Evidence map›Paper›PMID 31652491›Full record

ArticleCells2019

Tubulin: Structure, Functions and Roles in Disease.

Pavla Binarová, Jack Tuszynski

Open access · goldAbstract readEditorial
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

83 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
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  6. Review
  7. Flavonoids as colchicine binding site inhibitors: emerging scaffolds in anticancer drug design.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
  8. Review
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  14. Expanding the Clinical and Molecular Spectrum ofmedRxiv : the preprint server for health sciences · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Scaffold-Hopping Design and Synthesis of Thieno[3,2-International journal of molecular sciences · 2025
    Article
  19. Article
  20. Article

23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 3 countries.

Pavla BinarováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 142 20, Czech Republic. binarova@biomed.cas.cz.ORCID 0000-0002-7203-2250
Jack TuszynskiDIMEAS, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Torino, Italy. jack.tuszynski@gmail.com.
Czech Academy of Sciences · CZUniversity of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Highly conserved α- and β-tubulin heterodimers assemble into dynamic microtubules and perform multiple important cellular functions such as structural support, pathway for transport and force generation in cell division. Tubulin exists in different forms of isotypes expressed by specific genes with spatially- and temporally-regulated expression levels. Some tubulin isotypes are differentially expressed in normal and neoplastic cells, providing a basis for cancer chemotherapy drug development. Moreover, specific tubulin isotypes are overexpressed and localized in the nuclei of cancer cells and/or show bioenergetic functions through the regulation of the permeability of mitochondrial ion channels. It has also become clear that tubulin isotypes are involved in multiple cellular functions without being incorporated into microtubule structures. Understanding the mutations of tubulin isotypes specifically expressed in tumors and their post-translational modifications might help to identify precise molecular targets for the design of novel anti-microtubular drugs. Knowledge of tubulin mutations present in tubulinopathies brings into focus cellular functions of tubulin in brain pathologies such as Alzheimer's disease. Uncovering signaling pathways which affect tubulin functions during antigen-mediated activation of mast cells presents a major challenge in developing new strategies for the treatment of inflammatory and allergic diseases. γ-tubulin, a conserved member of the eukaryotic tubulin superfamily specialized for microtubule nucleation is a target of cell cycle and stress signaling. Besides its microtubule nucleation role, γ-tubulin functions in nuclear and cell cycle related processes. This special issue "Tubulin: Structure, Functions and Roles in Disease" contains eight articles, five of which are original research papers and three are review papers that cover diverse areas of tubulin biology and functions under normal and pathological conditions.

Indexed as

Alzheimer DiseaseAnimalsHumansMicrotubulesMutationNeoplasm ProteinsNeoplasmsProtein IsoformsTubulinNeoplasm ProteinsProtein IsoformsTubulincancer regulationchemotherapy drugsisoformsmicrotubulestubulin

Identifiers

PMID31652491
PMCPMC6829893
OpenAlexW2981181140

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.