Evidence map›Paper›PMID 26503463›Full record

ArticleScientific reports2015

Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering.

Eri Chatani, Rintaro Inoue, Hiroshi Imamura, Masaaki Sugiyama, Minoru Kato, Masahide Yamamoto, Koji Nishida, Toshiji Kanaya

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Carbon dots as a versatile tool to monitor insulin aggregation.Analytical and bioanalytical chemistry · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. 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

8 authors at 5 institutions in 1 country.

Eri ChataniDepartment of Chemistry, Graduate School of Science, Kobe University, Hyogo 657-8501, Japan.
Rintaro InoueResearch Reactor Institute, Kyoto University, Osaka 590-0494, Japan.
Hiroshi ImamuraCollege of Pharmaceutical Science, Ritsumeikan University, Shiga 525-8577, Japan.
Masaaki SugiyamaResearch Reactor Institute, Kyoto University, Osaka 590-0494, Japan.
Minoru KatoCollege of Pharmaceutical Science, Ritsumeikan University, Shiga 525-8577, Japan.
Masahide YamamotoKyoto University, Kyoto 606-8501, Japan.
Koji NishidaInstitute for Chemical Research, Kyoto University, Kyoto 611-0011, Japan.
Toshiji KanayaInstitute for Chemical Research, Kyoto University, Kyoto 611-0011, Japan.
Kyoto University Institute for Chemical ResearchKyoto University Research Reactor Institute · JPRitsumeikan University · JPKobe University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nucleation event of amyloid fibrils is one of the most crucial processes that dictate the timing and rate of the pathology of diseases; however, information regarding how protein molecules associate to produce fibril nuclei is currently limited. In order to explore this issue in more detail, we performed time-resolved small angle X-ray scattering (SAXS) measurements on insulin fibrillation, in combination with additional multidirectional analyses of thioflavin T fluorescence, FTIR spectroscopy, light scattering, and light transmittance, during the fibrillation process of bovine insulin. SAXS monitoring revealed that insulin molecules associated into rod-like prefibrillar aggregates in the very early stage of the reaction. After the formation of these early aggregates, they appeared to further coalesce mutually to form larger clusters, and the SAXS profiles subsequently showed the further time evolution of conformational development towards mature amyloid fibrils. Distinct types of structural units in terms of shape in a nano-scale order, cross-β content, and thioflavin T fluorescence intensity were observed in a manner that was dependent on the fibrillation pathways. These results suggest the presence of diverse substructures that characterize various fibrillation pathways, and eventually, manifest polymorphisms in mature amyloid fibrils.

Indexed as

InsulinScattering, RadiationX-Ray DiffractionInsulin

Identifiers

PMID26503463
PMCPMC4621412
OpenAlexW2304355334

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.