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 501–600 of 916

The tangled biology of tau
Wilhelmsen, K. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7120 · Cited by 26
[16] Purification of tau protein from brain
Drubin, D. G., & Kirschner, M. W. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)34084-9 · Cited by 26
Self-citation
High molecular weight protein MAP 2 promoting microtubuleassembly in vitro is associated with microtubules in cells
KUZNETSOV, S., Rodionov, V., Bershadsky, A. D., Gelfand, V. I., & Rosenblat, V. A. (1980) · Cell Biology International Reports · doi:10.1016/0309-1651(80)90174-5 · Cited by 26
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
“Subsequent research unveiled its biochemical properties, including the ability of tau to become phosphorylated, and physiological functions as a microtubule stabiliser in neurons and other cell-types [107,108].”
Background
Therapeutic and diagnostic challenges for frontotemporal dementia
Dâ€TMAlton, S., & Lewis, J. M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00204 · Cited by 26
Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils
Savastano, A., Jaipuria, G., Andreas, L. B., Mandelkow�, E., & Zweckstetter, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-78161-0 · Cited by 26
Subchronic exposure to acrylamide caused behaviour disorders and related pathological and molecular changes in rat cerebellum
Liu, Y., Yan, D., Wang, Y., Zhang, X., Wang, N., Jiao, Y., & Yan, H. (2021) · Toxicology Letters · doi:10.1016/j.toxlet.2021.01.009 · Cited by 26
Dityrosine cross-linking and its potential roles in Alzheimer’s disease
Maina, M. B., Al‐Hilaly, Y. K., & Serpell, L. C. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1132670 · Cited by 27
“Tau is well-known for its role in stabilizing the microtubules through their nucleation and elongation (Cleveland et al., 1977).”
Background
Increased Intrathecal High-Avidity Anti-Tau Antibodies in Patients with Multiple Sclerosis
Fialová, L., Bartoš, A., Švarcová, J., & Malbohan, I. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027476 · Cited by 25
“It is primarly expressed in a body of the cell and then it is localized in axons [15,16].”
Background
Quantitative Analysis of Tau-Microtubule Interaction Using FRET
di Maio, I. L., Barbier, P., Allegro, D., Brault, C., & Peyrot, V. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150814697 · Cited by 25
“Tau is the major microtubule associated protein (MAP) in neuronal axons [1] that stabilizes microtubules and maintains neuronal process [2,3].”
Background
Tau-peptide fragments and their copper(II) complexes: Effects on Amyloid-β aggregation
Natale, G. D., Bellia, F., Sciacca, M. F. M., Campagna, T., & Pappalardo, G. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.09.061 · Cited by 25
The effect of a 94 GHz electromagnetic field on neuronal microtubules
Samsonov, A., & Popov, S. V. (2012) · Bioelectromagnetics · doi:10.1002/bem.21760 · Cited by 25
Tau Phosphorylation and Aggregation as a Therapeutic Target in Tauopathies
Badiola, N., Suárez‐Calvet, M., & Lleó, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237403 · Cited by 26
“Tau was first isolated in 1975 as a MAP that co-purified with tubulin and had the ability to promote microtubule assembly in the brain [64-66].”
Background
Effects of Tau and MAP2 on the interaction of maytansine with tubulin: inhibitory effect of maytansine on vinblastine-induced aggregation of tubulin.
Fellous, A., Luduena, R. F., Prasad, V., Jordan, M. A., Anderson, W., Ohayon, R., & Smith, P. T. (1985) · PubMed · Cited by 25
Assembly of nonneural microtubules in the absence of glycerol and microtubule-associated proteins
Doenges, K. H., Weissinger, M., Fritzsche, R., & Schroeter, D. (1979) · Biochemistry · doi:10.1021/bi00576a010 · Cited by 25
Targeting Protein Misfolding and Aggregation as a Therapeutic Perspective in Neurodegenerative Disorders
Sidoryk‐Wȩgrzynowicz, M., Adamiak, K., & Strużyńska, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212448 · Cited by 26
A mathematical model of multisite phosphorylation of tau protein
Stepanov, A. A., Karelina, T., Markevich, N. I., Demin, O. O., & Nicholas, T. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192519 · Cited by 26
Targeting Mitophagy in Alzheimer’s Disease
Jayatunga, D. P. W., Hone, E., Bharadwaj, P., Garg, M. L., Verdile, G., Guillemin, G. J., & Martins, R. N. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191258 · Cited by 25
Characteristics of Microtubules at the Different Stages of Neuronal Differentiation and Maturation
Meininger, V., & Binet, S. (1989) · International review of cytology · doi:10.1016/s0074-7696(08)60858-x · Cited by 24
Microtubule elongation along actin filaments induced by microtubule-associated protein 4 contributes to the formation of cellular protrusions
Doki, C., Nishida, K., Saito, S., Siga, M., Ogara, H., Kuramoto, A., Kuragano, M., Nozumi, M., Igarashi, M., Nakagawa, H., et al. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa046 · Cited by 23
Tau Protein as Therapeutic Target for Cancer? Focus on Glioblastoma
Hedna, R., Kovacic, H., Pagano, A., Peyrot, V., Robin, M., Devred, F., & Breuzard, G. (2022) · Cancers · doi:10.3390/cancers14215386 · Cited by 25
Granular expression of prolyl-peptidyl isomerase PIN1 is a constant and specific feature of Alzheimer’s disease pathology and is independent of tau, Aβ and TDP-43 pathology
Dakson, A., Yokota, O., Esiri, M. M., Bigio, E. H., Horan, M. A., Pendleton, N., Richardson, A. M. T., Neary, D., Snowden, J. S., Robinson, A., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0798-y · Cited by 22
“The microtubule-associated protein tau regulates the polymerization of tubulin and maintains microtubule stability in vitro [11].”
Background
A common antigenic motif recognized by naturally occurring human VH5–51/VL4–1 anti-tau antibodies with distinct functionalities
Apetri, A. C., Crespo, R., Juraszek, J., Pascual, G., Janson, R., Zhu, X., Zhang, H., Keogh, E. A., Holland, T., Wadia, J., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0543-z · Cited by 22
Dendritic and axonal distribution of the microtubule-associated proteins MAP2 and tau in the cerebellum of the nervous mutant mouse
Brion, J., Guilleminot, J., & Nunez, J. (1988) · Developmental Brain Research · doi:10.1016/0165-3806(88)90220-9 · Cited by 23
Mutants of chinese hamster ovary cells affected in two different microtubule-associated proteins. Genetic and biochemical studies.
Gupta, R. S., & Gupta, R. S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43490-9 · Cited by 23
Ablation of tau causes an olfactory deficit in a murine model of Parkinson’s disease
Beauchamp, L. C., Chan, J., Hung, L. W., Padman, B. S., Vella, L. J., Liu, X. M., Coleman, B. M., Bush, A. I., Lazarou, M., Hill, A. F., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0560-y · Cited by 22
The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins
Rieloff, E., & Skepö, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011058 · Cited by 21
“Two of the peptides are fragments from the neuroprotein tau, involved in stabilizing neuronal microtubules [32].”
Background
Binding of polyribonucleotides and polydeoxyribonucleotides to bovine brain microtubule protein: Age-dependent modulation via phosphorylation of high-molecular-weight microtubule-associated proteins and tau proteins
Schröder, H. C., Bernd, A., Zahn, R. K., & Müller, W. E. G. (1984) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(84)90178-7 · Cited by 22
Human protein tau represses DNA replication in vitro
Li, W., Wang, X. S., Qu, M., Liu, Y. M., & He, R. Q. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.08.014 · Cited by 23
Timing of Expression of r and Its Encoding mRNAs in the Developing Cerebral Neocortex and Cerebellum of the Mouse
Mangin, G., Couchie, D., Charrière‐Bertrand, C., & Nunez, J. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb07293.x · Cited by 22
“The T family is composed at adult stages of four or five closely related variants (50,000-70,000 daltons) (Cleveland et al., 1977a,b), whereas at immature stages, smaller (48,000 daltons) 7 immunologically related proteins are expressed (Mareck et al., 1980; Francon et al., 1982; Couchie and Nunez,…”
Background
High and Low Molecular Weight r Proteins Are Differentially Expressed from a Single Gene
Mavilia, C., Couchie, D., Mattéi, M., Nivez, M.-P., & Nunez, J. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03622.x · Cited by 22
Triiodothyronine (T3) induces neurite formation and increases synthesis of a protein related to MAP 1B in cultured cells of neuronal origin
Hargreaves, A. J., Yusta, B., Aranda, A., Ávila, J., & Pascual, A. (1988) · Developmental Brain Research · doi:10.1016/0165-3806(88)90092-2 · Cited by 22
Microtubule‐associated proteins from antarctic fishes
Detrich, H. W., Neighbors, B., Sloboda, R. D., & Williams, R. C. (1990) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970170305 · Cited by 22
Astrocytes in Neurodegenerative Diseases: A Perspective from Tauopathy and α-Synucleinopathy
Wang, P., & Ye, Y. (2021) · Life · doi:10.3390/life11090938 · Cited by 21
“Tau is a microtubule-binding protein predominantly expressed in neurons in the brain [10,11].”
Background
Organophosphorus Flame Retardants (OPFR): Neurotoxicity
Abou-Donia, M. B. (2016) · JOURNAL OF ENVIRONMENT AND HEALTH SCIENCE · doi:10.15436/2378-6841.16.022 · Cited by 21
Nanoscale lipid membrane mimetics in spin-labeling and electron paramagnetic resonance spectroscopy studies of protein structure and function
Georgieva, E. R. (2016) · Nanotechnology Reviews · doi:10.1515/ntrev-2016-0080 · Cited by 21
“Although the primary role of tau is microtubule binding and stabilizing [160, 161], it also interacts with biological membranes in the cell [162].”
Background
An evaluation of hydromethylthionine as a treatment option for Alzheimer’s disease
Hashweh, N., Bartochowski, Z., Khoury, R., & Grossberg, G. T. (2020) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2020.1719066 · Cited by 22
Looking for novel ways to treat the hallmarks of Alzheimer's disease
Stewart, A. J., Fox, A. W., Morimoto, B. H., & Gozes, I. (2007) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.16.8.1183 · Cited by 21
Expression of tau exon 8 in different species
Chen, W., Liu, W.-K., & Yen, S.-H. C. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90688-2 · Cited by 21
Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction
Siano, G., Falcicchia, C., Origlia, N., Cattaneo, A., & Primio, C. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810145 · Cited by 22
β-arrestin1 promotes tauopathy by transducing GPCR signaling, disrupting microtubules and autophagy
Woo, J. A., Yan, Y., Kee, T. R., Cazzaro, S., Percy, K. C. M., Wang, X., Liu, T., Liggett, S. B., & Kang, D. E. (2021) · Life Science Alliance · doi:10.26508/lsa.202101183 · Cited by 20
“…β-arrestin1-shRNA-GFP significantly restored synaptophysin immunoreactivity (Fig S4A and B). β-arrestin1 promotes the dissociation of tau from microtubules and inhibits tau-induced microtubule assembly Tau is a microtubule-associated protein that stabilizes microtubules (Cleveland et al, 1977).”
Background
Fucoidans inhibited tau interaction and cellular uptake
Jin, W., Lu, C., Zhu, Y., Zhao, J., Zhang, W., Wang, L., Linhardt, R. J., Wang, C., & Zhang, F. (2022) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2022.120176 · Cited by 19
Vesicular Axonal Transport is Modified In Vivo by Tau Deletion or Overexpression in Drosophila
Talmat-Amar, Y., Arribat, Y., & Parmentier, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030744 · Cited by 20
Axonal microtubules of crayfish and spiny lobster nerve cords are decorated with a heat-stable protein of high molecular weight
Warren, R. H. (1984) · Journal of Cell Science · doi:10.1242/jcs.71.1.1 · Cited by 20
Differential diagnosis of neurodegenerative diseases with special emphasis on Creutzfeldt-Jakob disease
Otto, M., & Wiltfang, J. (2003) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-2003-00238 · Cited by 20
Electrochemical biosensors for biometal-protein interactions in neurodegenerative diseases
Li, S., & Kerman, K. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113035 · Cited by 19
Increased 4R tau expression and behavioural changes in a novel MAPT-N296H genomic mouse model of tauopathy
Wobst, H. J., Denk, F., Oliver, P., Livieratos, A., Taylor, T. N., Knudsen, M. H., Bengoa-Vergniory, N., Bannerman, D., & Wade-Martins, R. (2017) · Scientific Reports · doi:10.1038/srep43198 · Cited by 17
An Analysis of the Neurological and Molecular Alterations Underlying the Pathogenesis of Alzheimer’s Disease
Vidal, C., & Li, Z. (2021) · Cells · doi:10.3390/cells10030546 · Cited by 20
Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases
Uversky, V. N. (2008) · Focus on structural biology · doi:10.1007/978-1-4020-9434-7_2 · Cited by 20
Interaction of Tubulin and Microtubule Proteins with Vanadate Oligomers
Lobert, S., Isern, N., Hennington, B. S., & Correia, J. J. (1994) · Biochemistry · doi:10.1021/bi00186a026 · Cited by 19
Redox modifications in synaptic components as biomarkers of cognitive status, in brain aging and disease
Muñoz, P., Ardiles, Á. O., Pérez-Espinosa, B., Núñez-Espinosa, C. A., Paula-Lima, A. C., González-Billault, C. E., & Espinosa‐Parrilla, Y. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111250 · Cited by 21
“Thus, axonal microtubules are modulated by Tau protein (Cleveland et al., 1977), while dendritic microtubules”
Background
The pathology of the neuronal cytoskeleton in Alzheimer's disease
Brion, J. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90047-h · Cited by 19
Binding between Prion Protein and Aβ Oligomers Contributes to the Pathogenesis of Alzheimer’s Disease
Kong, C., Xie, H., Gao, Z., Shao, M., Li, H., Shi, R., Cai, L., Gao, S., Sun, T., & Li, C. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00124-1 · Cited by 18
Synthetic RNA Modulators in Drug Discovery
Zamani, F., & Suzuki, T. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00154 · Cited by 20
Tubulin isotypes and their interaction with microtubule associated proteins
Cowan, N. J., Lewis, S. A., Gu, W., & Burgoyne, R. D. (1988) · PROTOPLASMA · doi:10.1007/bf01349346 · Cited by 18
Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
Takei, Y. (2000) · Neuroscience Research · doi:10.1016/s0168-0102(00)81476-5 · Cited by 18
Isolation of Microtubules and Microtubule Proteins
Ávila, J., Soares, H., Fanárraga, M. L., & Zabala, J. C. (2008) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0329s39 · Cited by 18
“This high-molecularweight tau contains four repeated motifs in its microtubule-binding domain; it is similar to the adult brain tau isoform but has an additional insertion of 254 amino acids in its amino-terminal region (Goedert et al., 1991; Couchie et al., 1992).”
Background
Expression of Tau protein and Tau mRNA in the cerebellum during axonal outgrowth
Couchie, D., Legay, F., Guilleminot, J., Lebargy, F., Brion, J., & Nunez, J. (1990) · Experimental Brain Research · doi:10.1007/bf00228800 · Cited by 18
Polymorphic Assemblies of Tubulin
Burton, P. R. (1981) · Springer eBooks · doi:10.1007/978-1-4684-8196-9_8 · 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
“Mechanistically, 3R and 4R tau regulate MT dynamics by (i) lowering the critical concentration of tubulin dimers required for MT assembly, (ii) moderately increasing MT growth rates, (iii) increasing the amount of time MTs spend in an attenuated or static state, and (iv) suppressing the frequency of MT catastrophes (a…”
Background
Pharmacological intervention in oxidative stress as a therapeutic target in neurological disorders
Sharma, S., Advani, D., Das, A., Malhotra, N., Khosla, A., Arora, V., Jha, A., Yadav, M., Ambasta, R. K., & Kumar, P. (2021) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgab064 · Cited by 19
Prion-Like Propagation Mechanisms in Tauopathies and Traumatic Brain Injury: Challenges and Prospects
Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 20
“Tau is a microtubule-associated protein that plays important roles in microtubule assembly and other microtubule-related functions [8,9].”
Background
Binding of Alz 50 depends on Phe8 in tau synthetic peptides and varies between native and denatured tau proteins.
Księżak-Reding, H., Leibowitz, R. L., Bowser, R., & Davies, P. (1995) · Brain Research · doi:10.1016/0006-8993(95)00785-o · Cited by 18
Can tau filaments be both physiologically beneficial and toxic?
King, M. E. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.019 · Cited by 17
Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant Tau.
Zhang, X., Zhang, Y., Liu, S., Bulloj, A., Tong, G., Zhang, Z., Liao, F., & Xu, H. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-7 · Cited by 17
“The tau proteins are normally expressed in neuronal and glial cytoplasm including cell bodies, neurites and axons, where they bind to and stabilize microtubules [7-9].”
Background
Functional Analysis of Microtubule-binding Domain of Bovine MAP4.
Katsuki, M., Tokuraku, K., Murofushi, H., & Kotani, S. (1999) · Cell Structure and Function · doi:10.1247/csf.24.337 · Cited by 17
The novel microtubule-associated protein MAP3 contributes to the in vitro assembly of brain microtubules.
Huber, G., Pehling, G., & Matus, A. I. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35928-8 · Cited by 17
Immunocytochemical localization of 205 kDa microtubule-associated protein (205 kDa MAP) in the guinea pig organ of Corti
Oshima, T., Okabe, S., & Hirokawa, N. (1992) · Brain Research · doi:10.1016/0006-8993(92)91081-o · Cited by 17
Microtubule‐binding property of microtubule‐associated protein 2 differs from that of microtubule‐associated protein 4 and tau
Tokuraku, K., Katsuki, M., Matui, T., Kuroya, T., & Kotani, S. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00710.x · Cited by 17
Identification of the 190kD microtubule-associated protein in cultured fibroblasts and its association with interphase and mitotic microtubules.
Kotani, S., Murofushi, H., Maékawa, S., Aizawa, H., Kaji, K., & Sakai, H. (1987) · Cell Structure and Function · doi:10.1247/csf.12.1 · Cited by 17
The use of mouse models to study cell-to-cell transmission of pathological tau
Narasimhan, S., & Lee, V. M. ‐. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.009 · 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
High-specificity antibodies and detection methods for quantifying phosphorylated tau from clinical samples
Arbaciauskaite, M., Yu, L., & Cho, Y. K. (2021) · Antibody Therapeutics · doi:10.1093/abt/tbab004 · Cited by 16
Characterization of fluorescently derivatized bovine tau protein and its localization and functions in cultured Chinese hamster ovary cells
Lu, Q., & Wood, J. G. (1993) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970250208 · Cited by 17
Immunohistochemical studies on the new type of astrocytic inclusions identified in a patient with brain malformation
Kato, S., Hirano, A., Umahara, T., Herz, F., Shioda, K., & Minagawa, M. (1992) · Acta Neuropathologica · doi:10.1007/bf00227674 · Cited by 16
“p romote the assembly and stability of microtubules [4, 6, 39].”
Background
Suppression of a conditional mutation in alpha-tubulin by overexpression of two checkpoint genes
Guénette, S. Y., Magendantz, M., & Solomon, F. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.3.1195 · Cited by 16
Physiology
Kaplan, H., Brewer, N. R., & Blair, W. H. (1983) · Elsevier eBooks · doi:10.1016/b978-0-12-262503-9.50018-9 · Cited by 16
Purification of a microtubule‐associated protein based on its preferential association with tubulin during microtubule initiation
Stearns, M. E., & Brown, D. L. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81285-5 · Cited by 16
Polymorphism of tubulin oligomers in the presence of microtubule-associated proteins. Implications in microtubule assembly
Carlier, M., Simon, C., & Pantaloni, D. (1984) · Biochemistry · doi:10.1021/bi00302a037 · Cited by 16
The in vitro assembly of microtubules from purified brain tubulin
Timasheff, S. N. (1979) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(79)90264-0 · Cited by 16
Tau Protein Biosensors in the Diagnosis of Neurodegenerative Diseases
Sadeghzadeh, J., Shahabi, P., Farhoudi, M., Kalan, A. E., Mobed, A., & Shahpasand, K. (2022) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.061 · Cited by 15
“Journal of The Electrochemical Society 2018;165(12):G3018.”
More is different: Reconstituting complexity in microtubule regulation
Lawrence, E. J., Chatterjee, S., & Žanić, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105398 · Cited by 19
Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS
Kanaan, N. M. (2024) · Cytoskeleton · doi:10.1002/cm.21820 · Cited by 15
“Tau was discovered in the mid-1970s, when it was co-purified with microtubules from brain tissue lysates (Cleveland et al., 1977a, 1977b; Weingarten et al., 1975; Witman et al., 1976).”
Background
Crry silencing alleviates Alzheimer’s disease injury by regulating neuroinflammatory cytokines and the complement system
Zhu, X., Ma, T., Liu, L., & Dai, W.-Z. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.332160 · Cited by 16
“As a microtubuleassociated protein, tau is usually expressed in neuronal axons and is implicated in the dissociation of microtubules by binding to the tubulin dimers that constitute microtubules (Cleveland et al., 1977).”
Background
Conditionally inducible tau mice – designing a better mouse model of neurodegenerative diseases
Janus, C. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00375.x · Cited by 16
“The microtubule polymerization, regulated by repeat domains on the C-terminal, ensures axonal transport (Brandt & Lee 1993a,b; Cleveland et al. 1977a,b).”
Background
FRET and FRAP imaging: Approaches to characterise tau and stathmin interactions with microtubules in cells
Nouar, R., Devred, F., Breuzard, G., & Peyrot, V. (2013) · Biology of the Cell · doi:10.1111/boc.201200060 · Cited by 15
“Until the end of the 1970s, two categories of MAPs have been characterised: a first class including proteins with a molecular weight higher than 300,000 Da (Murphy and Borisy, 1975) and a second one with proteins between 55,000 and 75,000 Da (Weingarten et al., 1975; Cleveland et al., 1977).”
Background
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
Inhibition of microtubule formation by DNA
Vater, W., Müller, H., & Unger, E. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90764-7 · 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 Changes of Cytoskeletal Proteins in Plasma of Acrylamide-Induced Rats
Yi, C., Xie, K., Song, F., Yu, L.-H., Zhao, X., Li, G., & Yu, S. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9079-x · Cited by 14
“axonal elongation and maintenance [37, 38].”
Microtubule and MAPs
Devred, F., Barbier, P., Lafitte, D., Landrieu, I., Lippens, G. M., & Peyrot, V. (2010) · Methods in cell biology · doi:10.1016/s0091-679x(10)95023-1 · Cited by 18
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
“Although mammalian tau is encoded by a single gene (14), it exhibits high heterogeneity ranging from 45-65 kDa for the low molecular weight (LWM) isoforms (15) to 90-115 kDa for the high molecular weight (HMW) isoforms (16,17).”
Background
Tissue culture study on neuronal migration in the rat cerebral cortex: effects of low dose radiation
Matsushita, K., Yoshioka, H., Fushiki, S., Hirai, K., Kihara, M., Kadono, N., Hasegawa, K., Goma, H., & Sawada, T. (1997) · Brain and Development · doi:10.1016/s0387-7604(97)00057-0 · Cited by 14
“In addition, the neural cell adhesion molecule (N-CAM) [12] and L1 [13] are well known as cell adhesion molecules, and neurofilaments [14,15], tau protein [16,17], and MAP2 (microtubule associated protein 2) [18,19] as cytoskeletal elements.”
Background
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
Distinct mode of microtubule‐associated protein 2 expression in the neuroblastoma/glioma cell line 108CC15/NG108‐15
Beaman‐Hall, C. M., & Vallano, M. L. (1993) · Journal of Neurobiology · doi:10.1002/neu.480241105 · Cited by 14
Microtubule‐Associated‐Protein MAP1 is not Implicated in the Polymerization of Microtubules
Villasanté, A., de la TORRE, J., Manso-Martínez, R., & Ávila, J. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06126.x · Cited by 14
The effect of estramustine derivatives on microtubule assembly in vitro depends on the charge of the substituent
Fridén, B., Rutberg, M., Deinum, J., & Wallin, M. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90281-9 · Cited by 14
Purification of a thermostable high molecular weight factor promoting tubulin polymerization
Kuznetsov, S., Rodionov, V., Gelfand, V. I., & Rosenblat, V. A. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)81025-4 · Cited by 14
Physiopathological mechanisms underlying Alzheimer’s disease: a narrative review
Engelhardt, E., Resende, E. D. P. F., & Gomes, K. B. (2024) · Dementia & Neuropsychologia · doi:10.1590/1980-5764-dn-2024-vr01 · Cited by 20
Human MAP Tau Based Targeted Cytolytic Fusion Proteins
Akinrinmade, O. A., Jordaan, S., Hristodorov, D., Mladenov, R., Mungra, N., Chetty, S., & Barth, S. (2017) · Biomedicines · doi:10.3390/biomedicines5030036 · Cited by 13
“by co-purification with tubulin [30], MAP tau was re ognized as p otein factor essenti l for microtu ule assembly [31].”
BackgroundMethod

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