Evidence map›Paper›PMID 30030591›Full record

ReviewCellular and molecular life sciences : CMLS2018

Inhibition of protein misfolding and aggregation by natural phenolic compounds.

Zohra Dhouafli, Karina Cuanalo-Contreras, El Akrem Hayouni, Charles E Mays, Claudio Soto, Ines Moreno-Gonzalez

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

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  12. Modulatory Effects ofAntioxidants (Basel, Switzerland) · 2025
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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

6 authors.

Zohra DhouafliUniversité de Tunis El Manar, Faculté des Sciences de Tunis, 2092, Tunis, Tunisia.
Karina Cuanalo-ContrerasThe Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School, University of Texas Health Science Center at Houston, 6431 Fannin Street, Houston, TX, 77030, USA.
El Akrem HayouniLaboratory of Aromatic and Medicinal Plants, Center of Biotechnology of Borj-Cédria, BP 901, 2050, Hammam-Lif, Tunisia.
Charles E MaysThe Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School, University of Texas Health Science Center at Houston, 6431 Fannin Street, Houston, TX, 77030, USA.
Claudio SotoThe Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School, University of Texas Health Science Center at Houston, 6431 Fannin Street, Houston, TX, 77030, USA.
Ines Moreno-GonzalezThe Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School, University of Texas Health Science Center at Houston, 6431 Fannin Street, Houston, TX, 77030, USA. Ines.M.Gonzalez@uth.tmc.edu.ORCID http://orcid.org/0000-0003-3875-0889

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding and aggregation into fibrillar deposits is a common feature of a large group of degenerative diseases affecting the central nervous system or peripheral organs, termed protein misfolding disorders (PMDs). Despite their established toxic nature, clinical trials aiming to reduce misfolded aggregates have been unsuccessful in treating or curing PMDs. An interesting possibility for disease intervention is the regular intake of natural food or herbal extracts, which contain active molecules that inhibit aggregation or induce the disassembly of misfolded aggregates. Among natural compounds, phenolic molecules are of particular interest, since most have dual activity as amyloid aggregation inhibitors and antioxidants. In this article, we review many phenolic natural compounds which have been reported in diverse model systems to have the potential to delay or prevent the development of various PMDs, including Alzheimer's and Parkinson's diseases, prion diseases, amyotrophic lateral sclerosis, systemic amyloidosis, and type 2 diabetes. The lower toxicity of natural compounds compared to synthetic chemical molecules suggest that they could serve as a good starting point to discover protein misfolding inhibitors that might be useful for the treatment of various incurable diseases.

Indexed as

AmyloidosisAnimalsBiological ProductsDiabetes Mellitus, Type 2HumansPhenolsPrion DiseasesProtein Aggregation, PathologicalProtein FoldingProteostasis DeficienciesBiological ProductsPhenolsAggregatesAlpha-synucleinAlzheimer’s diseaseAmylinAmyloid betaAmyloid inhibitorsFlavonoidsMisfolded proteinsNatural compoundsParkinson’s diseasePolyphenolsPrion diseasesProtein misfolding disordersTauType 2 diabetes

Identifiers

PMID30030591
PMCPMC11105286

What Socratic 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 Socratic graph.