Evidence map›Paper›PMID 30828498›Full record

ArticlePeerJ2019

Emergence of visible light optical properties of L-phenylalanine aggregates.

Mantas Ziaunys, Vytautas Smirnovas

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

2 authors at 1 institution in 1 country.

Mantas ZiaunysVilnius University, Life Sciences Center, Institute of Biotechnology, Vilnius, Lithuania.
Vytautas SmirnovasVilnius University, Life Sciences Center, Institute of Biotechnology, Vilnius, Lithuania.ORCID 0000-0002-1829-5455
Vilnius University · LT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of phenylalanine to form fibrillar nanostructures was demonstrated on multiple occasions, and such an oligomerization reaction could be the cause of cytotoxicity in patients with phenylketonuria. These findings were supported by claims that L-phenylalanine (Phe) fibrils have amyloid properties and can be detected using thioflavin T fluorescence assay. However, a part of Phe aggregation studies reported the opposite data, suggesting no amyloid structures to be formed. Due to the contradicting reports, the amyloid nature of Phe aggregates remains uncertain. In this work we tested Phe aggregation under conditions where amyloid formation was previously reported. We show the emergence of Phe aggregates with visible light optical properties that overlap with the spectra of dyes used in amyloid fibril assays, which could lead to false-positive identifications.

Indexed as

AggregationAmyloidPhenylalanineSpectroscopy

Identifiers

PMID30828498
PMCPMC6394350
OpenAlexW2917207907

What OpenQuestion holds

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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.