In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510

Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain

Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559

Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A.

Yoshida, M., Kijima, M., Akita, M., & Beppu, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44885-x · Cited by 1,856

Acetylation of Histones and Transcription-Related Factors

Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824

High-Resolution Model of the Microtubule

Nogales, E., Whittaker, M., Milligan, R. A., & Downing, K. H. (1999) · Cell · doi:10.1016/s0092-8674(00)80961-7 · Cited by 1,200

Acetylation: a regulatory modification to rival phosphorylation?

Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155

Signaling to Chromatin through Histone Modifications

Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989

A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases

Richon, V. M., Emiliani, S., Verdin, E., Webb, Y., Breslow, R., Rifkind, R. A., & Marks, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3003 · Cited by 914

Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.

Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873

HDAC6 inhibition results in tau acetylation and modulates tau phosphorylation and degradation in oligodendrocytes

Noack, M., Leyk, J., & Richter‐Landsberg, C. (2014) · Glia · doi:10.1002/glia.22624 · Cited by 77

HDAC6 Regulates Epidermal Growth Factor Receptor (EGFR) Endocytic Trafficking and Degradation in Renal Epithelial Cells

Liu, W., Fan, L. X., Zhou, X., Sweeney, W. E., Avner, E. D., & Li, X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049418 · Cited by 78

Substrate and inhibitor specificity of class 1 and class 2 histone deacetylases

Hildmann, C., Wegener, D., Riester, D., Hempel, R., Schober, A., Merana, J., Giurato, L., Guccione, S., Nielsen, T. K., Ficner, R., et al. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.01.030 · Cited by 78

Corepressor Recruitment by Agonist-Bound Nuclear Receptors

White, J. H., Fernandes, I., Mader, S., & Yang, X. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68004-6 · Cited by 85

The NIMA-family kinase Nek3 regulates microtubule acetylation in neurons

Chang, J., Baloh, R. H., & Milbrandt, J. (2009) · Journal of Cell Science · doi:10.1242/jcs.048975 · Cited by 75

The emerging role of lysine acetylation of non-nuclear proteins

Close, P., Creppe, C., Gillard, M., Ladang, A., Chapelle, J.-P., Nguyen, L., & Chariot, A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0252-7 · Cited by 79

Interplay Between HDAC6 and Its Interacting Partners: Essential Roles in the Aggresome-Autophagy Pathway and Neurodegenerative Diseases

Yan, J. (2014) · DNA and Cell Biology · doi:10.1089/dna.2013.2300 · Cited by 77

Combining association mapping and transcriptomics identify HD2B histone deacetylase as a genetic factor associated with seed dormancy in Arabidopsis thaliana

Yano, R., Takebayashi, Y., Nambara, E., Kamiya, Y., & Seo, M. (2013) · The Plant Journal · doi:10.1111/tpj.12167 · Cited by 79

Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress

Watabe, M., & Nakaki, T. (2011) · Journal of Cell Science · doi:10.1242/jcs.081778 · Cited by 77

Inhibitors to understand molecular mechanisms of NAD+-dependent deacetylases (sirtuins)

Lawson, M. K., Uciechowska, U., Schemies, J., Rumpf, T., Jung, M., & Sippl, W. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.06.003 · Cited by 76

Microtubule Acetylation Through HDAC6 Inhibition Results in Increased Transfection Efficiency

Vaughan, E. E., Geiger, R., Miller, A. M., Loh-Marley, P. L., Suzuki, T., Miyata, N., & Dean, D. A. (2008) · Molecular Therapy · doi:10.1038/mt.2008.190 · Cited by 77

Posttranslational modification and beyond: interplay between histone deacetylase 6 and heat-shock protein 90

Liu, P., Xiao, J., Wang, Y., Song, X., Huang, L., Ren, Z., Kitazato, K., & Wang, Y. (2021) · Molecular Medicine · doi:10.1186/s10020-021-00375-3 · Cited by 79

Acetylated α-tubulin is reduced in individuals with poor sperm motility

Bhagwat, S., Dalvi, V., Chandrasekhar, D., Matthew, T., Acharya, K. K., Gajbhiye, R., Kulkarni, V., Sonawane, S., Ghosalkar, M. N., & Parte, P. P. (2013) · Fertility and Sterility · doi:10.1016/j.fertnstert.2013.09.016 · Cited by 75

HDAC6 and SIRT2 promote bladder cancer cell migration and invasion by targeting cortactin

Chen, W. (2011) · Oncology Reports · doi:10.3892/or.2011.1553 · Cited by 75

Impact of protein acetylation in inflammatory lung diseases

Ito, K., Charron, C. E., & Adcock, I. M. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.06.009 · Cited by 77

Histone Deacetylases Control Neurogenesis in Embryonic Brain by Inhibition of BMP2/4 Signaling

Shaked-Rabi, M., Weissmueller, K., Svoboda, H., Hortschansky, P., Nishino, N., Wölfl, S., & Tucker, K. L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002668 · Cited by 77

HDAC 6 at the Intersection of Neuroprotection and Neurodegeneration

d’Ydewalle, C. V. O., Bogaert, E., & Bosch, L. V. D. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01347.x · Cited by 75

C6-ceramide synergistically potentiates the anti-tumor effects of histone deacetylase inhibitors via AKT dephosphorylation and α-tubulin hyperacetylation both in vitro and in vivo

Zhu, Q.-Y., Wang, Z., Ji, C., Cheng, L., Yang, Y.-L., Ren, J., Jin, Y.-H., Wang, Q.-J., Gu, X.-J., Bi, Z.-G., et al. (2011) · Cell Death and Disease · doi:10.1038/cddis.2010.96 · Cited by 71

HDAC6 and RhoA are novel players in Abeta-driven disruption of neuronal polarity

Tsushima, H., Emanuele, M., Polenghi, A., Esposito, A., Vassalli, M., Barberis, A., Difato, F., & Chieregatti, E. (2015) · Nature Communications · doi:10.1038/ncomms8781 · Cited by 71

Histone Deacetylase Inhibitors: The Epigenetic Therapeutics That Repress Hypoxia‐Inducible Factors

Chen, S., & Sang, N. (2010) · BioMed Research International · doi:10.1155/2011/197946 · Cited by 73

F11L-Mediated Inhibition of RhoA-mDia Signaling Stimulates Microtubule Dynamics during Vaccinia Virus Infection

Arakawa, Y., Cordeiro, J. V., & Way, M. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.04.007 · Cited by 72

Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class I HDAC profiles between epithelial and stromal cells.

Waltregny, D., North, B. J., Mellaert, F. V., de Leval, J., Verdin, E. M., & CASTRONOVO, V. (2004) · PubMed · doi:10.4081/897 · Cited by 71

Increased acetylation of Peroxiredoxin1 by HDAC6 inhibition leads to recovery of Aβ-induced impaired axonal transport

Choi, H., Kim, H. J., Kim, J., Kim, S., Yang, J., Lee, W., Park, Y., Hyeon, S. J., Lee, D.-S., Ryu, H., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0164-1 · Cited by 71

Synthesis and Anticancer Activity of All Known (−)-Agelastatin Alkaloids

Han, S., Siegel, D. S., Morrison, K. C., Hergenrother, P. J., & Movassaghi, M. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo4020112 · Cited by 70

Valproic acid: how it works. Or not

Lagace, D. C., O'Brien, W. T., Gurvich, N., Nachtigal, M. W., & Klein, P. S. (2004) · Clinical Neuroscience Research · doi:10.1016/j.cnr.2004.09.013 · Cited by 72

HDAC6 Regulates Mutant SOD1 Aggregation through Two SMIR Motifs and Tubulin Acetylation

Gál, J., Chen, J., Barnett, K. R., Yang, L., Brumley, E., & Zhu, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431957 · Cited by 70

PTEN activation through K163 acetylation by inhibiting HDAC6 contributes to tumour inhibition

Meng, Z., Jia, L.-F., & Gan, Y. (2015) · Oncogene · doi:10.1038/onc.2015.293 · Cited by 68

HDAC6 inhibition protects cardiomyocytes against doxorubicin-induced acute damage by improving α-tubulin acetylation

Song, R. Y., Yang, Y., Han, L., Wang, G., Huang, Y. C., Xue, W., Wang, Y., Yao, L., & Zhu, Y. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.10.007 · Cited by 70

Apoptosis Induction byHistone Deacetylase Inhibitors in Cancer Cells: Role of Ku70

Gong, P., Wang, Y., & Jing, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071601 · Cited by 71

Therapeutic effects of histone deacetylase inhibitors in a murine asthma model

Ren, Y., Su, X., Kong, L., Li, M., Zhao, X., Yu, N., & Kang, J. (2016) · Inflammation Research · doi:10.1007/s00011-016-0984-4 · Cited by 68

A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth

Kaliszczak, M., Trousil, S., Åberg, O., Perumal, M., Nguyen, Q.-D., & Aboagye, E. O. (2013) · British Journal of Cancer · doi:10.1038/bjc.2012.576 · Cited by 66

Subcellular Localization of Class II HDAs in Arabidopsis thaliana: Nucleocytoplasmic Shuttling of HDA15 Is Driven by Light

Alinsug, M. V., Chen, F. F., Luo, M., Tai, R., Jiang, L., & Wu, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030846 · Cited by 71

Differential protein acetylation induced by novel histone deacetylase inhibitors

Glaser, K. B., Li, J., Pease, L. J., Staver, M. J., Marcotte, P. A., Guo, J., Frey, R. R., Garland, R. B., Heyman, H. R., Wada, C. K., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.082 · Cited by 67

Function of Histone Deacetylase 6 as a Cofactor of Nuclear Receptor Coregulator LCoR

Palijan, A., Fernandes, I., Bastien, Y., Tang, L., Verway, M., Kourelis, M., Tavera-Mendoza, L. E., Li, Z., Bourdeau, V., Mader, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045526 · Cited by 65

HDAC6 controls the kinetics of platelet activation

Sadoul, K., Wang, J., Diagouraga, B., Vitte, A.-L., Buchou, T., Rossini, T., Polack, B., Xi, X., Matthias, P., & Khochbin, S. (2012) · Blood · doi:10.1182/blood-2012-05-428011 · Cited by 67

African swine fever virus-cell interactions: From virus entry to cell survival

Alonso, C., Galindo, I., Cuesta-Geijo, M. Á., Cabezas, M., Hernáez, B., & Muñoz-Moreno, R. (2012) · Virus Research · doi:10.1016/j.virusres.2012.12.006 · Cited by 66

Regulation of SIRT2-dependent α-tubulin deacetylation by cellular NAD levels

Skoge, R. H., Dölle, C., & Ziegler, M. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.04.011 · Cited by 65

Novel histone deacetylase inhibitors: cyclic tetrapeptide with trifluoromethyl and pentafluoroethyl ketones

Jose, B., Oniki, Y., Kato, T., Nishino, N., Sumida, Y., & Yoshida, M. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.08.016 · Cited by 65

Infection with Replication-deficient Adenovirus Induces Changes in the Dynamic Instability of Host Cell Microtubules

Warren, J. C., Rutkowski, A., & Cassimeris, L. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0850 · Cited by 65

HDAC11 deficiency disrupts oncogene-induced hematopoiesis in myeloproliferative neoplasms

Yue, L., Sharma, V., Horvat, N. P., Akuffo, A. A., Beatty, M. S., Murdun, C., Colin, C., Billington, J. M. R., Goodheart, W. E., Sahakian, E., et al. (2020) · Blood · doi:10.1182/blood.2019895326 · Cited by 67

Microtubule stability, Golgi organization, and transport flux require dystonin-a2–MAP1B interaction

Ryan, S. D., Bhanot, K., Ferrier, A., Repentigny, Y. D., Chu, A., Blais, A., & Kothary, R. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201107096 · Cited by 64

Histone deacetylase inhibitors that target tubulin

Schemies, J., Sippl, W., & Jung, M. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.01.040 · Cited by 66

Identification of novel modulators of mitochondrial function by a genome-wide RNAi screen in Drosophila melanogasterPreprint

Chen, J., Shi, X., Padmanabhan, R., Wang, Q., Wu, Z., Stevenson, S. C., Hild, M., Garza, D., & Li, H. (2007) · Genome Research · doi:10.1101/gr.6940108 · Cited by 65

A selective histone deacetylase-6 inhibitor improves BDNF trafficking in hippocampal neurons from Mecp2 knockout mice: implications for Rett syndrome

Xu, X., Kozikowski, A. P., & Pozzo‐Miller, L. D. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00068 · Cited by 63

A novel Hsp90 inhibitor AT13387 induces senescence in EBV-positive nasopharyngeal carcinoma cells and suppresses tumor formation

Chan, K. C., Ting, C. M., Chan, P. S., Lo, M. C., Lo, K. W., Curry, J. E., Smyth, T., Lee, A. W. M., Ng, W. T., Tsao, G. S., et al. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-128 · Cited by 63

Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells

Li, D., Sun, X., Zhang, L., Yan, B., Xie, S., Liu, R., Liu, M., & Zhou, J. (2014) · Protein & Cell · doi:10.1007/s13238-013-0010-3 · Cited by 63

Altered microtubule dynamics and vesicular transport in mouse and human MeCP2-deficient astrocytes

Delépine, C., Méziane, H., Nectoux, J., Opitz, M., Smith, A. B., Ballatore, C., Saillour, Y., Griscelli, A. B., Chang, Q., Williams, E. C., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv464 · Cited by 60

Comparative proteomics of primitive hematopoietic cell populations reveals differences in expression of proteins regulating motility

Evans, C. A. (2004) · Blood · doi:10.1182/blood-2003-09-3294 · Cited by 63

Elongator – an emerging role in neurological disorders

Nguyen, L., Humbert, S., Saudou, F., & Chariot, A. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.11.002 · Cited by 61

Early axonal loss accompanied by impaired endocytosis, abnormal axonal transport, and decreased microtubule stability occur in the model of Krabbe's disease

Teixeira, C. A., Miranda, C. O., Sousa, V., Santos, T. E., Malheiro, A. R., Solomon, M. A., Maegawa, G. H. B., Brites, P., & Sousa, M. M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.02.012 · Cited by 62

4-Hydroxybenzoic acid derivatives as HDAC6-specific inhibitors modulating microtubular structure and HSP90α chaperone activity against prostate cancer

Seidel, C., Schnekenburger, M., Mazumder, A., Teiten, M.-H., Kirsch, G., Dicato, M. A., & Diederich, M. F. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.11.005 · Cited by 62

Selective HDAC6 inhibition prevents TNF-α-induced lung endothelial cell barrier disruption and endotoxin-induced pulmonary edema

Yu, J., Ma, Z., Shetty, S., Ma, M., & Fu, J. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00051.2016 · Cited by 61

2,4‑Di‑tert‑butylphenol, a potential HDAC6 inhibitor, induces senescence and mitotic catastrophe in human gastric adenocarcinoma AGS cells

Song, Y. W., Lim, Y., & Cho, S. K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.02.003 · Cited by 62

Revisiting Histone Deacetylases in Human Tumorigenesis: The Paradigm of Urothelial Bladder Cancer

Giannopoulou, A. F., Velentzas, A. D., Konstantakou, E. G., Avgeris, M., Katarachia, S. A., Papandreou, N. C., Kalavros, N., Mpakou, V., Iconomidou, V. A., Anastasiadou, E., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061291 · Cited by 62

OSU-HDAC42, a Histone Deacetylase Inhibitor, Blocks Prostate Tumor Progression in the Transgenic Adenocarcinoma of the Mouse Prostate Model

Sargeant, A. M., Rengel, R. C., Kulp, S. K., Klein, R. D., Clinton, S. K., Wang, Y.-C., & Chen, C. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0203 · Cited by 61

Antiproliferative and proapoptotic activities of 4-hydroxybenzoic acid-based inhibitors of histone deacetylases

Seidel, C., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.09.026 · Cited by 60

Erucin, the Major Isothiocyanate in Arugula (Eruca sativa), Inhibits Proliferation of MCF7 Tumor Cells by Suppressing Microtubule Dynamics

Azarenko, O., Jordan, M. A., & Wilson, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100599 · Cited by 64

The subcellular localization and activity of cortactin is regulated by acetylation and interaction with Keap1

Ito, A., Shimazu, T., Maeda, S., Shah, A. A., Tsunoda, T., Iemura, S., Natsume, T., Suzuki, T., Motohashi, H., Yamamoto, M. P., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aad0667 · Cited by 60

Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation

Carmona, B., Marinho, H. S., Matos, C. L., Nolasco, S., & Soares, H. (2023) · Biology · doi:10.3390/biology12040561 · Cited by 64

Furry promotes acetylation of microtubules in the mitotic spindle by inhibition of SIRT2 tubulin deacetylase

Nagai, T., Ikeda, M., Chiba, S., Kanno, S., & Mizuno, K. (2013) · Journal of Cell Science · doi:10.1242/jcs.127209 · Cited by 59

Multiple Histone Deacetylases and the CREB-binding Protein Regulate Pre-mRNA 3′-End Processing

Shimazu, T., Horinouchi, S., & Yoshida, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609745200 · Cited by 58

A novel orally active HDAC6 inhibitor T-518 shows a therapeutic potential for Alzheimer’s disease and tauopathy in mice

Onishi, T., Maeda, R., Terada, M., Sato, S., Fujii, T., Ito, M., Hashikami, K., Kawamoto, T., & Tanaka, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-94923-w · Cited by 61

The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation

Valera, M.-S., de Armas‐Rillo, L., González, J. B., Ziglio, S., Batisse, J., Dubois, N., Marrero‐Hernández, S., Borel, S., García-Expósito, L., Biard‐Piechaczyk, M., et al. (2015) · Retrovirology · doi:10.1186/s12977-015-0181-5 · Cited by 62

Hdac-Mediated Control of Endochondral and Intramembranous Ossification

Westendorf, J. J., Bradley, E. W., & McGee‐Lawrence, M. E. (2011) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v21.i2.10 · Cited by 61

Staphylococcus aureus–induced endothelial permeability and inflammation are mediated by microtubule destabilization

Karki, P., Ke, Y., Tian, Y., Ohmura, T., Sitikov, A. S., Sarich, N. A., Montgomery, C. P., & Birukova, A. A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004030 · Cited by 58

Microtubules are more stable and more highly acetylated in ethanol-treated hepatic cells

Kannarkat, G. T., Tuma, D. J., & Tuma, P. L. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.07.007 · Cited by 58

Primary cilium: an elaborate structure that blocks cell division?

Ke, Y., & Yang, W. (2014) · Gene · doi:10.1016/j.gene.2014.06.050 · Cited by 64

Increased gene expression of histone deacetylases in patients with Philadelphia-negative chronic myeloproliferative neoplasms

Skov, V., Larsen, T. S., Thomassen, M., Riley, C. H., Jensen, M. K., Bjerrum, O. W., Kruse, T. A., & Hasselbalch, H. C. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.597905 · Cited by 57

Direct Binding with Histone Deacetylase 6 Mediates the Reversible Recruitment of Parkin to the Centrosome

Jiang, Q., Ren, Y., & Feng, J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2860-08.2008 · Cited by 59

Tubacin suppresses proliferation and induces apoptosis of acute lymphoblastic leukemia cells

Aldana-Masangkay, G. I., Rodrı́guez-González, A., Lin, T. L., Ikeda, A. K., Hsieh, Y., Kim, Y., Lomenick, B., Okemoto, K., Landaw, E. M., Wang, D., et al. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.570821 · Cited by 56

Explorative Study on Isoform-Selective Histone Deacetylase Inhibitors

Suzuki, T. (2009) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.57.897 · Cited by 57

c-Cbl and Cbl-b Act Redundantly to Protect Osteoclasts from Apoptosis and to Displace HDAC6 from β-Tubulin, Stabilizing Microtubules and Podosomes

Purev, E., Neff, L., Horne, W. C., & Baron, R. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0248 · Cited by 59

Uropathogenic Escherichia coli Invades Host Cells via an HDAC6-modulated Microtubule-dependent Pathway

Dhakal, B. K., & Mulvey, M. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805010200 · Cited by 56

Microtubule Dynamic Instability Controls Podosome Patterning in Osteoclasts through EB1, Cortactin, and Src

Duplan, M. B., Zalli, D., Stephens, S., Zenger, S., Neff, L., Oelkers, J. M., Lai, F. P. L., Horne, W. C., Rottner, K., & Baron, R. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00578-13 · Cited by 59

Cancer Cells Acquire Mitotic Drug Resistance Properties Through Beta I-Tubulin Mutations and Alterations in the Expression of Beta-Tubulin Isotypes

Cheung, C. H. A., Wu, S.-Y., Lee, T., Chang, C.-Y., Wu, J., Hsieh, H., & Chang, J.-Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012564 · Cited by 56

Purification of tubulin with controlled post-translational modifications by polymerization–depolymerization cycles

Souphron, J., Bodakuntla, S., Jijumon, A. S., Lakisic, G., Gautreau, A. M., Janke, C., & Magiera, M. M. (2019) · Nature Protocols · doi:10.1038/s41596-019-0153-7 · Cited by 66

HDAC6 modulates myofibril stiffness and diastolic function of the heart

Lin, Y., Major, J. L., Liebner, T., Hourani, Z., Travers, J. G., Wennersten, S. A., Haefner, K. R., Cavasin, M. A., Wilson, C. E., Jeong, M. Y., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci148333 · Cited by 55

Panobinostat (LBH589)-induced acetylation of tubulin impairs megakaryocyte maturation and platelet formation

Iancu‐Rubin, C., Gajzer, D. C., Mosoyan, G., Feller, F. M., Mascarenhas, J. O., & Hoffman, R. (2012) · Experimental Hematology · doi:10.1016/j.exphem.2012.02.004 · Cited by 55

SIRT2 regulates ciliogenesis and contributes to abnormal centrosome amplification caused by loss of polycystin-1

Zhou, X., Fan, L. X., Li, K., Ramchandran, R., Calvet, J. P., & Li, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt556 · Cited by 55

The Centrosome in Normal and Transformed Cells

Wang, Q., Hirohashi, Y., Furuuchi, K., Zhao, H., Liu, Q., Zhang, H., Murali, R., Berezov, A., Du, X., Li, B., et al. (2004) · DNA and Cell Biology · doi:10.1089/1044549041562276 · Cited by 54

MeCP2 deficiency is associated with reduced levels of tubulin acetylation and can be restored using HDAC6 inhibitors

Gold, W. A., Lacina, T. A., Cantrill, L. C., & Christodoulou, J. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1202-x · Cited by 53

Novel Class IIa-Selective Histone Deacetylase Inhibitors Discovered Using an in Silico Virtual Screening Approach

Hsu, K., Liu, C., Lin, T. E., Hsieh, J.-H., Sung, T.-Y., Tseng, H.-J., Yang, J., & Huang, W. (2017) · Scientific Reports · doi:10.1038/s41598-017-03417-1 · Cited by 54

Microtubule-severing protein Katanin regulates neuromuscular junction development and dendritic elaboration in Drosophila

Mao, C., Xiong, Y., Xiong, Z., Wang, Q., Zhang, Y., & Jin, S. (2014) · Development · doi:10.1242/dev.097774 · Cited by 54

The growing landscape of tubulin acetylation: lysine 40 and many more

Sadoul, K., & Khochbin, S. (2016) · Biochemical Journal · doi:10.1042/bcj20160172 · Cited by 53

HDAC6 controls innate immune and autophagy responses to TLR-mediated signalling by the intracellular bacteria Listeria monocytogenes

Moreno-Gonzalo, O., Ramírez‐Huesca, M., Blas‐Rus, N., Cibrián, D., Sáiz, M. L., Jorge, I., Camafeita, E., Vázquez, J., & Sánchez‐Madrid, F. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006799 · Cited by 53

Circovirus Transport Proceeds via Direct Interaction of the Cytoplasmic Dynein IC1 Subunit with the Viral Capsid Protein

Cao, J., Lin, C., Wang, H., Wang, L., Zhou, N., Jin, Y., Liao, M., & Zhou, J. (2014) · Journal of Virology · doi:10.1128/jvi.03117-14 · Cited by 54

p97/valosin‐containing protein (VCP) is highly modulated by phosphorylation and acetylation

Konya, C., Kato, N., Maeda, R., Yasuda, K., Higashimae, N., Noguchi, M., Koike, M., Kimura, Y., Ohizumi, H., Hori, S., et al. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01286.x · Cited by 51

HDAC6: Physiological function and its selective inhibitors for cancer treatment

Yang, P. (2013) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2013.v7.6.233 · Cited by 56

Critical role of the HDAC6–cortactin axis in human megakaryocyte maturation leading to a proplatelet-formation defect

Messaoudi, K., Ali, A., Ishaq, R., Palazzo, A., Sliwa, D., Bluteau, O., Souquère, S., Muller, D., Diop, M. K., Rameau, P., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01690-2 · Cited by 52

Inhibitors of histone deacetylases induce tumor-selective cytotoxicity through modulating Aurora-A kinase

Park, J., Jong, H.-S., Kim, S. G., Jung, Y., Lee, K., Lee, J., Kim, D., Bang, Y., & Kim, T. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0260-8 · Cited by 52

Computational Studies on the Histone Deacetylases and the Design of Selective Histone Deacetylase Inhibitors

Wang, D. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609788085287 · Cited by 51

Dido3-dependent HDAC6 targeting controls cilium size

de Diego, A. S., Guerrero, A. A., Martínez‐A, C., & van Wely, K. H. M. (2014) · Nature Communications · doi:10.1038/ncomms4500 · Cited by 49

Alpha-tubulin acetyltransferase/MEC-17 regulates cancer cell migration and invasion through epithelial–mesenchymal transition suppression and cell polarity disruption

Lee, C.-C., Cheng, Y.-C., Chang, C.-Y., Lin, C.-M., & Chang, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-35392-6 · Cited by 51

Anti-cancer effects of naturally derived compounds targeting histone deacetylase 6-related pathways

Lernoux, M., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.11.004 · Cited by 49

Regulation of SV40 large T-antigen stability by reversible acetylation

Shimazu, T., Komatsu, Y., Nakayama, K. I., Fukazawa, H., Horinouchi, S., & Yoshida, M. (2006) · Oncogene · doi:10.1038/sj.onc.1209731 · Cited by 49

HDAC 6 mediates HIV ‐1 tat‐induced proinflammatory responses by regulating MAPK‐NF ‐kappa B/AP ‐1 pathways in astrocytes

Youn, G. S., Ju, S. M., Choi, S. Y., & Park, J. (2015) · Glia · doi:10.1002/glia.22865 · Cited by 49

Inhibition of HDAC6 Modifies Tau Inclusion Body Formation and Impairs Autophagic Clearance

Leyk, J., Goldbaum, O., Noack, M., & Richter‐Landsberg, C. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0460-y · Cited by 49

Transcriptional regulation of human osteopontin promoter by histone deacetylase inhibitor, trichostatin A in cervical cancer cells

Sharma, P., Kumar, S., & Kundu, G. C. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-178 · Cited by 49

Clostridium difficile Toxin A Decreases Acetylation of Tubulin, Leading to Microtubule Depolymerization through Activation of Histone Deacetylase 6, and This Mediates Acute Inflammation

Nam, H. J., Kang, J. K., Kim, S.-K., Ahn, K. J., Seok, H., Park, S. J., Chang, J., Pothoulakis, C., LaMont, J. T., & Kim, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.162743 · Cited by 49

Reduced microtubule acetylation in cystic fibrosis epithelial cells

Rymut, S. M., Harker, A. J., Corey, D. A., Burgess, J. D., Sun, H., Clancy, J. P., & Kelley, T. J. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00411.2012 · Cited by 48

Inhibition of HDAC6 Deacetylase Activity Increases Its Binding with Microtubules and Suppresses Microtubule Dynamic Instability in MCF-7 Cells

Asthana, J., Kapoor, S., Mohan, R., & Panda, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.489328 · Cited by 123

Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6

Zilberman, Y., Ballestrem, C., Carramusa, L., Mazitschek, R., Khochbin, S., & Bershadsky, A. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046813 · Cited by 250

HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo

Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740

HDAC6 is a microtubule-associated deacetylase

Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403

Stimulating Movement by Deacetylation

(2002) · Science Signaling · doi:10.1126/scisignal.1342002tw188