Evidence map›Paper›PMID 20668689›Full record

ArticlePloS one2010

Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin.

Scott A Houck, John I Clark

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Abnormal mitosis in reactive astrocytes.Acta neuropathologica communications · 2020
    Article
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  13. Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  14. Article
  15. Article
  16. 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

2 authors at 2 institutions in 1 country.

Scott A HouckMedicine Administration, University of North Carolina, Chapel Hill, North Carolina, United States of America.
John I Clark
University of North Carolina at Chapel Hill · USUniversity of Washington · US

Funding

DEVELOPMENT AND MAINTENANCE OF TRANSPARENCY IN LENSESR01EY004542 · NEI · UNIVERSITY OF WASHINGTON · PI CLARK, JOHN IRWIN · 1985 to 2013
$7.1M
NEI NIH HHS EY04542NEI NIH HHS R01 EY004542
6 · The paper itself

Abstract

backgroundThe small heat shock protein (sHSP), human alphaB crystallin, forms large, polydisperse complexes that modulate the tubulin-microtubule equilibrium using a dynamic mechanism that is poorly understood. The interactive sequences in alphaB crystallin for tubulin are surface exposed, and correspond to interactive sites for the formation of alphaB crystallin complexes. METHODOLOGY/PRINCIPAL

findingsThere is sequence homology between tubulin and the interactive domains in the beta8-strand of the core domain and the C-terminal extension of alphaB crystallin. This study investigated the hypothesis that the formation of tubulin and alphaB crystallin quaternary structures was regulated through common interactive domains that alter the dynamics of their assembly. Size exclusion chromatography (SEC), SDS-PAGE, microtubule assembly assays, aggregation assays, multiple sequence alignment, and molecular modeling characterized the dynamic response of tubulin assembly to increasing concentrations of alphaB crystallin. Low molar ratios of alphaB crystallin:tubulin were favorable for microtubule assembly and high molar ratios of alphaB crystallin:tubulin were unfavorable for microtubule assembly. Interactions between alphaB crystallin and unassembled tubulin were observed using SEC and SDS-PAGE. CONCLUSIONS/SIGNIFICANCE: Subunits of alphaB crystallin that exchange dynamically with the alphaB crystallin complex can interact with tubulin subunits to regulate the equilibrium between tubulin and microtubules.

Indexed as

alpha-Crystallin B ChainAmino Acid SequenceChromatography, GelHumansMicrotubulesModels, BiologicalMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidTubulinalpha-Crystallin B ChainTubulin

Identifiers

PMID20668689
PMCPMC2909917
OpenAlexW2064983936

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.