Evidence map›Paper›PMID 25799281›Full record

ArticlePloS one2015

Flavone derivatives as inhibitors of insulin amyloid-like fibril formation.

Ricardas Malisauskas, Akvile Botyriute, Jonathan G Cannon, Vytautas Smirnovas

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
2.3field-weighted citation impact, top 12% 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, 44 citations in OpenAlex.

  1. Article
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  8. Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  9. Article
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  12. Inhibition of Protein Aggregation by Several Antioxidants.Oxidative medicine and cellular longevity · 2018
    Article
  13. Article
  14. Article
  15. Article
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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

4 authors at 3 institutions in 2 countries.

Ricardas MalisauskasDepartment of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology, Vilnius, Lithuania; Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, Vilnius, Lithuania.
Akvile BotyriuteDepartment of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology, Vilnius, Lithuania.
Jonathan G CannonDepartment of Natural Sciences and Engineering, Middle Georgia State College, Cochran, Georgia, USA.
Vytautas SmirnovasDepartment of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology, Vilnius, Lithuania.
Vilnius University · LTMiddle Georgia State College · USVilnius Gediminas Technical University · LT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several natural and synthetic flavone derivatives have been reported to inhibit formation of amyloid fibrils or to remodel existing fibrils. These studies suggest that the numbers and positions of hydroxyl groups on the flavone rings determine their effectiveness as amyloid inhibitors. In many studies the primary method for determining the effectiveness of inhibition is measuring Thioflavin T (ThT) fluorescence. This method demonstrably results in a number of false positives for inhibition. We studied the effects of 265 commercially available flavone derivatives on insulin fibril formation. We enhanced the effectiveness of ThT fluorescence measurements by fitting kinetic curves to obtain halftime of aggregation (t50). Maximal values of ThT fluorescence varied two fold or more in one third of all cases, but this did not correlate with changes in t50. Changes in t50 values were more accurate measures of inhibition of amyloid formation. We showed that without a change in an assay, but just by observing complete kinetic curves it is possible to eliminate numbers of false positive and sometimes even false negative results. Examining the data from all 265 flavones we confirmed previous observations that identified the importance of hydroxyl groups for inhibition. Our evidence suggests the importance of hydroxyl groups at locations 5, 6, 7, and 4', and the absence of a hydroxyl group at location 3, for inhibiting amyloid formation. However, the main conclusion is that the positions are not additive. The structures and their effects must be thought of in the context of the whole molecule.

Indexed as

AmyloidBenzothiazolesInsulinPolymerizationThiazolesAmyloidBenzothiazolesInsulinThiazolesthioflavin T

Identifiers

PMID25799281
PMCPMC4370379
OpenAlexW1991790682

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.