{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T20:55:44Z","timestamp":1791665744082,"version":"4.3.4"},"reference-count":326,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2020,10,5]],"date-time":"2020-10-05T00:00:00Z","timestamp":1601856000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Neurons are particularly susceptible to microtubule (MT) defects and deregulation of the MT cytoskeleton is considered to be a common insult during the pathogenesis of neurodegenerative disorders. Evidence that dysfunctions in the MT system have a direct role in neurodegeneration comes from findings that several forms of neurodegenerative diseases are associated with changes in genes encoding tubulins, the structural units of MTs, MT-associated proteins (MAPs), or additional factors such as MT modifying enzymes which modulating tubulin post-translational modifications (PTMs) regulate MT functions and dynamics. Efforts to use MT-targeting therapeutic agents for the treatment of neurodegenerative diseases are underway. Many of these agents have provided several benefits when tested on both in vitro and in vivo neurodegenerative model systems. Currently, the most frequently addressed therapeutic interventions include drugs that modulate MT stability or that target tubulin PTMs, such as tubulin acetylation. The purpose of this review is to provide an update on the relevance of MT dysfunctions to the process of neurodegeneration and briefly discuss advances in the use of MT-targeting drugs for the treatment of neurodegenerative disorders.<\/jats:p>","DOI":"10.3390\/ijms21197354","type":"journal-article","created":{"date-parts":[[2020,10,5]],"date-time":"2020-10-05T08:35:57Z","timestamp":1601886957000},"page":"7354","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":132,"title":["Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases"],"prefix":"10.3390","volume":"21","author":[{"given":"Antonella","family":"Sferra","sequence":"first","affiliation":[{"name":"Unit of Neuromuscular and Neurodegenerative Disorders, Genetics and Rare Diseases Research Division, Bambino Ges\u00f9 Children\u2019s Hospital, IRCCS, 00146 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5612-821X","authenticated-orcid":false,"given":"Francesco","family":"Nicita","sequence":"additional","affiliation":[{"name":"Unit of Neuromuscular and Neurodegenerative Disorders, Genetics and Rare Diseases Research Division, Bambino Ges\u00f9 Children\u2019s Hospital, IRCCS, 00146 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9276-4590","authenticated-orcid":false,"given":"Enrico","family":"Bertini","sequence":"additional","affiliation":[{"name":"Unit of Neuromuscular and Neurodegenerative Disorders, Genetics and Rare Diseases Research Division, Bambino Ges\u00f9 Children\u2019s Hospital, IRCCS, 00146 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,10,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"511","DOI":"10.3389\/fpls.2014.00511","article-title":"The role of dynamic instability in microtubule organization","volume":"5","author":"Horio","year":"2014","journal-title":"Front. Plant Sci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ceb.2010.08.008","article-title":"Microtubule tip-interacting proteins: A view from both ends","volume":"23","author":"Jiang","year":"2011","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3515","DOI":"10.1091\/mbc.e16-03-0199","article-title":"GDP-to-GTP exchange on the microtubule end can contribute to the frequency of catastrophe","volume":"27","author":"Piedra","year":"2016","journal-title":"Mol. Biol. Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/324621a0","article-title":"Microtubule dynamics","volume":"324","author":"Kirschner","year":"1986","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1083\/jcb.107.4.1437","article-title":"Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies","volume":"107","author":"Walker","year":"1988","journal-title":"J. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1038\/nature08908","article-title":"Cell mechanics and the cytoskeleton","volume":"463","author":"Fletcher","year":"2010","journal-title":"Nature"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e1800194","DOI":"10.1002\/bies.201800194","article-title":"Microtubule plus end dynamics\u2014Do we know how microtubules grow? Cells boost microtubule growth by promoting distinct structural transitions at growing microtubule ends","volume":"41","author":"Wittmann","year":"2019","journal-title":"Bioessays"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"6746","DOI":"10.1038\/srep06746","article-title":"Molecular evolution and functional divergence of tubulin superfamily in the fungal tree of life","volume":"4","author":"Zhao","year":"2014","journal-title":"Sci. Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/B978-0-12-407699-0.00002-9","article-title":"A hypothesis on the origin and evolution of tubulin","volume":"302","year":"2013","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Bittermann, E., Abdelhamed, Z., Liegel, R.P., Menke, C., Timms, A., Beier, D.R., and Stottmann, R.W. (2019). Differential requirements of tubulin genes in mammalian forebrain development. PLoS Genet., 15.","DOI":"10.1371\/journal.pgen.1008243"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1016\/0006-2952(94)90537-1","article-title":"Interaction of ustiloxin A with bovine brain tubulin","volume":"47","author":"Roach","year":"1994","journal-title":"Biochem. Pharmacol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1021\/bi962724m","article-title":"Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified beta-tubulin isotypes","volume":"36","author":"Derry","year":"1997","journal-title":"Biochemistry"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/sj.embor.embor716","article-title":"The two alpha-tubulin isotypes in budding yeast have opposing effects on microtubule dynamics in vitro","volume":"4","author":"Bode","year":"2003","journal-title":"EMBO Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3564","DOI":"10.1091\/mbc.e17-02-0124","article-title":"Tubulin isoform composition tunes microtubule dynamics","volume":"28","author":"Vemu","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"ref_15","unstructured":"Fulton, C., and Simpson, P. (1976). Selective synthesis and utilization of flagellar tubulin. The multi-tubulin hypothesis. Cell Motility, Cold Spring Harbor Laboratory Press."},{"key":"ref_16","first-page":"3722","article-title":"Genetically essential and nonessential alpha-tubulin genes specify functionally interchangeable proteins","volume":"6","author":"Schatz","year":"1986","journal-title":"Mol. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1083\/jcb.105.4.1707","article-title":"In vivo microtubules are copolymers of available beta-tubulin isotypes: Localization of each of six vertebrate beta-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens","volume":"105","author":"Lopata","year":"1987","journal-title":"J. Cell Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/cm.970250104","article-title":"Beta IV is the major beta-tubulin isotype in bovine cilia","volume":"25","author":"Renthal","year":"1993","journal-title":"Cell Motil. Cytoskelet."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.cub.2017.02.039","article-title":"Cell-specific \u03b1-tubulin isotype regulates ciliary microtubule ultrastructure, intraflagellar transport, and extracellular vesicle biology","volume":"27","author":"Silva","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/0378-1119(86)90333-1","article-title":"Differential expression of several neurospecific beta-tubulin mRNAs in the mouse brain during development","volume":"50","author":"Denoulet","year":"1986","journal-title":"Gene"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1083\/jcb.109.2.663","article-title":"Differential utilization of beta-tubulin isotypes in differentiating neurites","volume":"109","author":"Joshi","year":"1989","journal-title":"J. Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1083\/jcb.103.5.1903","article-title":"The mammalian beta-tubulin repertoire: Hematopoietic expression of a novel, heterologous beta-tubulin isotype","volume":"103","author":"Wang","year":"1986","journal-title":"J. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/S0960-9822(01)00153-1","article-title":"A lineage-restricted and divergent beta-tubulin isoform is essential for the biogenesis, structure and function of blood platelets","volume":"11","author":"Schwer","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S0960-9822(01)00150-6","article-title":"Axoneme-specific beta-tubulin specialization: A conserved C-terminal motif specifies the central pair","volume":"11","author":"Nielsen","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1083\/jcb.111.3.1009","article-title":"Two drosophila beta tubulin isoforms are not functionally equivalent","volume":"111","author":"Hoyle","year":"1990","journal-title":"J. Cell Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1242\/dev.117.3.977","article-title":"A functionally specialized alpha-tubulin is required for oocyte meiosis and cleavage mitoses in Drosophila","volume":"117","author":"Matthews","year":"1993","journal-title":"Development"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1016\/j.celrep.2018.07.029","article-title":"Neuronal-specific TUBB3 is not required for normal neuronal function but is essential for timely axon regeneration","volume":"24","author":"Latremoliere","year":"2018","journal-title":"Cell Rep."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.devcel.2018.08.014","article-title":"Human \u03b2-tubulin isotypes can regulate microtubule protofilament number and stability","volume":"47","author":"Ti","year":"2018","journal-title":"Dev. Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1083\/jcb.82.1.278","article-title":"Organization of neuronal microtubules in the nematode Caenorhabditis elegans","volume":"82","author":"Chalfie","year":"1979","journal-title":"J. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1126\/science.2646709","article-title":"Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons","volume":"243","author":"Chalfie","year":"1989","journal-title":"Science"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1101\/gad.3.6.870","article-title":"mec-7 is a beta-tubulin gene required for the production of 15-protofilament microtubules in Caenorhabditis elegans","volume":"3","author":"Savage","year":"1989","journal-title":"Genes Dev."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/j.cub.2012.03.066","article-title":"Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization","volume":"22","author":"Topalidou","year":"2012","journal-title":"Curr. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"R351","DOI":"10.1016\/j.cub.2014.03.032","article-title":"Post-translational modifications of tubulin","volume":"24","author":"Magiera","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/ncb2920","article-title":"Regulation of microtubule motors by tubulin isotypes and post-translational modifications","volume":"16","author":"Sirajuddin","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.201305041","article-title":"Tubulin glycylases and glutamylases have distinct functions in stabilization and motility of ependymal cilia","volume":"202","author":"Rocha","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/ncb3091","article-title":"Lineage specificity of primary cilia in the mouse embryo","volume":"17","author":"Bangs","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"12917","DOI":"10.1038\/srep12917","article-title":"Deacetylation of \u03b1-tubulin and cortactin is required for HDAC6 to trigger ciliary disassembly","volume":"5","author":"Ran","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1242\/jcs.185983","article-title":"Ttll9-\/-mice sperm flagella show shortening of doublet 7, reduction of doublet 5 polyglutamylation and a stall in beating","volume":"129","author":"Konno","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1242\/jcs.199471","article-title":"The tubulin code at a glance","volume":"130","author":"Gadadhar","year":"2017","journal-title":"J. Cell Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.neuron.2015.05.046","article-title":"Building the Neuronal Microtubule Cytoskeleton","volume":"87","author":"Kapitein","year":"2015","journal-title":"Neuron"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nrn2631","article-title":"Microtubule assembly, organization and dynamics in axons and dendrites","volume":"10","author":"Conde","year":"2009","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1016\/0306-4522(82)90125-7","article-title":"The cytoskeleton in myelinated axons: A freeze-etch replica study","volume":"7","author":"Tsukita","year":"1982","journal-title":"Neuroscience"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2818","DOI":"10.1523\/JNEUROSCI.14-05-02818.1994","article-title":"Changes in microtubule number and length during axon differentiation","volume":"14","author":"Yu","year":"1994","journal-title":"J. Neurosci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/s13064-019-0134-0","article-title":"The model of local axon homeostasis\u2014Explaining the role and regulation of microtubule bundles in axon maintenance and pathology","volume":"14","author":"Hahn","year":"2019","journal-title":"Neural Dev."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1111\/jnc.12621","article-title":"Microtubules in neurons as information carriers","volume":"129","author":"Dent","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/cm.21286","article-title":"Stability properties of neuronal microtubules","volume":"73","author":"Baas","year":"2016","journal-title":"Cytoskeleton (Hoboken)"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1002\/dneu.20818","article-title":"Hooks and comets: The story of microtubule polarity orientation in the neuron","volume":"71","author":"Baas","year":"2011","journal-title":"Dev. Neurobiol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"5778","DOI":"10.1523\/JNEUROSCI.1382-04.2004","article-title":"Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules","volume":"24","author":"Karabay","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"3012","DOI":"10.1242\/dev.153171","article-title":"Microtubule organization, dynamics and functions in differentiated cells","volume":"144","author":"Muroyama","year":"2017","journal-title":"Development"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/j.neuron.2012.10.008","article-title":"Golgi outposts shape dendrite morphology by functioning as sites of acentrosomal microtubule nucleation in neurons","volume":"76","author":"Jan","year":"2012","journal-title":"Neuron"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"12187","DOI":"10.1038\/ncomms12187","article-title":"Non-centrosomal nucleation mediated by augmin organizes microtubules in post-mitotic neurons and controls axonal microtubule polarity","volume":"7","author":"Freixo","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/j.celrep.2018.06.093","article-title":"The HAUS complex is a key regulator of non-centrosomal microtubule organization during neuronal development","volume":"24","author":"Chazeau","year":"2018","journal-title":"Cell Rep."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4122","DOI":"10.1091\/mbc.e07-10-1079","article-title":"Microtubules have opposite orientation in axons and dendrites of Drosophila neurons","volume":"19","author":"Stone","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1523\/JNEUROSCI.2430-15.2016","article-title":"Dendrites in vitro and in vivo contain microtubules of opposite polarity and axon formation correlates with uniform plus-end-out microtubule orientation","volume":"36","author":"Yau","year":"2016","journal-title":"J. Neurosci."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"e10140","DOI":"10.7554\/eLife.10140","article-title":"Interplay between kinesin-1 and cortical dynein during axonal outgrowth and microtubule organization in Drosophila neurons","volume":"4","author":"Winding","year":"2015","journal-title":"eLife"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3271","DOI":"10.1091\/mbc.e17-06-0380","article-title":"Polarity sorting of axonal microtubules: A computational study","volume":"28","author":"Craig","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2210","DOI":"10.1016\/j.celrep.2017.05.064","article-title":"Cytoplasmic dynein transports axonal microtubules in a polarity-sorting manner","volume":"19","author":"Rao","year":"2017","journal-title":"Cell Rep."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1242\/jcs.110.19.2373","article-title":"Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientation","volume":"110","author":"Sharp","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1083\/jcb.136.3.659","article-title":"Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells","volume":"136","author":"Yu","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"5782","DOI":"10.1523\/JNEUROSCI.20-15-05782.2000","article-title":"Depletion of a microtubule-associated motor protein induces the loss of dendritic identity","volume":"20","author":"Yu","year":"2000","journal-title":"J. Neurosci."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"R660","DOI":"10.1016\/j.cub.2014.05.033","article-title":"Connecting the cytoskeleton to the endoplasmic reticulum and Golgi","volume":"24","author":"Gurel","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0166-2236(89)90124-0","article-title":"The basis of polarity in neurons","volume":"12","author":"Black","year":"1989","journal-title":"Trends Neurosci."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1083\/jcb.115.2.345","article-title":"Microtubule behavior in the growth cones of living neurons during axon elongation","volume":"115","author":"Tanaka","year":"1991","journal-title":"J. Cell Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"3595","DOI":"10.1242\/jcs.042309","article-title":"Cytoskeletal dynamics in growth-cone steering","volume":"122","author":"Geraldo","year":"2009","journal-title":"J. Cell Sci."},{"key":"ref_65","first-page":"531","article-title":"Class III beta-tubulin isotype: A key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology","volume":"19","author":"Katsetos","year":"2004","journal-title":"J. Child Neurol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1002\/dvg.20325","article-title":"A transgenic mouse class-III beta tubulin reporter using yellow fluorescent protein","volume":"45","author":"Liu","year":"2007","journal-title":"Genesis"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1242\/jcs.103.3.643","article-title":"Differential regulation of beta III and other tubulin genes during peripheral and central neuron development","volume":"103","author":"Jiang","year":"1992","journal-title":"J. Cell Sci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"11358","DOI":"10.1073\/pnas.91.24.11358","article-title":"Microtubule dynamics in vitro are regulated by the tubulin isotype composition","volume":"91","author":"Panda","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1016\/S0021-9258(19)40087-2","article-title":"Increased microtubule assembly in bovine brain tubulin lacking the type III isotype of beta-tubulin","volume":"265","author":"Banerjee","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"4462","DOI":"10.1093\/hmg\/ddq377","article-title":"Mutations in the neuronal \u00df-tubulin subunit TUBB3 result in malformation of cortical development and neuronal migration defects","volume":"19","author":"Poirier","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.cell.2009.12.011","article-title":"Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance","volume":"140","author":"Tischfield","year":"2010","journal-title":"Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2729","DOI":"10.3892\/mmr.2014.3047","article-title":"A family with axonal sensorimotor polyneuropathy with TUBB3 mutation","volume":"11","author":"Hong","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"2329048X16665758","DOI":"10.1177\/2329048X16665758","article-title":"mutation in the tubulin-encoding TUBB3 gene causes complex cortical malformations and unilateral hypohidrosis","volume":"3","author":"Fukumura","year":"2016","journal-title":"Child Neurol. Open."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1002\/ajmg.a.37362","article-title":"Two unique TUBB3 mutations cause both CFEOM3 and malformations of cortical development","volume":"170","author":"Whitman","year":"2016","journal-title":"Am. J. Med. Genet. A"},{"key":"ref_75","first-page":"2","article-title":"Mutations in tubulin genes are frequent causes of various foetal malformations of cortical development including microlissencephaly","volume":"25","author":"Poirier","year":"2014","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"65","DOI":"10.5698\/1535-7597-15.2.65","article-title":"Tubulinopathies and their brain malformation syndromes: Every TUB on its own bottom","volume":"15","author":"Chang","year":"2015","journal-title":"Epilepsy Curr."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.ejmg.2018.07.012","article-title":"Tubulin genes and malformations of cortical development","volume":"61","author":"Romaniello","year":"2018","journal-title":"Eur. J. Med. Genet."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1016\/j.celrep.2012.11.017","article-title":"Mutations in the \u03b2-tubulin gene TUBB5 cause microcephaly with structural brain abnormalities","volume":"2","author":"Breuss","year":"2012","journal-title":"Cell Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"5147","DOI":"10.1093\/hmg\/ddu238","article-title":"TUBB5 and its disease-associated mutations influence the terminal differentiation and dendritic spine densities of cerebral cortical neurons","volume":"23","author":"Ngo","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1016\/j.ajhg.2015.10.014","article-title":"Mutations in either TUBB or MAPRE2 cause circumferential skin creases Kunze type","volume":"97","author":"Isrie","year":"2015","journal-title":"Am. J. Hum. Genet."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1111\/cge.13232","article-title":"Intrafamiliar clinical variability of circumferential skin creases Kunze type caused by a novel heterozygous mutation of N-terminal TUBB gene","volume":"93","author":"Dentici","year":"2018","journal-title":"Clin. Genet."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.gene.2019.02.002","article-title":"Spectrum of clinical heterogeneity of \u03b2-tubulin TUBB5 gene mutations","volume":"695","author":"Madrigal","year":"2019","journal-title":"Gene"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Sferra, A., Petrini, S., Bellacchio, E., Nicita, F., Scibelli, F., Dentici, M.L., Alfieri, P., Cestra, G., Bertini, E.S., and Zanni, G. (2020). TUBB variants underlying different phenotypes result in altered vesicle trafficking and microtubule dynamics. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21041385"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1002\/cne.23836","article-title":"The expression of Tubb2b undergoes a developmental transition in murine cortical neurons","volume":"523","author":"Breuss","year":"2015","journal-title":"J. Comp. Neurol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1038\/ng.380","article-title":"Mutations in the beta-tubulin gene TUBB2B result in asymmetrical polymicrogyria","volume":"41","author":"Jaglin","year":"2009","journal-title":"Nat. Genet."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"5484","DOI":"10.1093\/hmg\/dds393","article-title":"An inherited TUBB2B mutation alters a kinesin-binding site and causes polymicrogyria, CFEOM and axon dysinnervation","volume":"21","author":"Cederquist","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1038\/ejhg.2012.21","article-title":"Symmetric polymicrogyria and pachygyria associated with TUBB2B gene mutations","volume":"20","author":"Guerrini","year":"2012","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1111\/j.1469-8749.2012.04316.x","article-title":"A novel mutation in the \u03b2-tubulin gene TUBB2B associated with complex malformation of cortical development and deficits in axonal guidance","volume":"54","author":"Romaniello","year":"2012","journal-title":"Dev. Med. Child Neurol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1080\/15513815.2018.1538273","article-title":"De novo mutated TUBB2B associated pachygyria diagnosed by medical exome sequencing and long-range PCR","volume":"38","author":"Wang","year":"2019","journal-title":"Fetal Pediatr. Pathol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1002\/cm.20436","article-title":"Tumoral and tissue-specific expression of the major human beta-tubulin isotypes","volume":"67","author":"Landa","year":"2010","journal-title":"Cytoskeleton (Hoboken)"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1016\/j.ajhg.2014.03.009","article-title":"De novo mutations in the beta-tubulin gene TUBB2A cause simplified gyral patterning and infantile-onset epilepsy","volume":"94","author":"Cushion","year":"2014","journal-title":"Am. J. Hum. Genet."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2725","DOI":"10.1002\/ajmg.a.38352","article-title":"De novo pathogenic variant in TUBB2A presenting with arthrogryposis multiplex congenita, brain abnormalities, and severe developmental delay","volume":"173","author":"Ejaz","year":"2017","journal-title":"Am. J. Med. Genet. A"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1038\/s10038-020-0739-5","article-title":"De novo mutations of TUBB2A cause infantile-onset epilepsy and developmental delay","volume":"65","author":"Cai","year":"2020","journal-title":"J. Hum. Genet."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1093\/hmg\/ddy096","article-title":"Defective kinesin binding of TUBB2A causes progressive spastic ataxia syndrome resembling sacsinopathy","volume":"27","author":"Sferra","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.neuron.2014.09.027","article-title":"Exome-wide rare variant analysis identifies TUBA4A mutations associated with familial ALS","volume":"84","author":"Smith","year":"2014","journal-title":"Neuron"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1002\/ana.23832","article-title":"Mutations in the autoregulatory domain of \u03b2-tubulin 4a cause hereditary dystonia","volume":"73","author":"Hersheson","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1002\/ana.23829","article-title":"Whispering dysphonia (DYT4 dystonia) is caused by a mutation in the TUBB4 gene","volume":"73","author":"Lohmann","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1093\/brain\/awu110","article-title":"Hypomyelination with atrophy of the basal ganglia and cerebellum: Further delineation of the phenotype and genotype-phenotype correlation","volume":"137","author":"Hamilton","year":"2014","journal-title":"Brain"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1212\/WNL.0000000000000754","article-title":"TUBB4A de novo mutations cause isolated hypomyelination","volume":"83","author":"Pizzino","year":"2014","journal-title":"Neurology"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"17035","DOI":"10.1038\/hgv.2017.35","article-title":"A novel TUBB4A mutation G96R identified in a patient with hypomyelinating leukodystrophy onset beyond adolescence","volume":"4","author":"Lu","year":"2017","journal-title":"Hum. Genome Var."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1002\/mds.26196","article-title":"Mosaic dominant TUBB4A mutation in an inbred family with complicated hereditary spastic paraplegia","volume":"30","author":"Kancheva","year":"2015","journal-title":"Mov. Disord."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.jns.2016.07.002","article-title":"Congenital-onset spastic paraplegia in a patient with TUBB4A mutation and mild hypomyelination","volume":"368","author":"Nicita","year":"2016","journal-title":"J. Neurol. Sci."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/s00415-016-8020-8","article-title":"Early-onset progressive spastic paraplegia caused by a novel TUBB4A mutation: Brain MRI and FDG-PET findings","volume":"263","author":"Sagnelli","year":"2016","journal-title":"J. Neurol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.1093\/brain\/awu082","article-title":"The wide spectrum of tubulinopathies: What are the key features for the diagnosis?","volume":"137","author":"Poirier","year":"2014","journal-title":"Brain"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Aiken, J., Buscaglia, G., Bates, E.A., and Moore, J.K. (2017). The \u03b1-Tubulin gene TUBA1A in brain development: A key ingredient in the neuronal isotype blend. J. Dev. Biol., 5.","DOI":"10.3390\/jdb5030008"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1083\/jcb.101.3.852","article-title":"Five mouse tubulin isotypes and their regulated expression during development","volume":"101","author":"Lewis","year":"1985","journal-title":"J. Cell Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3065","DOI":"10.1083\/jcb.105.6.3065","article-title":"Isotypes of alpha-tubulin are differentially regulated during neuronal maturation","volume":"105","author":"Miller","year":"1987","journal-title":"J. Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.cell.2006.12.017","article-title":"Mutations in alpha-tubulin cause abnormal neuronal migration in mice and lissencephaly in humans","volume":"128","author":"Keays","year":"2007","journal-title":"Cell"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1002\/humu.20572","article-title":"Large spectrum of lissencephaly and pachygyria phenotypes resulting from de novo missense mutations in tubulin alpha 1A (TUBA1A)","volume":"28","author":"Poirier","year":"2007","journal-title":"Hum. Mutat."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1212\/WNL.0b013e31821043f5","article-title":"TUBA1A mutations: From isolated lissencephaly to familial polymicrogyria","volume":"76","author":"Jansen","year":"2011","journal-title":"Neurology"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.ejpn.2012.12.006","article-title":"Description of a novel TUBA1A mutation in Arg-390 associated with asymmetrical polymicrogyria and mid-hindbrain dysgenesis","volume":"17","author":"Zanni","year":"2013","journal-title":"Eur. J. Paediatr. Neurol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/ejhg.2012.195","article-title":"Expanding the spectrum of TUBA1A-related cortical dysgenesis to Polymicrogyria","volume":"21","author":"Poirier","year":"2013","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.braindev.2012.05.006","article-title":"Lissencephaly with marked ventricular dilation, agenesis of corpus callosum, and cerebellar hypoplasia caused by TUBA1A mutation","volume":"35","author":"Okumura","year":"2013","journal-title":"Brain Dev."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1093\/hmg\/ddy416","article-title":"TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity","volume":"28","author":"Aiken","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1006\/bbrc.2000.2571","article-title":"TUBA8: A new tissue-specific isoform of alpha-tubulin that is highly conserved in human and mouse","volume":"270","author":"Stanchi","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/j.ajhg.2009.10.007","article-title":"Mutation of the variant alpha-tubulin TUBA8 results in polymicrogyria with optic nerve hypoplasia","volume":"85","author":"Abdollahi","year":"2009","journal-title":"Am. J. Hum. Genet."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1091\/mbc.e13-07-0387","article-title":"Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure","volume":"25","author":"Howes","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2972","DOI":"10.1242\/jcs.187518","article-title":"SIRT2 inactivation reveals a subset of hyperacetylated perinuclear microtubules inaccessible to HDAC6","volume":"129","author":"Skoge","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1016\/j.cell.2018.05.018","article-title":"Tubulin posttranslational modifications and emerging links to human disease","volume":"173","author":"Magiera","year":"2018","journal-title":"Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.cell.2014.03.061","article-title":"Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase","volume":"157","author":"Szyk","year":"2014","journal-title":"Cell"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"11547","DOI":"10.1038\/s41598-017-11739-3","article-title":"Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules","volume":"7","author":"Skultetyova","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"E7176","DOI":"10.1073\/pnas.1605397113","article-title":"Mechanism of microtubule lumen entry for the alpha-tubulin acetyltransferase enzyme alphaTAT1","volume":"113","author":"Coombes","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"35624","DOI":"10.1038\/srep35624","article-title":"\u03b1TAT1 controls longitudinal spreading of acetylation marks from open microtubules extremities","volume":"6","author":"Ly","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"R1287","DOI":"10.1016\/j.cub.2017.10.044","article-title":"Causes and Consequences of Microtubule Acetylation","volume":"27","author":"Janke","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/ncb3481","article-title":"Tubulin acetylation protects long-lived microtubules against mechanical ageing","volume":"19","author":"Portran","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/ana.10300","article-title":"WldS mice are resistant to paclitaxel (taxol) neuropathy","volume":"52","author":"Wang","year":"2002","journal-title":"Ann. Neurol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/j.neuroscience.2007.04.059","article-title":"Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: A crucial role of tubulin deacetylation","volume":"147","author":"Suzuki","year":"2007","journal-title":"Neuroscience"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1523\/JNEUROSCI.13-02-00856.1993","article-title":"Regional differences in microtubule dynamics in the axon","volume":"13","author":"Ahmad","year":"1993","journal-title":"J. Neurosci."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.tcb.2014.10.004","article-title":"Post-translational modifications of tubulin: Pathways to functional diversity of microtubules","volume":"25","author":"Song","year":"2015","journal-title":"Trends Cell Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1016\/j.cub.2006.09.014","article-title":"Microtubule acetylation promotes kinesin-1 binding and transport","volume":"16","author":"Reed","year":"2006","journal-title":"Curr. Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"3571","DOI":"10.1523\/JNEUROSCI.0037-07.2007","article-title":"Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington\u2019s disease by increasing tubulin acetylation","volume":"27","author":"Dompierre","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"R18","DOI":"10.1016\/j.cub.2006.11.036","article-title":"Microtubule modification: Acetylation speeds anterograde traffic flow","volume":"17","author":"Bulinski","year":"2007","journal-title":"Curr. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1016\/j.bpj.2017.08.009","article-title":"Acetylated microtubules are preferentially bundled leading to enhanced kinesin-1 motility","volume":"113","author":"Balabanian","year":"2017","journal-title":"Biophys. J."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1080\/21541248.2016.1277002","article-title":"CAP-Gly proteins contribute to microtubule-dependent trafficking via interactions with the C-terminal aromatic residue of \u03b1-tubulin","volume":"10","author":"Andrieux","year":"2019","journal-title":"Small GTPases"},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Wloga, D., Joachimiak, E., and Fabczak, H. (2017). Tubulin post-translational modifications and microtubule dynamics. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18102207"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"17163","DOI":"10.1074\/jbc.R115.637447","article-title":"Writing and reading the tubulin code","volume":"290","author":"Yu","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"22936","DOI":"10.1074\/jbc.C110.128280","article-title":"Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases (CCPs)","volume":"285","author":"Kimura","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.cell.2010.10.014","article-title":"A family of protein-deglutamylating enzymes associated with neurodegeneration","volume":"143","author":"Rogowski","year":"2010","journal-title":"Cell"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3017","DOI":"10.1091\/mbc.e14-06-1072","article-title":"The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids","volume":"25","author":"Tort","year":"2014","journal-title":"Mol. Biol. Cell."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/0092-8674(84)90273-3","article-title":"Distinct populations of microtubules: Tyrosinated and nontyrosinated alpha tubulin are distributed differently in vivo","volume":"38","author":"Gundersen","year":"1984","journal-title":"Cell"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1083\/jcb.103.5.1883","article-title":"Ultrastructural colocalization of tyrosinated and detyrosinated alpha-tubulin in interphase and mitotic cells","volume":"103","author":"Geuens","year":"1986","journal-title":"J. Cell Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1242\/jcs.104.2.339","article-title":"Composite microtubules of the axon: Quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules","volume":"104","author":"Brown","year":"1993","journal-title":"J. Cell Sci."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1146\/annurev.biochem.69.1.277","article-title":"Structural insights into microtubule function","volume":"69","author":"Nogales","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"16254","DOI":"10.1038\/s41598-017-16586-w","article-title":"Identification of DmTTLL5 as a major tubulin glutamylase in the drosophila nervous system","volume":"7","author":"Devambez","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1074\/jbc.M705813200","article-title":"Polyglutamylation is a post-translational modification with a broad range of substrates","volume":"283","author":"Miro","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.4103\/1673-5374.259611","article-title":"Tubulin glutamylation: A skeleton key for neurodegenerative diseases","volume":"14","author":"Dubra","year":"2019","journal-title":"Neural Regen. Res."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1083\/jcb.201001024","article-title":"Tubulin polyglutamylation stimulates spastin-mediated microtubule severing","volume":"189","author":"Lacroix","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1016\/j.cell.2016.01.019","article-title":"Graded control of microtubule severing by tubulin glutamylation","volume":"164","author":"Valenstein","year":"2016","journal-title":"Cell"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"12471","DOI":"10.1021\/bi00207a014","article-title":"Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein Tau and tubulin","volume":"33","author":"Boucher","year":"1994","journal-title":"Biochemistry"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"12839","DOI":"10.1074\/jbc.M011380200","article-title":"Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation","volume":"276","author":"Bonnet","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_151","first-page":"920","article-title":"Polyglutamylation makes the cut","volume":"189","author":"Short","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1242\/jcs.107.8.2313","article-title":"Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons","volume":"107","author":"Audebert","year":"1994","journal-title":"J. Cell Sci."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"30707","DOI":"10.1074\/jbc.M603984200","article-title":"TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of MAP2-positive neurites","volume":"281","author":"Ikegami","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"3542","DOI":"10.1091\/mbc.e16-12-0820","article-title":"Two kinesins drive anterograde neuropeptide transport","volume":"28","author":"Lim","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1007\/s00018-016-2168-3","article-title":"Microtubule plus-end tracking proteins in neuronal development","volume":"73","author":"Hoogenraad","year":"2016","journal-title":"Cell Mol. Life Sci."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"jcs227850","DOI":"10.1242\/jcs.227850","article-title":"Microtubule minus-end regulation at a glance","volume":"132","author":"Akhmanova","year":"2019","journal-title":"J. Cell Sci."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/nrm3209","article-title":"Microtubule nucleation by \u03b3-tubulin complexes","volume":"12","author":"Kollman","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/emboj.2013.3","article-title":"Kif3a interacts with Dynactin subunit p150 Glued to organize centriole subdistal appendages","volume":"32","author":"Kodani","year":"2013","journal-title":"EMBO J."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1242\/bio.20135231","article-title":"Ninein is essential for the maintenance of the cortical progenitor character by anchoring the centrosome to microtubules","volume":"2","author":"Shinohara","year":"2013","journal-title":"Biol. Open"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/bs.ircmb.2015.10.002","article-title":"Building blocks of functioning brain: Cytoskeletal dynamics in neuronal development","volume":"322","author":"Menon","year":"2016","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1242\/jcs.1991.Supplement_15.9","article-title":"Microtubule-associated proteins and neuronal morphogenesis","volume":"15","author":"Matus","year":"1991","journal-title":"J. Cell Sci. Suppl."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0304-3940(99)00964-7","article-title":"Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice","volume":"279","author":"Ikegami","year":"2000","journal-title":"Neurosci. Lett."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1242\/jcs.114.6.1179","article-title":"Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice","volume":"114","author":"Dawson","year":"2001","journal-title":"J. Cell Sci."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"2350","DOI":"10.1101\/gad.223302","article-title":"The suppression of brain cold-stable microtubules in mice induces synaptic defects associated with neuroleptic-sensitive behavioral disorders","volume":"16","author":"Andrieux","year":"2002","journal-title":"Genes Dev."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0306-4522(03)00094-0","article-title":"Deletion of the N-terminus of murine map2 by gene targeting disrupts hippocampal ca1 neuron architecture and alters contextual memory","volume":"119","author":"Khuchua","year":"2003","journal-title":"Neuroscience"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"2287","DOI":"10.1038\/emboj.2013.166","article-title":"MAP1B-dependent Rac activation is required for AMPA receptor endocytosis during long-term depression","volume":"32","author":"Benoist","year":"2013","journal-title":"EMBO J."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"15539","DOI":"10.1523\/JNEUROSCI.2671-15.2015","article-title":"Defects in synaptic plasticity, reduced NMDA-receptor transport, and instability of postsynaptic density proteins in mice lacking microtubule-associated protein 1A","volume":"35","author":"Takei","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"13297","DOI":"10.1074\/jbc.RA118.001769","article-title":"Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics","volume":"293","author":"Zapletal","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Melkov\u00e1, K., Zapletal, V., Narasimhan, S., Jansen, S., Hritz, J., \u0160krabana, R., Zweckstetter, M., Ringkj\u00f8bing Jensen, M., Blackledge, M., and \u017d\u00eddek, L. (2019). Structure and functions of microtubule associated proteins tau and MAP2c: Similarities and differences. Biomolecules, 9.","DOI":"10.3390\/biom9030105"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1110\/ps.4210102","article-title":"Natively unfolded proteins: A point where biology waits for physics","volume":"11","author":"Uversky","year":"2002","journal-title":"Protein Sci."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1111\/j.1471-4159.1988.tb02954.x","article-title":"A 70-kilodalton microtubule-associated protein (MAP2c), related to MAP2","volume":"50","author":"Garner","year":"1988","journal-title":"J. Neurochem."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"4503","DOI":"10.1523\/JNEUROSCI.08-12-04503.1988","article-title":"The sequential appearance of low- and high-molecular-weight forms of MAP2 in the developing cerebellum","volume":"8","author":"Tucker","year":"1988","journal-title":"J. Neurosci."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/0166-2236(91)90105-4","article-title":"Molecular characterization of microtubule-associated proteins tau and MAP2","volume":"14","author":"Goedert","year":"1991","journal-title":"Trends Neurosci."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0165-3806(95)00117-V","article-title":"Developmental regulation of MAP2 variants during neuronal differentiation in vitro","volume":"89","author":"Przyborski","year":"1995","journal-title":"Brain Res. Dev. Brain Res."},{"key":"ref_175","first-page":"1","article-title":"Cytoskeletal maturation in cultured hippocampal slices","volume":"78","author":"Hartel","year":"1997","journal-title":"Neuroscience"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1046\/j.1460-9568.1998.00044.x","article-title":"MAP2d mRNA is expressed in identified neuronal populations in the developing and adult rat brain and its subcellular distribution differs from that of MAP2b in hippocampal neurones","volume":"10","author":"Ferhat","year":"1998","journal-title":"Eur. J. Neurosci."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"2538","DOI":"10.1002\/cne.22351","article-title":"Expression of the embryonal isoform (0N\/3R) of the microtubule-associated protein tau in the adult rat central nervous system","volume":"518","author":"Bullmann","year":"2010","journal-title":"J. Comp. Neurol."},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Liu, C., and G\u00f6tz, J. (2013). Profiling murine tau with 0N, 1N and 2N isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1N isoform being enriched in the nucleus. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0084849"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/j.1460-2075.1989.tb03390.x","article-title":"Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain","volume":"8","author":"Goedert","year":"1989","journal-title":"EMBO J."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/0896-6273(89)90077-9","article-title":"Developmentally regulated expression of specific tau sequences","volume":"2","author":"Kosik","year":"1989","journal-title":"Neuron"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1083\/jcb.200201048","article-title":"MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments","volume":"157","author":"Ozer","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0925-4773(01)00487-7","article-title":"Identification and characterization of the Drosophila tau homolog","volume":"108","author":"Heidary","year":"2001","journal-title":"Mech. Dev."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nrn2194","article-title":"Tau-mediated neurodegeneration in Alzheimer\u2019s disease and related disorders","volume":"8","author":"Ballatore","year":"2007","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S1474-4422(13)70090-5","article-title":"Tau pathology and neurodegeneration","volume":"12","author":"Spillantini","year":"2013","journal-title":"Lancet Neurol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1016\/j.jmb.2016.03.010","article-title":"Regulation of Microtubule Assembly by Tau and not by Pin1","volume":"428","author":"Kutter","year":"2016","journal-title":"Mol. Biol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"9548","DOI":"10.1073\/pnas.1633508100","article-title":"Differential regulation of microtubule dynamics by three- and four-repeat tau: Implications for the onset of neurodegenerative disease","volume":"100","author":"Panda","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"12459","DOI":"10.1073\/pnas.96.22.12459","article-title":"Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau","volume":"96","author":"Panda","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/360674a0","article-title":"Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons","volume":"360","author":"Chen","year":"1992","journal-title":"Nature"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"7445","DOI":"10.1073\/pnas.0802036105","article-title":"Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis","volume":"105","author":"Rosenberg","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.bpj.2009.04.047","article-title":"Human microtubule-associated-protein tau regulates the number of protofilaments in microtubules: A synchrotron x-ray scattering study","volume":"97","author":"Choi","year":"2009","journal-title":"Biophys. J."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1083\/jcb.132.4.667","article-title":"Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons","volume":"132","author":"Hirokawa","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1083\/jcb.104.6.1575","article-title":"Colocalization of microtubule-associated protein 1A and microtubule-associated protein 2 on neuronal microtubules in situ revealed with double-label immunoelectron microscopy","volume":"104","author":"Shiomura","year":"1987","journal-title":"J. Cell Biol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"2769","DOI":"10.1523\/JNEUROSCI.08-08-02769.1988","article-title":"MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies","volume":"8","author":"Hirokawa","year":"1988","journal-title":"J. Neurosci."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"9847","DOI":"10.1016\/S0021-9258(18)98423-1","article-title":"Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly","volume":"268","author":"Kowalski","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1111\/j.1471-4159.1993.tb03225.x","article-title":"Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 s repeated sequence analogue","volume":"60","author":"Yamauchi","year":"1993","journal-title":"J. Neurochem."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1002\/(SICI)1097-0169(1996)35:2<134::AID-CM6>3.0.CO;2-A","article-title":"Differences in the regulation of microtubule dynamics by microtubule-associated proteins MAP1B and MAP2","volume":"35","author":"Vandecandelaere","year":"1996","journal-title":"Cell Motil. Cytoskelet."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/(SICI)1097-0169(1998)40:3<272::AID-CM6>3.0.CO;2-F","article-title":"Molecular and functional characteristics of MAP-2a: Ability of MAP-2a versus MAP-2b to induce stable microtubules in COS cells","volume":"40","author":"Kalcheva","year":"1998","journal-title":"Cell Motil. Cytoskelet."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/0092-8674(91)90510-6","article-title":"Inhibition of MAP2 expression affects both morphological and cell division phenotypes of neuronal differentiation","volume":"64","author":"Dinsmore","year":"1991","journal-title":"Cell"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1083\/jcb.200106025","article-title":"Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth, and microtubule organization","volume":"155","author":"Teng","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1083\/jcb.200110134","article-title":"MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction","volume":"158","author":"Harada","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.ajhg.2013.03.018","article-title":"A de novo mutation in the \u03b2-tubulin gene TUBB4A results in the leukoencephalopathy hypomyelination with atrophy of the basal ganglia and cerebellum","volume":"92","author":"Simons","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.ejpn.2015.11.006","article-title":"TUBB4A-related hypomyelinating leukodystrophy: New insights from a series of 12 patients","volume":"20","author":"Tonduti","year":"2016","journal-title":"Eur. J. Paediatr. Neurol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1038\/emboj.2013.59","article-title":"\u03b2-Tubulin mutations that cause severe neuropathies disrupt axonal transport","volume":"32","author":"Niwa","year":"2013","journal-title":"EMBO J."},{"key":"ref_204","first-page":"31","article-title":"The cell cycle and human neurodegenerative disease","volume":"5","author":"Vincent","year":"2003","journal-title":"Prog. Cell Cycle Res."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1093\/mutage\/gem044","article-title":"Chromosome 17 and 21 aneuploidy in buccal cells is increased with ageing and in Alzheimer\u2019s disease","volume":"23","author":"Thomas","year":"2008","journal-title":"Mutagenesis"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.mad.2011.04.008","article-title":"Chromosomal aneuploidy in the aging brain","volume":"132","author":"Faggioli","year":"2011","journal-title":"Mech. Ageing Dev."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Granic, A., and Potter, H. (2013). Mitotic spindle defects and chromosome mis-segregation induced by LDL\/cholesterol-implications for Niemann-Pick C1, Alzheimer\u2019s disease, and atherosclerosis. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0060718"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1242\/dmm.013391","article-title":"Aneuploidy: Implications for protein homeostasis and disease","volume":"7","author":"Oromendia","year":"2014","journal-title":"Dis. Models Mech."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"15","DOI":"10.2353\/ajpath.2010.090955","article-title":"Selective cell death of hyperploid neurons in Alzheimer\u2019s disease","volume":"177","author":"Arendt","year":"2010","journal-title":"Am. J. Pathol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/1755-8166-7-20","article-title":"X chromosome aneuploidy in the Alzheimer\u2019s disease brain","volume":"7","author":"Yurov","year":"2014","journal-title":"Mol. Cytogenet."},{"key":"ref_211","first-page":"115","article-title":"Expansion of the spectrum of TUBB4A-related disorders: A new phenotype associated with a novel mutation in the TUBB4A gene","volume":"15","author":"Blumkin","year":"2014","journal-title":"Neurogenetics"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s00439-015-1617-7","article-title":"Genetic heterogeneity in 26 infants with a hypomyelinating leukodystrophy","volume":"135","author":"Uematsu","year":"2016","journal-title":"Hum. Genet."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"2230","DOI":"10.1212\/WNL.0000000000000535","article-title":"Expanding the phenotypic spectrum of TUBB4A-associated hypomyelinating leukoencephalopathies","volume":"82","author":"Miyatake","year":"2014","journal-title":"Neurology"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/j.pediatrneurol.2014.01.051","article-title":"Clinical exome sequencing identifies a novel TUBB4A mutation in a child with static hypomyelinating leukodystrophy","volume":"50","author":"Purnell","year":"2014","journal-title":"Pediatr. Neurol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/jnen\/nly105","article-title":"Severe TUBB4A-related hypomyelination with atrophy of the basal ganglia and cerebellum: Novel neuropathological findings","volume":"78","author":"Joyal","year":"2019","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_216","doi-asserted-by":"crossref","unstructured":"Ji, H., Li, D., Wu, Y., Zhang, Q., Gu, Q., Xie, H., Ji, T., Wang, H., Zhao, L., and Zhao, H. (2018). Hypomyelinating disorders in China: The clinical and genetic heterogeneity in 119 patients. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0188869"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"e327","DOI":"10.1093\/brain\/awu242","article-title":"TUBB4A novel mutation reinforces the genotype-phenotype correlation of hypomyelination with atrophy of the basal ganglia and cerebellum","volume":"138","author":"Carvalho","year":"2015","journal-title":"Brain"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1002\/ajmg.a.36526","article-title":"Novel TUBB4A mutations and expansion of the neuroimaging phenotype of hypomyelination with atrophy of the basal ganglia and cerebellum (H-ABC)","volume":"164","author":"Ferreira","year":"2014","journal-title":"Am. J. Med. Genet. A"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"4506","DOI":"10.1093\/hmg\/ddx338","article-title":"TUBB4A mutations result in specific neuronal and oligodendrocytic defects that closely match clinically distinct phenotypes","volume":"26","author":"Curiel","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"e52986","DOI":"10.7554\/eLife.52986","article-title":"TUBB4A mutations result in both glial and neuronal degeneration in an H-ABC leukodystrophy mouse model","volume":"9","author":"Sase","year":"2020","journal-title":"eLife"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"2444","DOI":"10.1002\/humu.23913","article-title":"Motor protein binding and mitochondrial transport are altered by pathogenic TUBB4A variants","volume":"40","author":"Vulinovic","year":"2019","journal-title":"Hum. Mutat."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/334580a0","article-title":"Autoregulated instability of beta-tubulin mRNAs by recognition of the nascent amino terminus of beta-tubulin","volume":"334","author":"Yen","year":"1988","journal-title":"Nature"},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.bbrc.2017.11.038","article-title":"Dystonia-4 (DYT4)-associated TUBB4A mutants exhibit disorganized microtubule networks and inhibit neuronal process growth","volume":"495","author":"Watanabe","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1038\/nm.2396","article-title":"HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease","volume":"17","author":"Krishnan","year":"2011","journal-title":"Nat. Med."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1093\/hmg\/ddt028","article-title":"Hdac6 deletion delays disease progression in the SOD1G93A mouse model of ALS","volume":"22","author":"Taes","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"5245","DOI":"10.1038\/ncomms6245","article-title":"Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations","volume":"5","author":"Godena","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"25279","DOI":"10.1074\/jbc.A113.464792","article-title":"Mice lacking \u03b1-tubulin acetyltransferase 1 are viable but display \u03b1-tubulin acetylation deficiency and dentate gyrus distortion","volume":"291","author":"Kim","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1097\/00005072-199609000-00003","article-title":"Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer\u2019s disease","volume":"55","author":"Hempen","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1111\/j.1471-4159.2008.05564.x","article-title":"Histone deacetylase 6 interacts with the microtubule-associated protein tau","volume":"106","author":"Ding","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1002\/emmm.201201923","article-title":"Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer\u2019s disease","volume":"5","author":"Govindarajan","year":"2013","journal-title":"EMBO Mol. Med."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1750-1326-8-7","article-title":"HDAC6 as a target for neurodegenerative diseases: What makes it different from the other HDACs?","volume":"8","author":"Zwick","year":"2013","journal-title":"Mol. Neurodegener."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1073\/pnas.1207586110","article-title":"HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila","volume":"110","author":"Xiong","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"104717","DOI":"10.1016\/j.nbd.2019.104717","article-title":"Loss of Parkin contributes to mitochondrial turnover and dopaminergic neuronal loss in aged mice","volume":"136","author":"Noda","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neurobiolaging.2017.09.010","article-title":"Parkin absence accelerates microtubule aging in dopaminergic neurons","volume":"61","author":"Cartelli","year":"2018","journal-title":"Neurobiol. Aging"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1096\/fj.09-147942","article-title":"CCP1\/Nna1 functions in protein turnover in mouse brain: Implications for cell death in Purkinje cell degeneration mice","volume":"24","author":"Berezniuk","year":"2010","journal-title":"FASEB J."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"e100440","DOI":"10.15252\/embj.2018100440","article-title":"Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport","volume":"37","author":"Magiera","year":"2018","journal-title":"EMBO J."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1083\/jcb.201709028","article-title":"CCP1 promotes mitochondrial fusion and motility to prevent Purkinje cell neuron loss in pcd mice","volume":"218","author":"Kuo","year":"2019","journal-title":"J. Cell Biol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"jcs241802","DOI":"10.1242\/jcs.241802","article-title":"Tubulin polyglutamylation is a general traffic-control mechanism in hippocampal neurons","volume":"133","author":"Bodakuntla","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"e100540","DOI":"10.15252\/embj.2018100540","article-title":"Loss of tubulin deglutamylase CCP1 causes infantile-onset neurodegeneration","volume":"37","author":"Shashi","year":"2018","journal-title":"EMBO J."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"40205","DOI":"10.1038\/srep40205","article-title":"Increase in \u03b1-tubulin modifications in the neuronal processes of hippocampal neurons in both kainic acid-induced epileptic seizure and Alzheimer\u2019s disease","volume":"7","author":"Vu","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1242\/jcs.115.5.941","article-title":"Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington\u2019s disease","volume":"115","author":"Hoffner","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"334","DOI":"10.4161\/pri.20677","article-title":"Dysfunction of microtubule-associated proteins of MAP2\/tau family in Prion disease","volume":"6","author":"Zhang","year":"2012","journal-title":"Prion"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s00018-016-2351-6","article-title":"Back to the tubule: Microtubule dynamics in Parkinson\u2019s disease","volume":"74","author":"Pellegrini","year":"2017","journal-title":"Cell Mol. Life Sci."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.pneurobio.2008.03.002","article-title":"Microtubule-associated protein tau in development, degeneration and protection of neurons","volume":"85","author":"Wang","year":"2008","journal-title":"Prog. Neurobiol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/197192b0","article-title":"Paired helical filaments in electron microscopy of Alzheimer\u2019s disease","volume":"197","author":"Kidd","year":"1963","journal-title":"Nature"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1146\/annurev.neuro.24.1.1121","article-title":"Neurodegenerative tauopathies","volume":"24","author":"Lee","year":"2001","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/0896-6273(93)90057-X","article-title":"Abnormal tau phosphorylation at Ser396 in Alzheimer\u2019s disease recapitulates development and contributes to reduced microtubule binding","volume":"10","author":"Bramblett","year":"1993","journal-title":"Neuron"},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"5562","DOI":"10.1073\/pnas.91.12.5562","article-title":"Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease","volume":"91","author":"Alonso","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"615","DOI":"10.3233\/JAD-2011-111778","article-title":"Intracellular amyloid-\u03b2 accumulation in calcium-binding protein-deficient neurons leads to amyloid-\u03b2 plaque formation in animal model of Alzheimer\u2019s disease","volume":"29","author":"Moon","year":"2012","journal-title":"J. Alzheimers Dis."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"9733","DOI":"10.1523\/JNEUROSCI.22-22-09733.2002","article-title":"Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer\u2019s disease","volume":"22","author":"Fath","year":"2002","journal-title":"J. Neurosci."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease: Progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"6364","DOI":"10.1073\/pnas.092136199","article-title":"Tau is essential to beta -amyloid-induced neurotoxicity","volume":"99","author":"Rapoport","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1126\/science.1141736","article-title":"Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer\u2019s disease mouse model","volume":"316","author":"Roberson","year":"2007","journal-title":"Science"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"2920","DOI":"10.1038\/emboj.2013.207","article-title":"Amyloid-\u03b2 oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin","volume":"32","author":"Zempel","year":"2013","journal-title":"EMBO J."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"11117","DOI":"10.1021\/bi00035a017","article-title":"Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau","volume":"34","author":"Panda","year":"1995","journal-title":"Biochemistry"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.bcp.2014.01.002","article-title":"Alzheimer disease therapeutics: Focus on the disease and not just plaques and tangles","volume":"88","author":"Iqbal","year":"2014","journal-title":"Biochem. Pharmacol."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1073\/pnas.94.1.298","article-title":"Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau","volume":"94","author":"Alonso","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1523\/JNEUROSCI.2824-07.2008","article-title":"The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy","volume":"28","author":"Mocanu","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_259","first-page":"31825","article-title":"Dysregulation of protein phosphorylation\/dephosphorylation in Alzheimer\u2019s disease: A therapeutic target","volume":"2006","author":"Gong","year":"2006","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"6026","DOI":"10.1523\/JNEUROSCI.21-16-06026.2001","article-title":"Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments","volume":"21","author":"Ishihara","year":"2001","journal-title":"J. Neurosci."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1523\/JNEUROSCI.22-01-00133.2002","article-title":"Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau","volume":"22","author":"Tanemura","year":"2002","journal-title":"J. Neurosci."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"137","DOI":"10.2174\/1567205053585936","article-title":"Synaptic fatigue is more pronounced in the APP\/PS1 transgenic mouse model of Alzheimer\u2019s disease","volume":"2","author":"Zhang","year":"2005","journal-title":"Curr. Alzheimer Res."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"7137","DOI":"10.1523\/JNEUROSCI.0188-12.2012","article-title":"Hyperdynamic microtubules, cognitive deficits, and pathology are improved in tau transgenic mice with low doses of the microtubule-stabilizing agent BMS-241027","volume":"32","author":"Barten","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1016\/S0002-9440(10)64296-4","article-title":"Microtubule reduction in Alzheimer\u2019s disease and aging is independent of tau filament formation","volume":"162","author":"Cash","year":"2003","journal-title":"Am. J. Pathol."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s40035-015-0030-4","article-title":"Posttranslational modifications of \u03b1-tubulin in alzheimer disease","volume":"4","author":"Zhang","year":"2015","journal-title":"Transl. Neurodegener."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s13024-020-00368-6","article-title":"Initiation and propagation of \u03b1-synuclein aggregation in the nervous system","volume":"15","author":"Hijaz","year":"2020","journal-title":"Mol. Neurodegener."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"S23","DOI":"10.1016\/S1353-8020(13)70009-9","article-title":"Genetics of Parkinson\u2019s disease\u2013State of the art, 2013","volume":"1","author":"Bonifati","year":"2014","journal-title":"Parkinsonism Relat. Disord."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"3316","DOI":"10.1523\/JNEUROSCI.23-08-03316.2003","article-title":"Parkin binds to alpha\/beta tubulin and increases their ubiquitination and degradation","volume":"23","author":"Ren","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1074\/jbc.M113.507913","article-title":"A direct interaction between leucine-rich repeat kinase 2 and specific \u03b2-tubulin isoforms regulates tubulin acetylation","volume":"289","author":"Law","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"17154","DOI":"10.1074\/jbc.M500843200","article-title":"Parkin stabilizes microtubules through strong binding mediated by three independent domains","volume":"280","author":"Yang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"33289","DOI":"10.1038\/srep33289","article-title":"\u03b1-synuclein is a novel microtubule dynamase","volume":"6","author":"Cartelli","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"1685","DOI":"10.2147\/NDT.S166322","article-title":"The direct and indirect effects of \u03b1-synuclein on microtubule stability in the pathogenesis of Parkinson\u2019s disease","volume":"14","author":"Carnwath","year":"2018","journal-title":"Neuropsychiatr. Dis. Treat."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/33416","article-title":"Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism","volume":"392","author":"Kitada","year":"1998","journal-title":"Nature"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"R127","DOI":"10.1093\/hmg\/ddh089","article-title":"Parkin genetics: One model for Parkinson\u2019s disease","volume":"1","author":"Mata","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/77060","article-title":"Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase","volume":"25","author":"Shimura","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_276","doi-asserted-by":"crossref","unstructured":"Cartelli, D., Goldwurm, S., Casagrande, F., Pezzoli, G., and Cappelletti, G. (2012). Microtubule destabilization is shared by genetic and idiopathic Parkinson\u2019s disease patient fibroblasts. PLoS ONE, 7.","DOI":"10.1371\/annotation\/6db7193b-913a-42f2-aa7c-139d6e15142a"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"4009","DOI":"10.1074\/jbc.M806245200","article-title":"Parkin protects dopaminergic neurons against microtubule-depolymerizing toxins by attenuating microtubule-associated protein kinase activation","volume":"284","author":"Ren","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1002\/stem.1854","article-title":"Parkin mutations reduce the complexity of neuronal processes in iPSC-derived human neurons","volume":"33","author":"Ren","year":"2015","journal-title":"Stem Cells"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-3-319-49969-7_1","article-title":"Leucine-rich repeat kinase (LRRK2) genetics and Parkinson\u2019s disease","volume":"14","author":"Monfrini","year":"2017","journal-title":"Adv. Neurobiol."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1111\/j.1471-4159.2009.06235.x","article-title":"Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability\u2014A point of convergence in parkinsonian neurodegeneration?","volume":"110","author":"Gillardon","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1002\/jnr.21622","article-title":"The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules","volume":"86","author":"Gandhi","year":"2008","journal-title":"Neurosci. Res."},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.neuron.2006.10.008","article-title":"The familial Parkinsonism gene LRRK2 regulates neurite process morphology","volume":"52","author":"MacLeod","year":"2006","journal-title":"Neuron"},{"key":"ref_283","doi-asserted-by":"crossref","unstructured":"Kawakami, F., Yabata, T., Ohta, E., Maekawa, T., Shimada, N., Suzuki, M., Maruyama, H., Ichikawa, T., and Obata, F. (2012). LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030834"},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1007\/s00401-013-1188-4","article-title":"LRRK2 phosphorylates novel tau epitopes and promotes tauopathy","volume":"126","author":"Bailey","year":"2013","journal-title":"Acta Neuropathol."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.neulet.2004.05.100","article-title":"Alpha-synuclein missense and multiplication mutations in autosomal dominant Parkinson\u2019s disease","volume":"367","author":"Hope","year":"2004","journal-title":"Neurosci. Lett."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of \u03b1-synuclein: From structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"435","DOI":"10.3233\/JAD-2004-6412","article-title":"Demonstration of a role for alpha-synuclein as a functional microtubule-associated protein","volume":"6","author":"Alim","year":"2004","journal-title":"Alzheimers Dis."},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.bbrc.2007.02.163","article-title":"Oligomeric alpha-synuclein inhibits tubulin polymerization","volume":"356","author":"Chen","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"6762","DOI":"10.1007\/s12035-016-0188-5","article-title":"Microtubule destabilization paves the way to Parkinson\u2019s disease","volume":"54","author":"Cartelli","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1073\/pnas.0406361102","article-title":"Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model","volume":"102","author":"Zhang","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"3601","DOI":"10.1523\/JNEUROSCI.4922-11.2012","article-title":"The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice","volume":"32","author":"Zhang","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1038\/srep01837","article-title":"Microtubule alterations occur early in experimental parkinsonism and the microtubule stabilizer epothilone D is neuroprotective","volume":"3","author":"Cartelli","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1242\/bio.20147641","article-title":"Low dose tubulin-binding drugs rescue peroxisome trafficking deficit in patient-derived stem cells in Hereditary Spastic Paraplegia","volume":"3","author":"Fan","year":"2014","journal-title":"Biol. Open"},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-018-0291-3","article-title":"A brain-penetrant triazolopyrimidine enhances microtubule-stability, reduces axonal dysfunction and decreases tau pathology in a mouse tauopathy model","volume":"13","author":"Zhang","year":"2018","journal-title":"Mol. Neurodegener."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"23465","DOI":"10.1074\/jbc.M703434200","article-title":"Stabilization of hyperdynamic microtubules is neuroprotective in amyotrophic lateral sclerosis","volume":"282","author":"Fanara","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1124\/jpet.106.106898","article-title":"NAP enhances neurodevelopment of newborn apolipoprotein E-deficient mice subjected to hypoxia","volume":"319","author":"Rotstein","year":"2006","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.nbd.2009.02.011","article-title":"NAP protects memory, increases soluble tau and reduces tau hyperphosphorylation in a tauopathy model","volume":"34","author":"Shiryaev","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"455","DOI":"10.2174\/156720509789207895","article-title":"Addressing Alzheimer\u2019s disease tangles: From NAP to AL-108","volume":"6","author":"Gozes","year":"2009","journal-title":"Curr. Alzheimer Res."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1159\/000348347","article-title":"A double-blind, placebo-controlled, ascending-dose, randomized study to evaluate the safety, tolerability and effects on cognition of AL-108 after 12 weeks of intranasal administration in subjects with mild cognitive impairment","volume":"35","author":"Morimoto","year":"2013","journal-title":"Dement. Geriatr. Cogn. Disord."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"872","DOI":"10.3389\/fnins.2018.00872","article-title":"The HDAC6 inhibitor trichostatin A acetylates microtubules and protects axons from excitotoxin-induced degeneration in a compartmented culture model","volume":"12","author":"Hanson","year":"2018","journal-title":"Front. Neurosci."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/alzrt241","article-title":"Histone deacetylase 6 inhibition improves memory and reduces total tau levels in a mouse model of tau deposition","volume":"6","author":"Selenica","year":"2014","journal-title":"Alzheimers Res. Ther."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1126\/science.1143780","article-title":"Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson\u2019s disease","volume":"317","author":"Outeiro","year":"2007","journal-title":"Science"},{"key":"ref_303","doi-asserted-by":"crossref","unstructured":"Chen, X., Wales, P., Quinti, L., Zuo, F., Moniot, S., Herisson, F., Rauf, N.A., Wang, H., Silverman, R.B., and Ayata, C. (2015). The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson\u2019s disease but not amyotrophic lateral sclerosis and cerebral ischemia. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0116919"},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.1016\/j.celrep.2012.11.001","article-title":"The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington\u2019s disease mouse models","volume":"2","author":"Chopra","year":"2012","journal-title":"Cell Rep."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/277665a0","article-title":"Promotion of microtubule assembly in vitro by taxol","volume":"277","author":"Schiff","year":"1979","journal-title":"Nature"},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1073\/pnas.77.3.1561","article-title":"Taxol stabilizes microtubules in mouse fibroblast cells","volume":"77","author":"Schiff","year":"1980","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/375424a0","article-title":"Structure of tubulin at 6.5 A and location of the taxol-binding site","volume":"375","author":"Nogales","year":"1995","journal-title":"Nature"},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/30288","article-title":"Structure of the alpha beta tubulin dimer by electron crystallography","volume":"393","author":"Nogales","year":"1998","journal-title":"Nature"},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"226","DOI":"10.3389\/fncel.2018.00226","article-title":"Repositioning microtubule stabilizing drugs for brain disorders","volume":"12","author":"Varidaki","year":"2018","journal-title":"Front. Cell. Neurosci."},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"13861","DOI":"10.1523\/JNEUROSCI.3059-10.2010","article-title":"Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy","volume":"30","author":"Brunden","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/j.chembiol.2017.05.016","article-title":"Triazolopyrimidines are microtubule-stabilizing agents that bind the vinca inhibitor site of tubulin","volume":"24","author":"Sharma","year":"2017","journal-title":"Cell Chem. Biol."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.pharmthera.2007.01.004","article-title":"Activity-dependent neuroprotective protein: From gene to drug candidate","volume":"114","author":"Gozes","year":"2007","journal-title":"Pharmacol. Ther."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"507","DOI":"10.2174\/156720507783018208","article-title":"NAP, a neuroprotective drug candidate in clinical trials, stimulates microtubule assembly in the living cell","volume":"4","author":"Gozes","year":"2007","journal-title":"Curr. Alzheimer Res."},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.3233\/JAD-2010-1335","article-title":"The neuroprotective peptide NAP does not directly affect polymerization or dynamics of reconstituted neural microtubules","volume":"19","author":"Yenjerla","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1385\/JMN\/31:02:165","article-title":"Intranasal NAP administration reduces accumulation of amyloid peptide and tau hyperphosphorylation in a transgenic mouse model of Alzheimer\u2019s disease at early pathological stage","volume":"31","author":"Matsuoka","year":"2007","journal-title":"J. Mol. Neurosci."},{"key":"ref_316","first-page":"1091","article-title":"Activity-dependent neurotrophic factor: Intranasal administration of femtomolar-acting peptides improve performance in a water maze","volume":"293","author":"Gozes","year":"2000","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"e00065","DOI":"10.1002\/prp2.65","article-title":"Intranasal NAP (davunetide) decreases tau hyperphosphorylation and moderately improves behavioral deficits in mice overexpressing \u03b1-synuclein","volume":"2","author":"Magen","year":"2014","journal-title":"Pharmacol. Res. Perspect."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1161\/01.STR.0000014207.05597.D7","article-title":"NAP, a femtomolar-acting peptide, protects the brain against ischemic injury by reducing apoptotic death","volume":"33","author":"Leker","year":"2002","journal-title":"Stroke"},{"key":"ref_319","first-page":"774","article-title":"Prevention of fetal demise and growth restriction in a mouse model of fetal alcohol syndrome","volume":"297","author":"Spong","year":"2001","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1038\/mp.2013.32","article-title":"NAP (davunetide) rescues neuronal dysfunction in a Drosophila model of tauopathy","volume":"18","author":"Quraishe","year":"2013","journal-title":"Mol. Psychiatry"},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1038\/mp.2016.255","article-title":"ADNP\/NAP dramatically increase microtubule end-binding protein-Tau interaction: A novel avenue for protection against tauopathy","volume":"22","author":"Sayas","year":"2017","journal-title":"Mol. Psychiatry"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"643","DOI":"10.4161\/auto.5050","article-title":"HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration","volume":"3","author":"Pandey","year":"2007","journal-title":"Autophagy"},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1093\/emboj\/cdf682","article-title":"In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation","volume":"21","author":"Matsuyama","year":"2002","journal-title":"EMBO J."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1093\/emboj\/cdg115","article-title":"HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo","volume":"22","author":"Zhang","year":"2003","journal-title":"EMBO J."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"297","DOI":"10.2183\/pjab.93.019","article-title":"Chemical and structural biology of protein lysine deacetylases","volume":"93","author":"Yoshida","year":"2017","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"10842","DOI":"10.1021\/ja102758v","article-title":"Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A","volume":"132","author":"Butler","year":"2010","journal-title":"J. Am. Chem. Soc."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/19\/7354\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:16:37Z","timestamp":1760177797000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/19\/7354"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,5]]},"references-count":326,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2020,10]]}},"alternative-id":["ijms21197354"],"URL":"https:\/\/doi.org\/10.3390\/ijms21197354","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,10,5]]}}}