Evidence map›Paper›PMID 28122213›Full record

ArticleBiophysical journal2017

How Do Gyrating Beads Accelerate Amyloid Fibrillization?

Alireza Abdolvahabi, Yunhua Shi, Sanaz Rasouli, Corbin M Croom, Aleksandra Chuprin, Bryan F Shaw

Abstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Micro- and Nanoplastics' Effects on Protein Folding and Amyloidosis.International journal of molecular sciences · 2022
    Review
  9. Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022
    Review
  10. Article
  11. Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles.Chemistry of materials : a publication of the American Chemical Society · 2021
    Article
  12. Article
  13. Review
  14. Structure and Aggregation Mechanisms in Amyloids.Molecules (Basel, Switzerland) · 2020
    Review
  15. Acetylation of AβACS chemical neuroscience · 2020
    Article
  16. Article
  17. 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

6 authors.

Alireza AbdolvahabiDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas.
Yunhua ShiDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas.
Sanaz RasouliDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas; Institute of Biomedical Studies, Baylor University, Waco, Texas.
Corbin M CroomDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas.
Aleksandra ChuprinDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas.
Bryan F ShawDepartment of Chemistry and Biochemistry, Baylor University, Waco, Texas. Electronic address: bryan_shaw@baylor.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chemical and physical mechanisms by which gyrating beads accelerate amyloid fibrillization in microtiter plate assays are unclear. Identifying these mechanisms will help optimize high-throughput screening assays for molecules and mutations that modulate aggregation and might explain why different research groups report different rates of aggregation for identical proteins. This article investigates how the rate of superoxide dismutase-1 (SOD1) fibrillization is affected by 12 different beads with a wide range of hydrophobicity, mass, stiffness, and topology but identical diameter. All assays were performed on D90A apo-SOD1, which is a stable and wild-type-like variant of SOD1. The most significant and uniform correlation between any material property of each bead and that bead's effect on SOD1 fibrillization rate was with regard to bead mass. A linear correlation existed between bead mass and rate of fibril elongation (R

Indexed as

MicrospheresRotationAmyloidHumansHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularProtein MultimerizationProtein Structure, SecondarySuperoxide Dismutase-1AmyloidSuperoxide Dismutase-1

Identifiers

PMID28122213
PMCPMC5266089

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.