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
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“Microtubule affinity has also been employed in the purification of other proteins such as MAP1, tau, and dynein (Vallee and Bloom, 1984; Cleveland et al., 1977; Nasr and Satir, 1985).”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Cleveland et al., 1977
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Cites
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-citationMicrotubule-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
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
Dentler, W., Granett, S. E., & Rosenbaum, J. L. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.65.1.237 · Cited by 261
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
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
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Pathogenesis of neurodegenerative diseases via templated recruitment
Guo, J. (2013) · ScholarlyCommons (University of Pennsylvania) · Cited by 1
From Protein Tangles to Genetic Variants: The Central Role of Tau in Neurodegenerative Disease
Julia, H., & Wade‐Martins, R. (2011) · InTech eBooks · doi:10.5772/29839 · Cited by 1
“The primary function of tau is the stabilisation of microtubules and the promotion of microtubule polymerisation, by binding to microtubules via the C-terminal MT-binding domain (Cleveland et al., 1977; Weingarten et al., 1975).”
Tau Phosphorylation as a Therapeutic Target in Alzheimer’s Disease
Medina, M., & Ávila, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00012-5 · Cited by 1
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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/bf00173092 · Cited by 5
Methods for Biochemical Isolation of Insoluble Tau in Rodent Models of Tauopathies
Canet, G., Rocaboy, E., Diego-Diàz, S., Whittington, R. A., Julien, C., & Planel, E. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_17 · Cited by 1
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“Although the microtubule-associated protein Tau has been described for nearly 50 years [1] and its role in neurodegenerative dementias has been firmly established [2,3], the physiological processes within neurons requiring this protein are less understood.”
BackgroundImmunopathogenesis of Alzheimer’s disease, Parkinson’s Disease, and other Neurodegenerative Diseases
Kumar, S., Shukla, A. K., Yadav, V. K., Srivastava, A., Dwivedi, D., & Singh, S. P. (2024) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815238754124010006 · Cited by 1
Xie, D., Guo, P., Zhao, Q., Gao, Y., Zhang, J., & Zhou, J. (2025) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266354743241216065502 · Cited by 1
“Tau is a protein that binds to microtubules and is mostly found in neurons in the brain [22].”
Passareiro, H., Erneux, C., & Nunez, J. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04956.x · Cited by 1
Chen, J., Wang, H., Ying, Y., Juarez, L., Binder, L. I., Ghanbari, H., & Murad, F. (1995) · Springer eBooks · doi:10.1007/978-1-4615-1903-4_25 · Cited by 1
Tau in Tauopathies That Leads to Cognitive Disorders and in Cancer
Huda, M. N., & Pan, C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.74025 · Cited by 1
“Among them, 53% phosphorylation sites of tau [45] are serine, 41% sites [41] are threonine while only 6% sites [5] are tyrosine [35–37].”
BackgroundTau, Tangles and Tauopathies: Insights from Drosophila Disease Models
Nisha, N., Pragati, Tandon, S., Aqsa, A., Aggarwal, P., & Sarkar, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_8 · Cited by 1
Delacourte, A., Sergeant, N., & Buée, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_20 · Cited by 1
Amyloid Fibril Formation of Natively Unfolded Proteins
Uversky, V. N., & Fink, A. L. (2008) · Wiley eBooks · doi:10.1002/9783527610754.md15 · Cited by 1
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Hartmann, A. M. (2003) · doi:10.5282/edoc.1675 · Cited by 1
Chapter 12 Cytoskeletal Abnormalities in Amyotrophic Lateral Sclerosis/Motor Neuron Disease
Robertson, J., & Julien, J. (2003) · Blue books of practical neurology · doi:10.1016/s1877-3419(09)70113-8 · Cited by 1
Komatsu, M. (1998) · Hepatology Research · doi:10.1016/s1386-6346(98)00060-6 · Cited by 1
The Carboxyterminal Region of Tubulin Regulates Its Assembly into Microtubules
Serrano, L. G., Maccioni, R. B., & Ávila, J. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38442.x · Cited by 1
Sparkman, D. R. (1992) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(92)90042-c · Cited by 1
A biochemical model for neurite outgrowth during brain development
Francon, J., Mareck, A., Lennon, A. M., Fellous, A., Nunez, J., Chantoux, F., & Osty, J. (1982) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19820207 · Cited by 1
Bhattacharya, A., Levy, S. F., LeBoeuf, A. C., Gaylord, M. A., Wilson, L., Singh, A. K., & Feinstein, S. C. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-339 · Cited by 1
“It binds directly to microtubules [9,10], and its ability to regulate microtubule dynamics [11-13] is itself tightly regulated by both alternative RNA splicing [14] and phosphorylation (for review, see [15]).”
BackgroundPurification and characterization of tubulin from the catfishHeteropneustes fossilis
Chaudhuri, A. (1986) · Journal of Biosciences · doi:10.1007/bf02716649 · Cited by 1
“No associated proteins corresponding to the γ protein of Mr 55,000–64,000 (Weingarten et al., 1975; Cleveland et al., 1977b), or to the high Mr MAPs (Mr 275,000–325,000) (Murphy and Borisy, 1975; Sloboda et al., 1975) found in MT protein from vertebrate brain (as shown by goat brain tubulin here)…”
Inhibitors of Microtubule Formation
Sternlicht, H. (1983) · Cancer treatment and research · doi:10.1007/978-1-4613-3891-8_4 · Cited by 1
Wischik, C. M., Harrington, C. R., & Mena, R. (1995) · International Review of Psychiatry · doi:10.3109/09540269509022985 · Cited by 1
Tau and α-Synuclein in Neurodegenerative Diseases
Giasson, B. I., Wilson, C., Trojanowski, J. Q., & Lee, V. M. ‐. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-006-3_7 · Cited by 1
Biochemie cytoplasmatischer Mikrotubuli
Mann, K. (1979) · Biologie in unserer Zeit · doi:10.1002/biuz.19790090105 · Cited by 1
DIRECT VISUALIZATION OF FLUORESCEIN-LABELED MICROTUBULES IN LIVING CELLS
KEITH, C. H., & Shelanski, M. L. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-615080-3.50040-9 · Cited by 1
``A world in miniature'': Charles Willson Peale's Philadelphia Museum and its audience, 1786--1827
Brigham, D. R. (1992) · Scholarly Commons (University of Pennsylvania) · Cited by 1
Dynamic Conformational Ensembles of Soluble Tau Encode Neuronal Toxicity Prior to AggregationPreprint
Georgescauld, F., Okekenwa, S., Boyd, T., Donahue, C., Quittot, N., Dickson, J. R., Fan, Z., Brady, S., Blackstone, C. D., Hyman, B. T., et al. (2026) · SSRN Electronic Journal · doi:10.64898/2026.01.26.701882 · Cited by 2
“MTs were polymerized from pig brain tubulin with or without Taxol and then mixed with Tau at a stoichiometry resembling the physiological ratio in axons (5 tubulin dimers to 1 Tau monomer) till equilibrium 52,53 .”
Kordower (1999) · doi:10.1002/1531-8249(199909)46:3
Chapter 9.13 Microtubular Proteins
Sullivan, K. F., & Wilson, L. (1983) · Journal of chromatography library · doi:10.1016/s0301-4770(08)61319-6
González, M. C. (2013) · Gredos (University of Salamanca) · doi:10.14201/gredos.122909
Brain Dysfunction Associated with Amyloid Fibrils and Other Aggregated Proteins
Giaccone, G., Salmona, M., Tagliavini, F., & Forloni, G. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch16
Fundamentals of Protein Folding
Uversky, V. N. (2014) · Wiley eBooks · doi:10.1002/9781118845363.ch1
“In vitro, tau binds to microtubules, promotes microtubule assembly, and affects the dynamic instability of individual microtubules (Cleveland et al., 1977a, b; Drechsel et al., 1992; Brandt and lee, 1993a, b). in situ, tau is highly enriched in the axons (Binder et al., 1985). in living cells and…”
BackgroundRichardson, E. E. (2011) · Human Biology
Protein Aggregates in Neurodegenerative Disorders
Giaccone, G., Salmona, M., Tagliavini, F., & Forloni, G. (2008) · Wiley eBooks · doi:10.1002/9783527610754.md09
Electron Spin Resonance Analysis of Cu(II) Coordination in Alzheimer's Disease-Related Peptides
Shin, B. (2011) · D-Scholarship@Pitt (University of Pittsburgh)
Conformational And Assembly Studies Of Two Tau Repeats: 2R and 3R
Koshiari, C. P. (2006) · University Libraries (University of Maryland)
Hall, K. (2011) · ORCA Online Research @Cardiff (Cardiff University)
The C‐terminal region of human tau protein with ability of filament formation
Chung, S. H. (1997) · Korean Journal of Biological Sciences · doi:10.1080/12265071.1997.9647372
Odajima, M. (1999) · Japanese Journal of Oral Biology · doi:10.2330/joralbiosci1965.41.596
Kanai, Y., Takemura, R., & Hirokawa, N. (1990) · Neuroscience Research Supplements · doi:10.1016/0921-8696(90)90688-y
“Among these proteins of neuronal tissues, high molecular mass microtubule-associated proteins (MAPs; MAP1 and MAP2) ~ and tau proteins are the major species, and recently several minor proteins have also been identified ( Cleveland et al., 1977a, b; Murphy and Borisy, 1975; Olmsted, 1986; Sloboda et al., 1975; Weingar…”
BackgroundInfluentialTau Gene Mutations in FTDP-17 Syndromes
Winton, M. J., Trojanowski, J. Q., & Lee, V. M. ‐. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_12
“However, tau is best characterized for its ability to bind to, stabilize and promote the polymerization of microtubules (MTs) (Cleveland et al., 1977; Weingarten et al., 1975).”
BackgroundUnderstanding and treating neurodegeneration: insights from the flies
Lu, B. (2005) · AGE · doi:10.1007/s11357-005-2917-y
“Tau is normally a highly soluble microtubule-binding protein enriched in axons ( Cleveland et al. 1977 ), but it becomes abnormally phosphorylated and insoluble in NFT (Greenberg and Davies 1990; Grundke-Iqbal et al. 1986; Lee et al. 1991).”
BackgroundPseudophosphorylation of tau modulates its function and induces AD-like changes
Sun, Q. (2009) · KU ScholarWorks (The University of Kansas)
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Agholme, L. (2012) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Mouse and stem cell models of frontotemporal dementia
Orr, M. E. (2012) · Montana State University ScholarWorks (Montana State University)
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Gozes, I. (2012) · Advances in predictive, preventive and personalised medicine · doi:10.1007/978-94-007-5866-7_5
Fontana, L. (2014) · Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) · doi:10.13130/fontana-laura_phd2014-01-24
“Tau belongs to the MAP (Microtuble Associated Protein) protein family and is involved in microtubule assembly and stabilisation upon phosphorylation by specific kinases, including MARK4 (MAP/Microtubule Affinity Regulating Kinase 4) (Cleveland et al., 1977).”
BackgroundMucci, N. J. (2015) · KU ScholarWorks (The University of Kansas)
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Lau, H. W. D. (2015)
Liu, C., Min, S., Wei, K., Dong, L. I. U., Dong, J., Luo, J., & Liu, X. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00483
Kakiuchi, S. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-615080-3.50016-1
New Small Molecule Drug Discovery for Alzheimer's Disease
Liu, K., Zhang, M., & Nagappan, G. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-6
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Koon, Y. L. (2018) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/73360
THE CYTOPLASM DURING INTERPHASE
Brachet, J. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-123370-9.50008-4
Micro-fabricated super-hydrophobic substrate for amyloid fibers characterization
Ricco, A. (2018) · King Abdullah University of Science and Technology Repository (King Abdullah University of Science and Technology) · doi:10.25781/kaust-cg55f
“Early discoveries on this field include the biochemistry of the Tau protein, thanks to its biochemical characterization [99]; the demonstration of its main place-of-action which is the axonal region (in contrast to that one that is mainly dendritic, called MAP2,) [100]; the cloning and isoforms characterization from m…”
BackgroundGenetics of Tau in Parkinsonism
Rademakers, R., Cruts, M., & Broeckhoven, C. V. (2007) · CRC Press eBooks · doi:10.3109/9781420019223-13
Constance, B. H. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/jk28-gv66
Developing Modified Peptide Nucleic Acids to Regulate Dysregulated Splicing
Enze, S. F., Xuan, T. L. Y., & Jun-Sheng, J. K. (2019) · Springer eBooks · doi:10.1007/978-981-32-9828-6_27
Gozes, I. (1985) · Elsevier eBooks · doi:10.1016/b978-0-08-031994-0.50032-3
Harilal, C. C. (2019) · DUT Open Scholar (Durban University of Technology) · doi:10.51415/10321/3608
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Lou, Y., Sun, S., & Tan, J. (2021) · E3S Web of Conferences · doi:10.1051/e3sconf/202130802012
Brelstaff, J. (2014) · UCL Discovery (University College London)
Characterisation of the ghrelinergic system in human models of neurodegenerative diseases
Carisi, M. C. (2021) · Cronfa (Swansea University) · doi:10.23889/suthesis.58915
Inhibitors of Microtubule Formation
Sternlicht, H. (1983) · Cancer treatment and research · doi:10.1007/978-94-011-8815-9_4
Sabnis, D. D. (1985) · Modern methods of plant analysis · doi:10.1007/978-3-642-82587-3_18
Ternaux, J. (2001) · Springer eBooks · doi:10.1007/978-3-662-06162-6_9
A biochemical and molecular analysis of functional differences between dystrophin and utrophin
Belanto, J. J. (2013) · University of Minnesota Digital Conservancy (University of Minnesota)
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Colautti, J., & Nagales, K. (2021) · The Meducator · doi:10.35493/medu.37.12
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. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.18.500499
Management of Alzheimer’s disease in the next ten years
Sani, I. (2023) · University of Toronto Medical Journal · doi:10.33137/utmj.v100i1.39014
Systematic review and PASS assisted prediction of selected phytoconstituents for Alzheimer’s disease
Sharma, I., Khurana, N., Muduli, S. K., & Sharma, N. (2023) · AIP conference proceedings · doi:10.1063/5.0163334
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Magalhães, A. L. D. A., Mas, J. J. D. M. P., Ferreira, R. M. S., Borges, D. G. V. M., Costa, A. C. P. D., & Araújo, G. L. M. D. (2023) · Brazilian Journal of Health Review · doi:10.34119/bjhrv6n5-562
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BackgroundCastellani, R. J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99651-8.00008-9
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Liu, W., Bai, Y., Qu, W., Zhang, X., Zhou, S., Luo, H., Zhu, M., Li, D., & Fang, X. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1752446
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Laumet, G. O. (2010) · theses.fr (ABES) · doi:10.70675/94126786zf990z488ezb471z5f1d5686766c
“Contrairement à leur nom, les DNF ne sont pas constituées de neurofilaments, composants physiologiques du cytosquelette de la cellule, mais d’une protéine appelée Tau déjà connue des spécialistes des tubules (Brion et al., 1986 ; Cleveland et al., 1977).”
BackgroundTau nucléaire : un acteur clé dans le stress neuronal
Sultan, A. (2010) · theses.fr (ABES) · doi:10.70675/98c582c8z1d31z4edazbbfaz92750b338b46
Sepulveda-Diaz, J. E. (2013) · theses.fr (ABES) · doi:10.70675/56c42bcbz41dfz432bzbb78z77110b373285
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Tardivel, M. (2017) · theses.fr (ABES) · doi:10.70675/0cfcd049z970ez4f2dz8417z195cfabdc00d
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Neves, J. F. (2019) · theses.fr (ABES) · doi:10.70675/6952dbaezebb9z4212z9c01z6ea8f2190a06
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Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau
Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc
Metadata
- Authors
- Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W.
- Affiliations
- Princeton University (US)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1977-10
- Volume
- 116
- Issue
- 2
- Pages
- 207-225
- ISSN
- 0022-2836 (ISSN-L)
- 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
- 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
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