Evidence map›Paper›PMID 27381175›Full record

ArticleScientific reports2016

New insight into the dynamical system of αB-crystallin oligomers.

Rintaro Inoue, Takumi Takata, Norihiko Fujii, Kentaro Ishii, Susumu Uchiyama, Nobuhiro Sato, Yojiro Oba, Kathleen Wood, Koichi Kato, Noriko Fujii and 1 more

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  8. Article
  9. Review
  10. Article
  11. The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Article
  14. Article
  15. The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020
    Review
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

11 authors.

Rintaro InoueResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.
Takumi TakataResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.
Norihiko FujiiTeikyo Univ., Radioisotope Res. Ctr, Kaga Itabashi Ku, Tokyo, 173-8605, Japan.
Kentaro IshiiOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
Susumu UchiyamaOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
Nobuhiro SatoResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.
Yojiro ObaResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.
Kathleen WoodAustralian Nuclear Science and Technology Organization, Lucas Heights, NSW Australia.
Koichi KatoOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki 444-8787, Japan.
Noriko FujiiResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.
Masaaki SugiyamaResearch Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Crystallin possesses a dynamic quaternary structure mediated by its subunit dynamics. Elucidation of a mechanism of subunit dynamics in homo-oligomers of αB-crystallin was tackled through deuteration-assisted small-angle neutron scattering (DA-SANS) and electrospray ionization (ESI) native mass spectrometry (nMS). The existence of subunit exchange was confirmed with DA-SANS, and monomers liberated from the oligomers were observed with nMS. With increasing temperature, an increase in both the exchange rate and monomer population was observed despite the absence of oligomer collapse. It is proposed that transiently liberated subunits, namely, "traveling subunits," play a role in subunit exchange. Moreover, we propose that protein function is regulated by these traveling subunits.

Identifiers

PMID27381175
PMCPMC4933968

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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.