ArticleThe Biochemical journal2002
Association of brain gamma-tubulins with alpha beta-tubulin dimers.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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.
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Who cites it
11 citing papers in PubMed, 42 citations in OpenAlex.
- γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022Review
- Review
- γ-Tubulin Complexes and Fibrillar Arrays: Two Conserved High Molecular Forms with Many Cellular Functions.Cells · 2021Review
- TUBG1 missense variants underlying cortical malformations disrupt neuronal locomotion and microtubule dynamics but not neurogenesis.Nature communications · 2019Article
- Review
- Mast Cell Activation and Microtubule Organization Are Modulated by Miltefosine Through Protein Kinase C Inhibition.Frontiers in immunology · 2018Article
- Regulation of microtubule nucleation mediated by γ-tubulin complexes.Protoplasma · 2017Review
- Cytoskeleton in mast cell signaling.Frontiers in immunology · 2012Article
- γ-Tubulin 2 nucleates microtubules and is downregulated in mouse early embryogenesis.PloS one · 2012Article
- Class III beta-tubulin and gamma-tubulin are co-expressed and form complexes in human glioblastoma cells.Neurochemical research · 2007Article
- Plant gamma-tubulin interacts with alphabeta-tubulin dimers and forms membrane-associated complexes.The Plant cell · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
gamma-Tubulin is necessary for nucleation and polar orientation of microtubules in vivo. The molecular mechanism of microtubule nucleation by gamma-tubulin and the regulation of this process are not fully understood. Here we show that there are two gamma-tubulin forms in the brain that are present in complexes of various sizes. Large complexes tend to dissociate in the presence of a high salt concentration. Both gamma-tubulins co-polymerized with tubulin dimers, and multiple gamma-tubulin bands were identified in microtubule protein preparations under conditions of non-denaturing electrophoresis. Immunoprecipitation experiments with monoclonal antibodies against gamma-tubulin and alpha-tubulin revealed interactions of both gamma-tubulin forms with tubulin dimers, irrespective of the size of complexes. We suggest that, besides small and large gamma-tubulin complexes, other molecular gamma-tubulin form(s) exist in brain extracts. Two-dimensional electrophoresis revealed multiple charge variants of gamma-tubulin in both brain extracts and microtubule protein preparations. Post-translational modification(s) of gamma-tubulins might therefore have an important role in the regulation of microtubule nucleation in neuronal cells.
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Registered trials
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.