Evidence map›Paper›PMID 32213585›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy.

Hiroki Konno, Takahiro Watanabe-Nakayama, Takayuki Uchihashi, Momoko Okuda, Liwen Zhu, Noriyuki Kodera, Yousuke Kikuchi, Toshio Ando, Hideki Taguchi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024
    Review
  9. Article
  10. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. A new fibrillization mechanism of β-lactoglobulin in glycine solutions.International journal of biological macromolecules · 2022
    Article
  16. Article
  17. Review
  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

9 authors.

Hiroki KonnoWorld Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
Takahiro Watanabe-NakayamaWorld Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
Takayuki UchihashiDepartment of Physics, Nagoya University, 464-8602 Nagoya, Japan.ORCID 0000-0002-0263-5312
Momoko OkudaSchool of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, 226-8503 Yokohama, Japan.
Liwen ZhuImaging Research Division, Bio-Atomic Force Microscopy Frontier Research Center, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.
Noriyuki KoderaWorld Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan.ORCID 0000-0003-4880-8423
Yousuke KikuchiSchool of Natural System, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa, 920-1192 Ishikawa, Japan.
Toshio AndoWorld Premier International Research Center Initiative Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa-shi, 920-1192 Ishikawa, Japan; tando@staff.kanazawa-u.ac.jp taguchi@bio.titech.ac.jp.ORCID 0000-0001-8819-154X
Hideki TaguchiSchool of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, 226-8503 Yokohama, Japan; tando@staff.kanazawa-u.ac.jp taguchi@bio.titech.ac.jp.ORCID 0000-0002-6612-9339

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast prion protein Sup35, which contains intrinsically disordered regions, forms amyloid fibrils responsible for a prion phenotype [

Indexed as

Microscopy, Atomic ForceAmyloidPeptide Termination FactorsPrion ProteinsProtein Conformation, beta-StrandProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidPeptide Termination FactorsPrion ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeamyloidhigh-speed AFMintrinsically disordered proteinssup35yeast prion

Identifiers

PMID32213585
PMCPMC7149427

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.