ArticleMolecular biology of the cell1993
Dynamics of microtubules from erythrocyte marginal bands.
Article in Molecular biology of the cell, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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.
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Who cites it
9 citing papers in PubMed, 46 citations in OpenAlex.
- Microtubule minus-end stability is dictated by the tubulin off-rate.The Journal of cell biology · 2019Article
- Structure and Dynamics of Single-isoform Recombinant Neuronal Human Tubulin.The Journal of biological chemistry · 2016Article
- Article
- Microtubule assembly of isotypically purified tubulin and its mixtures.Biophysical journal · 2008Article
- Models of assembly and disassembly of individual microtubules: stochastic and averaged equations.Journal of biological physics · 1999Article
- Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules.Molecular biology of the cell · 1996Article
- Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules.Molecular biology of the cell · 1995Article
- The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice.The Journal of cell biology · 1994Article
- A model of microtubule oscillations.European biophysics journal : EBJ · 1994Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules can adjust their length by the mechanism of dynamic instability, that is by switching between phases of growth and shrinkage. Thus far this phenomenon has been studied with microtubules that contain several components, that is, a mixture of tubulin isoforms, with or without a mixture of microtubule-associated proteins (MAPs), which can act as regulators of dynamic instability. Here we concentrate on the influence of the tubulin component. We have studied MAP-free microtubules from the marginal band of avian erythrocytes and compared them with mammalian brain microtubules. The erythrocyte system was selected because it represents a naturally stable aggregate of microtubules; second, the tubulin is largely homogeneous, in contrast to brain tubulin. Qualitatively, erythrocyte microtubules show similar features as brain microtubules, but they were found to be much less dynamic. The critical concentration of elongation, and the rates of association and dissociation of tubulin are all lower than with brain microtubules. Catastrophes are rare, rescues frequent, and shrinkage slow. This means that dynamic instability can be controlled by the tubulin isotype, independently of MAPs. Moreover, the extent of dynamic behavior is highly dependent on buffer conditions. In particular, dynamic instability is strongly enhanced in phosphate buffer, both for erythrocyte marginal band and brain microtubules. The lower stability in phosphate buffer argues against the hypothesis that a cap of tubulin.GDP.Pi subunits stabilizes microtubules. The difference in dynamics between tubulin isotypes and between the two ends of microtubules is preserved in the different buffer systems.
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