The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Tubulin Posttranslational Modifications and Emerging Links to Human Disease
Open accessAbstract
Tubulin posttranslational modifications are currently emerging as important regulators of the microtubule cytoskeleton and thus have a strong potential to be implicated in a number of disorders. Here, we review the latest advances in understanding the physiological roles of tubulin modifications and their links to a variety of pathologies.
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“Induction of microtubule detyrosination (removal of the C-terminal tyrosine of α-tubulin), another modification associated with microtubule stability 31 , by overexpressing the detyrosinating enzymes VASH2-SVBP or MATCAP 56-58 , either did not impact the localization of GEF-H1 to microtubules or showed a slight increase in binding (Extended Data Fig. 4b-e).”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [31]
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“However, microtubule stabilization can potentially affect microtubule-associated components of signalling cascades by altering their turnover and tubulin post-translational modifications 31 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [31]
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Citations
Cites
Genes and molecular pathways underpinning ciliopathies
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Self-citationMicrotubules acquire resistance from mechanical breakage through intralumenal acetylation
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A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration
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Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes
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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
Metadata
- Authors
- Magiera, M. M., Singh, P., Gadadhar, S., & Janke, C.
- Affiliations
- Université Paris-Sud (FR)
- Corresponding author
- Magiera, Maria M.
- Janke, Carsten
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2018-05
- Volume
- 173
- Issue
- 6
- Pages
- 1323-1327
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2807269502
- Cited by
- 169
- References
- 51
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 17 · 2023: 21 · 2022: 18 · 2021: 17 · 2020: 36 · 2019: 28 · 2018: 7
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- the French National Research Agency
- ANR (ANR-10-LBX-0038, ANR-10-IDEX-0001-02 PSL, ANR-12-BSV2-0007)
- Institut National du Cancer
- INCA (2013-1-PL BIO-02-ICR-1, 2014-PL BIO-11-ICR-1)
- EMBO (ASTF 148-2015)
- Fondation Vaincre Alzheimer (FR-16055p.)
- Ligue contre le Cancer
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tubulin post-translational modifications, microtubule cytoskeleton, tubulin acetylation, microtubule dynamics, human disease, neurodegenerative diseases, cancer
- MeSH terms
- Animals, Blood Platelets, Cilia, Cytoskeleton, Flagella, Heart Diseases, Humans, Microtubules, Mutation, Phenotype, Protein Processing, Post-Translational, Risk Factors, Tubulin, Neurodegenerative Diseases, Mice
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