Tubulin Posttranslational Modifications and Emerging Links to Human Disease

Genes and molecular pathways underpinning ciliopathies

Reiter, J. F., & Leroux, M. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.60 · Cited by 1,588

Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation

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Purkinje cell degeneration, a new neurological mutation in the mouse.

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The tubulin code: Molecular components, readout mechanisms, and functions

Janke, C. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201406055 · Cited by 534

Microtubules acquire resistance from mechanical breakage through intralumenal acetylation

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HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1–induced Charcot-Marie-Tooth disease

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A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration

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Centriole Disassembly In Vivo and Its Effect on Centrosome Structure and Function in Vertebrate Cells

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Post-translational modifications of tubulin: pathways to functional diversity of microtubules

Song, Y., & Brady, S. T. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.10.004 · Cited by 377

Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes

Robison, P., Caporizzo, M. A., Ahmadzadeh, H., Bogush, A. I., Chen, C. Y., Margulies, K. B., Shenoy, V. B., & Prosser, B. L. (2016) · Science · doi:10.1126/science.aaf0659 · Cited by 338

Primary cilia as dynamic and diverse signalling hubs in development and disease

Mill, P., Christensen, S. T., & Pedersen, L. B. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00587-9 · Cited by 417

Effects of α-tubulin acetylation on microtubule structure and stability

Eshun-Wilson, L., Zhang, R., Portran, D., Nachury, M. V., Toso, D. B., Löhr, T., Vendruscolo, M., Bonomi, M., Fraser, J. S., & Nogales, E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900441116 · Cited by 367

The Tubulin Code in Microtubule Dynamics and Information Encoding

Roll‐Mecak, A. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.008 · Cited by 307

Structure of the Decorated Ciliary Doublet Microtubule

Ma, M., Stoyanova, M., Rademacher, G., Dutcher, S. K., Brown, A., & Zhang, R. (2019) · Cell · doi:10.1016/j.cell.2019.09.030 · Cited by 290

Mechanisms of microtubule organization in differentiated animal cells

Akhmanova, A., & Kapitein, L. C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00473-y · Cited by 233

Ciliary Beating Compartmentalizes Cerebrospinal Fluid Flow in the Brain and Regulates Ventricular Development

Olstad, E. W., Ringers, C., Hansen, J. N., Wens, A., Brandt, C., Wachten, D., Yaksi, E., & Jurisch‐Yaksi, N. (2018) · Current Biology · doi:10.1016/j.cub.2018.11.059 · Cited by 214

Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases

Sferra, A., Nicita, F., & Bertini, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197354 · Cited by 138

Generation and regulation of microtubule network asymmetry to drive cell polarity

Meiring, J. C. M., Shneyer, B. I., & Akhmanova, A. S. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.10.004 · Cited by 124

Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders

Muñoz-Lasso, D. C., Mateo, C. R., Pallardó, F. V., & González‐Cabo, P. (2020) · Cells · doi:10.3390/cells9020358 · Cited by 129

Cardiac microtubules in health and heart disease

Caporizzo, M. A., Chen, C. Y., & Prosser, B. L. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219868960 · Cited by 115

The Tubulin Detyrosination Cycle: Function and Enzymes

Nieuwenhuis, J., & Brummelkamp, T. R. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.08.003 · Cited by 110

Metabolic regulation of cytoskeleton functions by HDAC6-catalyzed α-tubulin lactylation

Sun, S., Xu, Z., He, L., Shen, Y., Yan, Y., Lv, X., Zhu, X., Li, W., Tian, W.-Y., Zheng, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52729-0 · Cited by 114

The role of microtubules in secretory protein transport

Fourrière, L., Jiménez, A. J., Perez, F., & Boncompain, G. (2020) · Journal of Cell Science · doi:10.1242/jcs.237016 · Cited by 99

Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A

Lessard, D. V., Zinder, O. J., Hotta, T., Verhey, K. J., Ohi, R., & Berger, C. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005765 · Cited by 85

Tubulin in Platelets: When the Shape Matters

Cuenca‐Zamora, E. J., Ferrer‐Marín, F., Rivera, J., & Teruel‐Montoya, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143484 · Cited by 73

Structural basis of tubulin detyrosination by vasohibins

Li, F., Hu, Y., Qi, S., Luo, X., & Yu, H. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0242-x · Cited by 68

Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes

Mahalingan, K. K., Keenan, E. K., Strickland, M., Li, Y., Liu, Y., Ball, H. L., Tanner, M. E., Tjandra, N., & Roll‐Mecak, A. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0462-0 · Cited by 70

The Joubert–Meckel–Nephronophthisis Spectrum of Ciliopathies

Weghe, J. C. V. D., Gómez, A. E., & Doherty, D. (2022) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-121321-093528 · Cited by 69

Genome-wide association for milk production traits and somatic cell score in different lactation stages of Ayrshire, Holstein, and Jersey dairy cattle

de Oliveira, H. R., Cant, J. P., Brito, L. F., Feitosa, F. L. B., Chud, T. C. S., Fonseca, P. A. D. S., Jamrozik, J., Silva, F. F., Lourenco, D. A. L., & Schenkel, F. S. (2019) · Journal of Dairy Science · doi:10.3168/jds.2019-16451 · Cited by 71

Actin-microtubule cytoskeletal interplay mediated by MRTF-A/SRF signaling promotes dilated cardiomyopathy caused by LMNA mutations

Dour, C. L., Chatzifrangkeskou, M., Macquart, C., Magiera, M. M., Peccate, C., Jouve, C., Virtanen, L., Heliö, T. M., Aalto‐Setälä, K., Crasto, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35639-x · Cited by 69

A review of research progress of antitumor drugs based on tubulin targets

Cheng, Z., Lu, X., & Feng, B. (2020) · Translational Cancer Research · doi:10.21037/tcr-20-682 · Cited by 62

Cytolinker Gas2L1 regulates axon morphology through microtubule‐modulated actin stabilization

van de Willige, D., Hummel, J. J. A., Alkemade, C., Kahn, O. I., Au, F. K. C., Qi, R. Z., Dogterom, M., Koenderink, G. H., Hoogenraad, C. C., & Akhmanova, A. S. (2019) · EMBO Reports · doi:10.15252/embr.201947732 · Cited by 64

Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex

Wang, N., Bosc, C., Choi, S. R., Boulan, B., Peris, L., Olieric, N., Bao, H., Krichen, F., Chen, L., Andrieux, A., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0241-y · Cited by 61

Cilia, neural development and disease

Suciu, S. K., & Caspary, T. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.07.014 · Cited by 61

Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation

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

Intrinsic and Extrinsic Factors Affecting Microtubule Dynamics in Normal and Cancer Cells

Borys, F., Joachimiak, E., Krawczyk, H., & Fabczak, H. (2020) · Molecules · doi:10.3390/molecules25163705 · Cited by 55

The Mechanical Role of Microtubules in Tissue Remodeling

Matis, M. (2020) · BioEssays · doi:10.1002/bies.201900244 · Cited by 53

Targeting Tubulin-colchicine Site for Cancer Therapy: Inhibitors, Antibody- Drug Conjugates and Degradation Agents

Duan, Y., Liu, W., Tian, L., Mao, Y., & Song, C. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190618130008 · Cited by 54

Microtubules and Cell Division: Potential Pharmacological Targets in Cancer Therapy

Sebastian, J., & Rathinasamy, K. (2023) · Current Drug Targets · doi:10.2174/1389450124666230731094837 · Cited by 56

Microtubule-associated protein MAP7 promotes tubulin posttranslational modifications and cargo transport to enable osmotic adaptation

Shen, Y., & Ori-McKenney, K. M. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.03.022 · Cited by 58

The synaptic life of microtubules

Waites, C. L., Qu, X., & Bartolini, F. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.03.004 · Cited by 45

Microtubule lattice plasticity

Cross, R. A. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.10.004 · Cited by 43

Human disease biomarker panels through systems biology

Smith, B. J., Silva-Costa, L. C., & Martins‐de‐Souza, D. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00849-y · Cited by 44

A tri-functional amino acid enables mapping of binding sites for posttranslational-modification-mediated protein-protein interactions

Lin, J., Bao, X., & Li, X. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.001 · Cited by 46

Post-translational modifications of tubulin: their role in cancers and the regulation of signaling molecules

Wattanathamsan, O., & Pongrakhananon, V. (2021) · Cancer Gene Therapy · doi:10.1038/s41417-021-00396-4 · Cited by 43

CSPP1 stabilizes growing microtubule ends and damaged lattices from the luminal side

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Asymmetries in the cilia of Chlamydomonas

Dutcher, S. K. (2019) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2019.0153 · Cited by 41

Cryo-EM structure of VASH1-SVBP bound to microtubules

Li, F., Li, Y., Ye, X., Gao, H., Shi, Z., Luo, X., Rice, L. M., & Yu, H. (2020) · eLife · doi:10.7554/elife.58157 · Cited by 40

Regulators of tubulin polyglutamylation control nuclear shape and cilium disassembly by balancing microtubule and actin assembly

Wang, L., Paudyal, S. C., Kang, Y., Owa, M., Liang, F., Spektor, A., Knaut, H., Sánchez, I., & Dynlacht, B. D. (2021) · Cell Research · doi:10.1038/s41422-021-00584-9 · Cited by 41

Crystal structure of VASH1-SVBP complex bound with EpoY

Li, F., Luo, X., & Yu, H. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6ocg/pdb · Cited by 39

Perfluorooctane sulfonate induces mitochondrial calcium overload and early hepatic insulin resistance via autophagy/detyrosinated alpha-tubulin-regulated IP3R2-VDAC1-MICU1 interaction

Dong, Z., Wang, J., Qiu, T., Wu, J., An, Y., Shi, X., Sun, X., Jiang, L., Liu, X., Yang, G., et al. (2022) · Science of The Total Environment · doi:10.1016/j.scitotenv.2022.153933 · Cited by 41

Tubulin tails and their modifications regulate protein diffusion on microtubules

Bigman, L. S., & Levy, Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914772117 · Cited by 35

Genetically encoded live-cell sensor for tyrosinated microtubules

Kesarwani, S., Lama, P., Chandra, A., Reddy, P. P., Jijumon, A. S., Bodakuntla, S., Rao, B. M., Janke, C., Das, R., & Sirajuddin, M. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201912107 · Cited by 37

Huntington’s Disease—An Outlook on the Interplay of the HTT Protein, Microtubules and Actin Cytoskeletal Components

Taran, A., Belikova, L. D., Lagarkova, M. A., & Alieva, I. B. (2020) · Cells · doi:10.3390/cells9061514 · Cited by 37

The tubulin code in mammalian sperm development and function

Gadadhar, S., Hirschmugl, T., & Janke, C. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.003 · Cited by 33

The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases

Iuzzolino, A., Pellegrini, F. R., Rotili, D., Degrassi, F., & Trisciuoglio, D. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05227-x · Cited by 33

Microtubule-Associated Proteins with Regulatory Functions by Day and Pathological Potency at Night

Oláh, J., Lehotzky, A., Szunyogh, S., Szénási, T., Orosz, F., & Ovádi, J. (2020) · Cells · doi:10.3390/cells9020357 · Cited by 30

Hypothalamic cell diversity: non-neuronal codes for long-distance volume transmission by neuropeptides

Alpár, A., Benevento, M., Romanov, R. A., Hökfelt, T. G. M., & Harkany, T. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.10.012 · Cited by 31

Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer

Zhou, C. Y., Yan, L., Zhang, W., & Liu, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-11277-8 · Cited by 32

Tubulin alpha-1b chain was identified as a prognosis and immune biomarker in pan-cancer combing with experimental validation in breast cancer

Wang, Y., Li, Y., Jing, Y., Yang, Y., Wang, H., Ismtula, D., & Guo, C. (2024) · Scientific Reports · doi:10.1038/s41598-024-58982-z · Cited by 36

CAMSAP2-mediated noncentrosomal microtubule acetylation drives hepatocellular carcinoma metastasis

Li, D., Ding, X., Xie, M., Huang, Z., Han, P., Tian, D., & Xia, L. (2020) · Theranostics · doi:10.7150/thno.42596 · Cited by 30

Remodeling the epigenome and (epi)cytoskeleton: a new paradigm for co-regulation by methylation

Walker, C. L., & Burggren, W. W. (2020) · Journal of Experimental Biology · doi:10.1242/jeb.220632 · Cited by 31

Macrophage migration inhibitory factor (MIF) acetylation protects neurons from ischemic injury

Hu, J., Ma, W.-J., He, L., Zhang, C.-H., Zhang, C., Wang, Y., Chen, C.-N., Shen, D., Gao, H.-M., Guo, R.-R., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04918-2 · Cited by 30

Discover 4β-NH-(6-aminoindole)-4-desoxy-podophyllotoxin with nanomolar-potency antitumor activity by improving the tubulin binding affinity on the basis of a potential binding site nearby colchicine domain

Zhao, W., He, L., Xiang, T.-L., & Ya-jie Tang, A. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.03.006 · Cited by 31

Spatial control of membrane traffic in neuronal dendrites

Radler, M. R., Suber, A., & Spiliotis, E. T. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103492 · Cited by 29

Mechanisms of Axonal Sorting of Tau and Influence of the Axon Initial Segment on Tau Cell Polarity

Zempel, H., & Mandelkow�, E. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_6 · Cited by 30

Doublecortin restricts neuronal branching by regulating tubulin polyglutamylation

Sébastien, M., Paquette, A. L., Prowse, E. N. P., Hendricks, A. G., & Brouhard, G. J. (2025) · Nature Communications · doi:10.1038/s41467-025-56951-2 · Cited by 33

Coenzyme A-aptamer-facilitated label-free electrochemical stripping strategy for sensitive detection of histone acetyltransferase activity

Hu, D., Hu, Y., Zhan, T., Zheng, Y., Ran, P., Liu, X., Guo, Z., Wei, W., & Wang, S. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.111934 · Cited by 27

Development of DNA aptamers for visualization of glial brain tumors and detection of circulating tumor cells

Kichkailo, A. S., Аркадьевич, Н. А., Komarova, M. A., Zamay, T. N., Сергеевна, З. Г., Kolovskaya, O. S., Erakhtin, E. E., Glazyrin, Y. E., Veprintsev, D. V., Moryachkov, R. V., et al. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.03.015 · Cited by 27

The emerging role of tubulin posttranslational modifications in cilia and ciliopathies

He, K., Ling, K., & Hu, J. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00111-0 · Cited by 25

A Network-Guided Approach to Discover Phytochemical-Based Anticancer Therapy: Targeting MARK4 for Hepatocellular Carcinoma

Ahmed, S., Mobashir, M., Al‐Keridis, L. A., Alshammari, N. I., Adnan, M., Abid, M., & Hassan, M. I. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.914032 · Cited by 26

MAP4 as a New Candidate in Cardiovascular Disease

Li, L., Zhang, Q., Lei, X., Huang, Y., & Hu, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01044 · Cited by 24

SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics

Feng, W., Liu, R., Xie, X., Diao, L., Gao, N., Cheng, J., Zhang, X., Li, Y., & Bao, L. (2020) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaa076 · Cited by 24

Tubulin post-translational modifications in meiosis

Akera, T. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.014 · Cited by 24

Structural basis for α-tubulin-specific and modification state-dependent glutamylation

Mahalingan, K. K., Grotjahn, D. A., Li, Y., Lander, G. C., Zehr, E. A., & Roll‐Mecak, A. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01599-0 · Cited by 23

Microtubules in Polyomavirus Infection

Horníková, L., Bruštíková, K., & Forstová, J. (2020) · Viruses · doi:10.3390/v12010121 · Cited by 23

AlphaFold2-guided engineering of split-GFP technology enables labeling of endogenous tubulins across species while preserving function

Xu, K., Li, Z., Mao, L., Guo, Z., Chen, Z., Chai, Y., Xie, C., Yang, X., Na, J., Li, W., et al. (2024) · PLOS Biology · doi:10.1371/journal.pbio.3002615 · Cited by 21

α-Tubulin detyrosination links the suppression of MCAK activity with taxol cytotoxicity

Lopes, D., Seabra, A. L., Orr, B., & Maiato, H. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205092 · Cited by 23

From Young to Old: AMPylation Hits the Brain

Sieber, S. A., Cappello, S., & Kielkowski, P. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.05.009 · Cited by 19

A new light of proteomics in cell biology and toxicology

Qiao, T., & Wang, X. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09492-6 · Cited by 22

Polyglutamylation: biology and analysis

Ruse, C. I., Chin, H. G., & Pradhan, S. (2022) · Amino Acids · doi:10.1007/s00726-022-03146-4 · Cited by 20

C-Terminal Tail Polyglycylation and Polyglutamylation Alter Microtubule Mechanical Properties

Wall, K. P., Hart, H., Lee, T., Page, C., Hawkins, T. L., & Hough, L. E. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.09.040 · Cited by 18

Peptidome analysis of cerebrospinal fluid in neonates with hypoxic-ischemic brain damage

Hou, X., Yuan, Z., Wang, X., Cheng, R., Zhou, X., & Qiu, J. (2020) · Molecular Brain · doi:10.1186/s13041-020-00671-9 · Cited by 21

Primary Cilia and Atherosclerosis

Wang, Z., Gao, X., Zhang, J., & Chen, S. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.640774 · Cited by 22

The lifecycle of the neuronal microtubule transport machinery

Twelvetrees, A. E. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.02.008 · Cited by 22

Donepezil down‐regulates propionylation, 2‐hydroxyisobutyrylation, butyrylation, succinylation, and crotonylation in the brain of bilateral common carotid artery occlusion‐induced vascular dementia rats

Wang, H., Lu, J., Gao, W., Ma, X., Li, N., Ding, Z., Wu, C., Zhu, M., Qiao, G., Xiao, C., et al. (2020) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13352 · Cited by 18

Enhanced Raman spectroscopic analysis of protein post-translational modifications

Ma, H., Han, X., & Zhao, B. (2020) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2020.116019 · Cited by 20

Interleukin-6 promotes microtubule stability in axons via Stat3 protein–protein interactions

Wareham, L. K., Echevarría, F. D., Sousa, J. L., Konlian, D. O., Dallas, G., Formichella, C. R., Sankaran, P., Goralski, P. J., Gustafson, J. R., & Sappington, R. M. (2021) · iScience · doi:10.1016/j.isci.2021.103141 · Cited by 17

Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets

Luo, J., Lam, W. H., Yu, D., Chao, V. C., Zopfi, M. N., Khoo, C. J., Zhao, C., Yan, S., Liu, Z., Li, X. D., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01406-3 · Cited by 18

Transactive Response DNA-Binding Protein (TARDBP/TDP-43) Regulates Cell Permissivity to HIV-1 Infection by Acting on HDAC6

Cabrera-Rodríguez, R., Pérez-Yanes, S., González‐Montelongo, R., Lorenzo-Salazar, J. M., Estévez‐Herrera, J., García-Luis, J., Íñigo-Campos, A., Rubio‐Rodríguez, L. A., Muñoz‐Barrera, A., Trujillo‐González, R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116180 · Cited by 18

VASH2 enhances KIF3C-mediated EGFR-endosomal recycling to promote aggression and chemoresistance of lung squamous cell carcinoma by increasing tubulin detyrosination

Wang, J., Liu, P., Zhang, R., Xing, B., Chen, G., Han, L., & Yu, J. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07155-x · Cited by 17

SPECC1L binds the myosin phosphatase complex MYPT1/PP1β and can regulate its distribution between microtubules and filamentous actin

Mehta, V., Decan, N., Ooi, S., Gaudreau-Lapierre, A., Copeland, J. W. R., & Trinkle‐Mulcahy, L. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102893 · Cited by 16

Protein Diffusion Along Protein and DNA Lattices: Role of Electrostatics and Disordered Regions

Bigman, L. S., & Levy, Y. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111622-091220 · Cited by 17

Beyond uniformity: Exploring the heterogeneous and dynamic nature of the microtubule lattice

Motta, M. R., Biswas, S., & Schaedel, L. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151370 · Cited by 18

Mitochondrial Arrest on the Microtubule Highway—A Feature of Heart Failure and Diabetic Cardiomyopathy?

Kassab, S., Albalawi, Z., Daghistani, H., & Kitmitto, A. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.689101 · Cited by 16

Transcription Factors as Targets of Natural Compounds in Age-Related Diseases and Cancer: Potential Therapeutic Applications

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Measuring the Impact of Tubulin Posttranslational Modifications on Axonal Transport

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