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Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Open accessAbstract
The subcellular distribution of microtubules containing acetylated alpha-tubulin in mammalian cells in culture was analyzed with 6-11B-1, a monoclonal antibody specific for acetylated alpha-tubulin. Cultures of 3T3, HeLa, and PtK2 cells were grown on coverslips and observed by immunofluorescence microscopy after double-staining by 6-11B-1 and B-5-1-2, a monoclonal antibody specific for all alpha-tubulins. The antibody 6-11B-1 binds to primary cilia, centrioles, mitotic spindles, midbodies, and to subsets of cytoplasmic microtubules in 3T3 and HeLa cells, but not in PtK2 cells. These observations confirm that the acetylation of alpha-tubulin is a modification occurring in different microtubule structures and in a variety of eukaryotic cells. Some features of the acetylation of cytoplasmic microtubules of mammalian cells are also described here. First, acetylated alpha-tubulin is present in microtubules that, under depolymerizing conditions, are more stable than the majority of cytoplasmic microtubules. In addition to the specific microtubule frameworks already mentioned, cytoplasmic microtubules resistant to nocodazole or colchicine, but not cold-resistant microtubules, contain more acetylated alpha-tubulin than the rest of cellular microtubules. Second, the alpha-tubulin in all cytoplasmic microtubules of 3T3 and HeLa cells becomes acetylated in the presence of taxol, a drug that stabilizes microtubules. Third, acetylation and deacetylation of cytoplasmic microtubules are reversible in cells released from exposure to 0 degrees C or antimitotic drugs. Fourth, the epitope recognized by the antibody 6-11B-1 is not absolutely necessary for cell growth and division. This epitope is absent in PtK2 cells. The acetylation of alpha-tubulin could regulate the presence of microtubules in specific intracellular spaces by selective stabilization.
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“A characteristic feature of stable MTs is their curved appearance (Piperno et al., 1987; Friedman et al., 2010; Katrukha et al., 2017).”
From A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle (2023) · cites this paper as Piperno et al., 1987
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“acetylated tubulin (AcTub) (Fig. 5a), a marker for stable microtubules [29]”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [29]
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“Acetylation in interphase cells typically occurs on stable microtubules 37,38 , and stable microtubules were recently found to have a distinct, expanded lattice conformation 39 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [37]
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Taxol stabilizes microtubules in mouse fibroblast cells.
Schiff, P. B., & Horwitz, S. B. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1561 · Cited by 1,971
Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758
Self-citationTaxol binds to polymerized tubulin in vitro
Parness, J., & Horwitz, S. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.2.479 · Cited by 624
L’Hernault, S. W., & Rosenbaum, J. L. (1985) · Biochemistry · doi:10.1021/bi00323a034 · Cited by 497
Microtubule dynamics in interphase cells
Schulze, E., & Kirschner, M. (1986) · The Journal of cell biology · doi:10.1083/jcb.102.3.1020 · Cited by 335
L’Hernault, S. W., & Rosenbaum, J. L. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.258 · Cited by 255
A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters.
Jahn, R., SCHIEBLER, W., & Greengard, P. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.6.1684 · Cited by 244
Ledizet, M., & Piperno, G. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.1.13 · Cited by 204
Self-citationL’Hernault, S. W., & Rosenbaum, J. L. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.2.457 · Cited by 88
Linck, R. W., Amos, L., & Amos, W. B. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.126 · Cited by 85
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Items 401–500 of 872
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Florindo, C., Perdigão, J., Fesquet, D., Schiebel, E., Pines, J., & Tavares, Á. A. (2012) · Journal of Cell Science · doi:10.1242/jcs.097147 · Cited by 38
The effects of methylmercury on the cytoskeleton of murine embryonal carcinoma cells
Wasteneys, G. O., Cadrin, M., Reuhl, K. R., & Brown, D. L. (1988) · Cell Biology and Toxicology · doi:10.1007/bf00141286 · Cited by 37
Effects of Cold and Nocodazole Treatments on the Microtubular Systems of Paramecium in Interphase
Torres, A., & Delgado, P. (1989) · The Journal of Protozoology · doi:10.1111/j.1550-7408.1989.tb01056.x · Cited by 37
Posttranslational modifications of tubulin in cultured mouse brain neurons and astroglia
Eddé, B., Denoulet, P., de Néchaud, B., Koulakoff, A., Berwald‐Netter, Y., & Gros, F. (1989) · Biology of the Cell · doi:10.1016/0248-4900(89)90018-x · Cited by 37
Krupitza, G. (2009) · International Journal of Oncology · doi:10.3892/ijo_00000239 · Cited by 36
Coordination of microtubule acetylation and the actin cytoskeleton by formins
Fernández-Barrera, J., & Alonso, M. A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2855-3 · Cited by 35
Post-translational Acetylation Control of Cardiac Energy Metabolism
Ketema, E. B., & Lopaschuk, G. D. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.723996 · Cited by 37
Arce, C. A., Casale, C. H., & Barra, H. S. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06615.x · Cited by 35
Yedowitz, J. C., Kotsakis, A., Schlegel, E., & Blaho, J. A. (2005) · Journal of Virology · doi:10.1128/jvi.79.8.4730-4743.2005 · Cited by 35
Koivisto, L., Häkkinen, L., Matsumoto, K., McCulloch, C. A., Yamada, K. M., & Larjava, H. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.09.026 · Cited by 35
aPKC Phosphorylation of HDAC6 Results in Increased Deacetylation Activity
Du, Y., Seibenhener, M. L., Yan, J., Jiang, J., & Wooten, M. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123191 · Cited by 34
Age-related changes in microtubules in the guinea pig organ of Corti
Saha, S., & Slepecky, N. B. (2000) · Cell and Tissue Research · doi:10.1007/s004410050045 · Cited by 34
Cardiac Hypertrophic and Developmental Regulation of the β-Tubulin Multigene Family
Narishige, T., Blade, K. L., Ishibashi, Y., Nagai, T., Hamawaki, M., Menick, D. R., Kuppuswamy, D., & Cooper, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9692 · Cited by 34
Ojakian, G. K., & Schwimmer, R. (1992) · Journal of Cell Science · doi:10.1242/jcs.103.3.677 · Cited by 32
Claudin localization in cilia of the retinal pigment epithelium
Nishiyama, K., Sakaguchi, H., Hu, J. G., Bok, D., & Hollyfield, J. G. (2002) · The Anatomical Record · doi:10.1002/ar.10102 · Cited by 33
Yue, Y., Hotta, T., Higaki, T., Verhey, K. J., & Ohi, R. (2023) · Current Biology · doi:10.1016/j.cub.2023.07.062 · Cited by 39
Iuzzolino, A., Pellegrini, F. R., Rotili, D., Degrassi, F., & Trisciuoglio, D. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05227-x · Cited by 33
Ouyang, C., Mu, J., Lu, Q., Li, J., Zhu, H., Wang, Q., Zou, M., & Xie, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1707488 · Cited by 32
Hernández, J. M., Parato, J., Sharma, A., Soleilhac, J.-M., Qu, X., Tein, E., Sproul, A. A., Andrieux, A., Goldberg, Y., Moutin, M., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.926914 · Cited by 32
Zhou, J., Liu, M., Aneja, R., Chandra, R., & Joshi, H. C. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.08.032 · Cited by 33
Singh, H., Wray, N. H., Schappi, J. M., & Rasenick, M. M. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0016-x · Cited by 34
RetractedWarn, R. M., Harrison, A., Planques, V., Robert‐Nicoud, N., & Wehland, J. (1990) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970170106 · Cited by 33
Ouyang, C., Li, J., Zheng, X., Mu, J., Torres, G., Wang, Q., Zou, M., & Xie, Z. (2021) · Autophagy · doi:10.1080/15548627.2021.1911018 · Cited by 33
Silverman-Gavrila, R., Silverman‐Gavrila, L. B., Hou, G., Zhang, M., Charlton, M. P., & Bendeck, M. P. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.001 · Cited by 32
Effects of downregulated HDAC6 expression on the proliferation of lung cancer cells
Kamemura, K., Ito, A., Shimazu, T., Matsuyama, A., Maeda, S., Yao, T., Horinouchi, S., Khochbin, S., & Yoshida, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.092 · Cited by 32
Brown, A. S., Borgmann‐Winter, K. E., Hahn, C.-G., Role, L. W., Talmage, D. A., Gur, R. E., Chow, J. L., Prado, P., McCloskey, T., Bao, Y., et al. (2013) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2013.10.015 · Cited by 32
Characterization of the cold-adapted α-tubulin from the psychrophilic ciliate Euplotes focardii
Pucciarelli, S., & Miceli, C. (2002) · Extremophiles · doi:10.1007/s00792-002-0268-5 · Cited by 32
Gupta, R. P., & Abou-Donia, M. B. (1994) · Neurochemical Research · doi:10.1007/bf00967321 · Cited by 32
Sangrajrang, S., Denoulet, P., Laing, N. M., Tatoud, R., Millot, G., Calvo, F. M., Tew, K. D., & Fellous, A. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00472-3 · Cited by 32
Organization of microtubules in myelinating Schwann cells
Kidd, G. J., Andrews, S., & Trapp, B. D. (1994) · Journal of Neurocytology · doi:10.1007/bf01268092 · Cited by 32
Acetylated tubulin is found in all microtubule arrays of two species of pine
Gilmer, S., Clay, P., MacRae, T. H., & Fowke, L. C. (1999) · PROTOPLASMA · doi:10.1007/bf01282998 · Cited by 31
Kindlin1 regulates microtubule function to ensure normal mitosis
Patel, H., Stavrou, I., Shrestha, R. L., Draviam, V. M., Frame, M. C., & Brunton, V. G. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw009 · Cited by 31
Zfp423 Regulates Sonic Hedgehog Signaling via Primary Cilium Function
Hong, C., & Hamilton, B. A. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006357 · Cited by 32
Distribution of acetylated ?-tubulin in brain
Morales, M., & Fifkov�, E. (1991) · Cell and Tissue Research · doi:10.1007/bf00340864 · Cited by 31
African swine fever virus infection disrupts centrosome assembly and function
Jouvenet, N., & Wileman, T. E. (2005) · Journal of General Virology · doi:10.1099/vir.0.80623-0 · Cited by 31
MacRae, T. H., Langdon, C. M., & Freeman, J. A. (1991) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970180305 · Cited by 31
7 Axis Formation during Amphibian Oogenesis: Reevaluating the Role of the Cytoskeleton
Card, D. L. (1995) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)60568-2 · Cited by 31
Haakenson, J., & Zhang, X. M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14059514 · Cited by 31
Microtubule Plus-End Tracking Proteins and Their Roles in Cell Division
Ferreira, J. G. G., Pereira, A. L., & Maiato, H. (2014) · International review of cytology · doi:10.1016/b978-0-12-800255-1.00002-8 · Cited by 35
Involvement of Kif4a in Spindle Formation and Chromosome Segregation in Mouse Oocytes
Tang, F., Pan, M., Lu, Y., Wan, X., Zhang, Y., & Sun, S. (2018) · Aging and Disease · doi:10.14336/ad.2017.0901 · Cited by 30
Nicotinamide: a Class III HDACi Delays In Vitro Aging of Mouse Oocytes
Lee, A. R., Kishigami, S., Amano, T., Matsumoto, K., Wakayama, T., & Hosoi, Y. (2013) · Journal of Reproduction and Development · doi:10.1262/jrd.2012-171 · Cited by 30
Pittman, S. M., Geyp, M., Fraser, M. J., Ellem, K. A. O., Peaston, A. E., & Ireland, C. M. (1997) · Leukemia Research · doi:10.1016/s0145-2126(97)00038-6 · Cited by 30
Changes in Organization and Axonal Transport of Cytoskeletal Proteins During Regeneration
Tashiro, T., & Komiya, Y. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02051.x · Cited by 30
Liao, L.-S., Chen, Y., Mo, Z., Hou, C., Su, G., Liang, H., & Chen, Z. (2021) · Inorganic Chemistry Frontiers · doi:10.1039/d0qi01463j · Cited by 29
Tang, F., Pan, M., Wan, X., Lu, Y., Zhang, Y., & Sun, S. (2018) · Cell Division · doi:10.1186/s13008-018-0042-4 · Cited by 28
Asthana, J., Kuchibhatla, A., Jana, S. C., Ray, K., & Panda, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394353 · Cited by 29
Benbow, S. J., Cook, B. M., Reifert, J. R., Wozniak, K. M., Slusher, B. S., Littlefield, B. A., Wilson, L., Jordan, M. A., & Feinstein, S. C. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9580-6 · Cited by 29
Histone deacetylases as new therapy targets for platinum-resistant epithelial ovarian cancer
Pchejetski, D., Alfraidi, A., Sacco, K. A., Alshaker, H. A., Muhammad, A., & Monzon, L. (2015) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-015-2064-5 · Cited by 30
Eichwald, C., Ackermann, M., & Nibert, M. L. (2018) · Virology · doi:10.1016/j.virol.2018.02.009 · Cited by 29
Composition and organization of tubulin isoforms reveals a variety of axonemal models
Péchart, I., Kann, M., Levilliers, N., Bré, M., & Fouquet, J. (1999) · Biology of the Cell · doi:10.1016/s0248-4900(00)88532-9 · Cited by 29
Microtubule Motors in Establishment of Epithelial Cell PolarityPreprint
Kreitzer, G. E., & Myat, M. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a027896 · Cited by 29
Microtubule damage shapes the acetylation gradient
Andreu‐Carbó, M., Egoldt, C., Velluz, M., & Aumeier, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46379-5 · Cited by 31
Liu, X., Xiao, W., Wang, X., Li, Y., Han, J., & Li, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486910 · Cited by 28
Hexavalent chromium disrupts mitosis by stabilizing microtubules in Lens culinaris root tip cells
Eleftheriou, E. P., Adamakis, I. S., Fatsiou, M., & Panteris, E. (2012) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2012.01652.x · Cited by 28
Hwang, J. J., Kim, Y. S., Kim, M. J., Kim, D., Jeong, I. G., & Kim, C. (2010) · The Journal of Urology · doi:10.1016/j.juro.2010.07.035 · Cited by 28
SAS-1 Is a C2 Domain Protein Critical for Centriole Integrity in C. elegans
von Tobel, L., Mikeladze‐Dvali, T., Delattre, M., Balestra, F. R., Blanchoud, S., Finger, S., Knott, G. W., Müller‐Reichert, T., & Gönczy, P. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004777 · Cited by 28
Su, F., Bhattacharya, S., Abdisalaam, S., Mukherjee, S., Yajima, H., Yang, Y., Mishra, R., Kalayarasan, S., Ghose, S., Chen, D. J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6659 · Cited by 28
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Thiagarajan, D., Vedantham, S., Ananthakrishnan, R., Schmidt, A. M., & Ramasamy, R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.011 · Cited by 29
Deficiency of RITA results in multiple mitotic defects by affecting microtubule dynamics
Steinhäuser, K., Klöble, P., Kreis, N., Ritter, A., Friemel, A., Roth, S., Reichel, J. M., Michaelis, J., Rieger, M. A., Louwen, F., et al. (2016) · Oncogene · doi:10.1038/onc.2016.372 · Cited by 28
Psychiatric behaviors associated with cytoskeletal defects in radial neuronal migration
Fukuda, T., & Yanagi, S. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2539-4 · Cited by 31
Hage‐Sleiman, R., Herveau, S., Matera, E., Laurier, J.-F., & Dumontet, C. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-135 · Cited by 28
Knox, J., Mitchel, R. E. J., & Brown, D. L. (1993) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970240206 · Cited by 28
Dentler, W. L. (1987) · Elsevier eBooks · doi:10.1016/b978-0-08-091882-2.50016-6 · Cited by 28
HDAC8 functions in spindle assembly during mouse oocyte meiosis
Zhang, K., Lu, Y., Jiang, C., Liu, W., Shu, J., Chen, X., Shi, Y., Wang, E., Wang, L., Hu, Q., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15383 · Cited by 27
Gao, W., Meng, T., Shi, N., Hongmeng, Z., Yang, Z., & Qi, X. (2014) · Advanced Healthcare Materials · doi:10.1002/adhm.201400675 · Cited by 27
Histone deacetylase inhibition reduces cardiac connexin43 expression and gap junction communication
Xu, Q., Lin, X., Andrews, L. E., Patel, D., Lampe, P. D., & Veenstra, R. D. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00044 · Cited by 27
The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis
Kypri, E., Christodoulou, A., Maimaris, G., Lethan, M., Markaki, M., Lysandrou, C., Lederer, C. W., Tavernarakis, N., Geimer, S., Pedersen, L. B., et al. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1401-6 · Cited by 27
Calmodulin stabilization of kinetochore microtubule structure to the effect of nocodazole.
Sweet, S. C., Rogers, C. M., & Welsh, M. J. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.6.2243 · Cited by 27
Becker, I. C., Scheller, I., Wackerbarth, L. M., Beck, S., Heib, T., Aurbach, K., Manukjan, G., Gross, C., Spindler, M., Nagy, Z., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019001303 · Cited by 26
Schatten, H., & Sun, Q. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0817-2_4 · Cited by 27
Pustylnik, S., Fiorino, C., Nabavi, N., Zappitelli, T., da Silva, R., Aubin, J. E., & Harrison, R. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.481515 · Cited by 25
Arnette, C. R., Efimova, N., Zhu, X., Clark, G. J., & Kaverina, I. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0374 · Cited by 26
The emerging role of tubulin posttranslational modifications in cilia and ciliopathies
He, K., Ling, K., & Hu, J. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00111-0 · Cited by 25
Clayton, F. C., Kapetanovic, S., & Kotler, D. P. (2001) · AIDS · doi:10.1097/00002030-200101050-00019 · Cited by 26
Physarum plasmodia do contain cytoplasmic microtubules!
Salles-Passador, I., Moisand, A., Planques, V., & Wright, M. (1991) · Journal of Cell Science · doi:10.1242/jcs.100.3.509 · Cited by 26
Axons arrest the migration of Schwann cell precursors
Bhattacharyya, A., Brackenbury, R. W., & Ratner, N. (1994) · Development · doi:10.1242/dev.120.6.1411 · Cited by 26
Polo-like kinase 1 is essential for the first mitotic division in the mouse embryo
Baran, V., Solc, P., Kovaříková, V., Rehák, P., & Šutovský, P. (2013) · Molecular Reproduction and Development · doi:10.1002/mrd.22188 · Cited by 25
Pfister, A. S., Hadjihannas, M. V., Röhrig, W., Schambony, A., & Behrens, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.385393 · Cited by 28
Chawan, V., Yevate, S., Gajbhiye, R., Kulkarni, V., & Parte, P. P. (2020) · Bioscience Reports · doi:10.1042/bsr20202442 · Cited by 25
Li, X., Ju, J., Pan, Z., Wang, H., Wan, X., Pan, M., Xu, Y. Q., Sun, M., & Sun, S. (2020) · FEBS Journal · doi:10.1111/febs.15634 · Cited by 25
Jiang, Y., Wang, D., Zhang, C., Jiao, Y., Pu, Y., Cheng, R., Li, C., & Chen, Y. (2023) · Cell Proliferation · doi:10.1111/cpr.13419 · Cited by 24
FANCD2 influences replication fork processes and genome stability in response to clustered DSBs
Zhu, J., Su, F., Mukherjee, S., Mori, E., Hu, B., & Asaithamby, A. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1036210 · Cited by 25
Huang, T., Cheng, P., Chan, Y., Yeh, T., Young, Y., & Young, T. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.05.054 · Cited by 25
NEK2 phosphorylation antagonizes the microtubule stabilizing activity of centrobin
Park, J., & Rhee, K. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.12.106 · Cited by 25
Parker, W. H., Rhea, E. M., Qu, Z., Hecker, M. R., & May, J. M. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00076.2016 · Cited by 25
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Schimmack, S. J., Kneller, S., Dadabaeva, N., Bergmann, F., Taylor, A., Hackert, T., Werner, J., & Strobel, O. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164231 · Cited by 26
ATAT1 regulates forebrain development and stress-induced tubulin hyperacetylation
Li, L., Jayabal, S., Ghorbani, M., Legault, L., McGraw, S., Watt, A. J., & Yang, X. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03088-3 · Cited by 25
Colocalisation of acetylated microtubules, glial filaments, and mitochondria in astrocytes in vitro
Cambray-Deakin, M. A., Robson, S. J., & Burgoyne, R. D. (1988) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970100311 · Cited by 25
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Gallo, J., & Précigout, É. (1988) · Biology of the Cell · doi:10.1016/0248-4900(88)90073-1 · Cited by 25
Shah, R. M. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00166-0 · Cited by 25
Siegel, D. M., Bersie, S. M., Harris, P. S., Francesco, A. D., Armstrong, M., Reisdorph, N. A., Bernier, M., de Cabo, R., Fritz, K. S., & Ross, D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101840 · Cited by 24
Nephronophthisis: should we target cysts or fibrosis?
Slaats, G. G. G., Liliën, M. R., & Giles, R. H. (2015) · Pediatric Nephrology · doi:10.1007/s00467-015-3162-y · Cited by 26
Correa, L. M., & Miller, M. G. (2001) · Biology of Reproduction · doi:10.1095/biolreprod64.6.1644 · Cited by 24
Bielak-Żmijewska, A., Sikora-Polaczek, M., Nieznański, K., Mosieniak, G., Kolano, A., Maleszewski, M., Styrna, J., & Sikora, E. (2010) · Cell Proliferation · doi:10.1111/j.1365-2184.2010.00684.x · Cited by 24
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Violand, B. N., Schlittler, M. R., Lawson, C. Q., Kane, J. F., Siegel, N. R., Smith, C. E., Kolodziej, E. W., & Duffin, K. L. (1994) · Protein Science · doi:10.1002/pro.5560030712 · Cited by 24
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Metadata
- Authors
- Piperno, G., LeDizet, M., & Chang, X. J.
- Affiliations
- Rockefeller University (US)
- ORCID
- LeDizet, M
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1987-02-01
- Volume
- 104
- Issue
- 2
- Pages
- 289-302
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2114420
- OpenAlex
- W2155768517
- Cited by
- 873
- References
- 13
- Citations by year
- 2026: 15 · 2025: 18 · 2024: 23 · 2023: 27 · 2022: 19 · 2021: 30 · 2020: 24 · 2019: 29 · 2018: 32 · 2017: 28 · 2016: 28 · 2015: 34 · 2014: 33 · 2013: 34 · 2012: 36
- FWCI
- 15.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM28702)
- National Center for Research Resources (S07 RR077065)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- acetylated alpha-tubulin, alpha-tubulin acetylation, microtubules, cytoplasmic microtubules, primary cilia, centrioles, mitotic spindle, midbody, microtubule stabilization, paclitaxel, nocodazole, colchicine, deacetylation, 3T3 fibroblasts, HeLa cells, PtK2 cells
- MeSH terms
- Acetylation, Alkaloids, Animals, Cell Line, Cells, Cultured, Cold Temperature, Fluorescent Antibody Technique, HeLa Cells, Humans, Kinetics, Microtubules, Tubulin, Paclitaxel, Mice
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