Evidence map›Paper›PMID 8897602›Full record

ArticleProtein science : a publication of the Protein Society1996

Cation selective promotion of tubulin polymerization by alkali metal chlorides.

J Wolff, D L Sackett, L Knipling

Open access · greenAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Taurine Is Covalently Incorporated into Alpha-Tubulin.Journal of proteome research · 2020
    Article
  3. Review
  4. HeLife · 2017
    Article
  5. Review
  6. Article
  7. STAQ: A route toward low power, multicolor nanoscopy.Microscopy research and technique · 2015
    Article
  8. Article
  9. Article
  10. Production of reliable MALDI spectra with quality threshold clustering of replicates.Journal of the American Society for Mass Spectrometry · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

J WolffLaboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
D L Sackett
L Knipling
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A role for charge-based interactions in protein stability at the monomer or dimer level is well known. We show here that such interactions can also be important for the higher-order structures of microtubule assembly. Alkali metal chlorides increase the rate of polymerization of pure tubulin driven by either taxol or dimethyl sulfoxide. The effect is cation selective, exhibiting a sequence Na+ > K+ > Li+ > Cs+, with optimal concentrations for Na+ at approximately 160 mM. Hofmeister anion effects are additive with these rate stimulations. Sodium is less potent than guanidinium ion stimulation reported previously, but produces a larger fraction of normal microtubules. Alkali metal cations lower the critical concentration by a factor of approximately 2, produce cold reversible polymers whose formation is sensitive to podophyllotoxin inhibition, increase the fraction of polymers present as microtubules from approximately 0.9 to 0.99, and reverse or prevent urea-induced depolymerization of microtubules. In the presence of microtubule-associated proteins, the promotion of polymerization is no longer cation selective. In the polymerization of tubulin S, in which the acidic C termini of both monomers have been cleaved, the cation enhancement is markedly decreased, although selective persists. Because the selectivity sequence is similar to that of the coil/helix transition of polyglutamic acid, we suggest that a major part, although not all, of the cation selective enhancement of polymerization results from shielding of the glutamate-rich C termini of the tubulin monomers.

Indexed as

AnimalsBiopolymersCationsCesiumChloridesDimethyl SulfoxideGuanidineGuanidinesLithium ChlorideMicrotubule-Associated ProteinsMicrotubulesPaclitaxelPeptide FragmentsPodophyllotoxinPotassium ChlorideRatsBiopolymersCationsCesiumcesium chlorideChloridesDimethyl SulfoxideGuanidineGuanidinesLithium ChlorideMicrotubule-Associated ProteinsPaclitaxelPeptide FragmentsPodophyllotoxinPotassium ChlorideSodium ChlorideTubulintubulin S

Identifiers

PMID8897602
PMCPMC2143265
OpenAlexW2119569419

What OpenQuestion holds

Textmetadata
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.