cited by 2
The potential of circulating autoantibodies in the early diagnosis of Alzheimer’s disease
Yin, W., & Stover, C. M. (2017) · AIMS Allergy and Immunology · doi:10.3934/allergy.2017.2.62 · Cited by 2
“The τ protein has many potential phosphorylation sites, if these sites are hyperphosphorylated during inflammation in CSF and brain in AD patients, this abnormal structure results in the self-assembly of tangles of paired helical filaments and straight filaments which lead to neuronal damage [27].”
Contribution of Multivesicular Bodies to the Prion-Like Propagation of Lesions in Alzheimer’s Disease
Vingtdeux, V., Buée, L., & Sergeant, N. (2011) · InTech eBooks · doi:10.5772/20567 · Cited by 1
“Tau proteins are known to act as promoter of tubulin polymerization in vitro, and are involved in axonal transport (Brandt and Lee, 1993; Cleveland et al., 1977a; Weingarten et al., 1975).”
Nerve Growth Factor Enhances Tau Isoform Expression and Transcription in IMR32 Cells
Cragg, C. L., & Kalisch, B. E. (2014) · Neuroscience & Medicine · doi:10.4236/nm.2014.52015 · Cited by 2
Sensitive detection of proteins in polyacrylamide gel via isatoic anhydride derivatization: Introduction of a low‐cost fluorescent prelabeling procedure
Asadollahi, K., Rafiee, S., & Riazi, G. H. (2016) · Electrophoresis · doi:10.1002/elps.201600237 · Cited by 2
Biomarkers of Alzheimer’s disease
Pitt, J. E. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404630-6.00048-8 · Cited by 2
Effects of Formaldehyde on Protein (Tau) Aggregation and Cytotoxicity
He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_7 · Cited by 2
Alzheimer’s Disease
Tam, J. H. K., & Pasternak, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801942-9.00004-5 · Cited by 2
Tau Phosphorylation
Ávila, J., & Hernández, F. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_3 · Cited by 2
Novel Conformation-Dependent Tau Antibodies Are Modulated by Adjacent Phosphorylation Sites
Paterno, G., Torrellas, J., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Hery, G. P., Prokop, S., & Giasson, B. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813676 · Cited by 2
“Early investigation of tau proteins found that tau is highly soluble, heat stable, and possesses little secondary structure [2,3,51].”
Background
Diabetic rat serum has an increased capacity to inhibit brain microtubule formation in vitro
McLean, W. G., Beahon, S. J., & Casson, I. F. (1986) · Neurochemical Pathology · doi:10.1007/bf02834356 · Cited by 2
“These include a number of microtubule-associated proteins ( Cleveland et al., 1977, Herzog and Weber, 1978; Black and Kurdyla, 1983), phospholipids (Daleo et al., 1977; Caron and Berlin, 1979), and ions (Erickson and Voter, 1976; Regula et al., 1981).”
Background
Alzheimer disease models and human neuropathology: similarities and diVerences
Duyckaerts, C. J., Potier, M., & Delatour, B. (2008) · Cited by 2
Tau and High Molecular Weight Microtubule Associated Proteins in Aluminum-Induced Neurofibrillary Pathology
New, G. A., & Muma, N. A. (1995) · Advances in behavioral biology · doi:10.1007/978-1-4757-9145-7_27 · Cited by 2
The Biogenesis of Supramolecular Structures
Anderson, R. G. W. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-289504-3.50015-2 · Cited by 2
Axonal Tau sorting depends on the PRR2 domain and 0N4R-specific interactions hint at distinct roles of Tau isoforms in synaptic plasticityPreprint
Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.28.601286 · Cited by 3
“The microtubule-associated protein Tau regulates the dynamic assembly and disassembly of microtubule (MT) filaments in human brain neurons (Cleveland et al., 1977b; Gustke et al., 1994; Kadavath et al., 2015; Kanai & Hirokawa, 1995; Weingarten et al., 1975).”
Background
Microtubule associated proteins of goat brain
Majumder, A., Banerjee, S. K., & Sarkar, P. K. (1982) · Journal of Biosciences · doi:10.1007/bf02702581 · Cited by 1
Tau-Centric Therapies for Treating Alzheimer’s Disease
Quraishe, S., Cowan, C. M., & Mudher, A. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00005-3 · Cited by 1
Die krankheitsassoziierte Tau‐Phosphorylierung behindert die Tubulinpolymerisation in Tau‐Kondensaten
Savastano, A., Flores‐Solis, D., Kadavath, H., Biernat, J., Mandelkow�, E., & Zweckstetter, M. (2020) · Angewandte Chemie · doi:10.1002/ange.202011157 · Cited by 1
In silico designed microtubule-stabilizer drugs against tauopathy in Alzheimer’s disease
Sarukhanyan, E., & Dandekar, T. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2139760 · Cited by 1
Lithium mitigates hippocampal tau pathology in a rodent model of traumatic brain injury
Donison, N. S., Palik, J., Hintermayer, M. A., Volkening, K., & Strong, M. J. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02170-1 · Cited by 1
“Tau protein plays a critical role in the healthy functioning of the central nervous system by stabilizing microtubules and regulating axonal transport [25, 26, 117].”
How do copper( ii ) and zinc( ii ) bind to tau protein, and how might this promote aggregation?
Balogh, B. D., Natale, G. D., Pappalardo, G., & Várnagy, K. (2026) · Dalton Transactions · doi:10.1039/d5dt03057a · Cited by 1
Tau protein as a regulator of mitochondrial function and dynamics
Tsakiri, E. N., Campos‐Marques, C., Ploumi, C., Skourti, K., Roussos, A., Mytilinaiou, E., Vamvaka-Iakovou, A., Ferreira, I. L., Dioli, C., Gianniou, D. D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2521642123 · Cited by 1

Authors: Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W.
Affiliations: Princeton University (US)
ORCID: Cleveland, Don W.
Kirschner, Marc W.
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 1977-10
Volume: 116
Issue: 2
Pages: 207-225
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/0022-2836(77)90213-3
OpenAlex: W1971165215
Cited by: 915
References: 18
Citations by year: 2026: 12 · 2025: 19 · 2024: 20 · 2023: 25 · 2022: 24 · 2021: 43 · 2020: 26 · 2019: 29 · 2018: 26 · 2017: 36 · 2016: 20 · 2015: 20 · 2014: 24 · 2013: 16 · 2012: 20
FWCI: 11.02
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords: tau protein, microtubule-associated proteins, tubulin, microtubule assembly, microtubule nucleation, microtubule depolymerization, critical concentration, protein purification, phosphocellulose chromatography, ring structure
MeSH terms: Chromatography, Agarose, Electrophoresis, Polyacrylamide Gel, Glycoproteins, Microtubules, Molecular Weight, Proteins, Tubulin

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

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks