Evidence map›Paper›PMID 31529602›Full record

ReviewAngewandte Chemie (International ed. in English)2020

Peptide-Based Molecular Strategies To Interfere with Protein Misfolding, Aggregation, and Cell Degeneration.

Valentina Armiento, Anna Spanopoulou, Aphrodite Kapurniotu

Open access · hybridAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

41 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Review
  4. Polymer conformational entropy as the driver of complex coacervation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  19. Article
  20. AβACS chemical neuroscience · 2023
    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

3 authors at 1 institution in 1 country.

Valentina ArmientoDivision of Peptide Biochemistry, TUM School of Life Sciences, Technische Universität München, Emil-Erlenmeyer-Forum 5, 85354, Freising, Germany.
Anna SpanopoulouDivision of Peptide Biochemistry, TUM School of Life Sciences, Technische Universität München, Emil-Erlenmeyer-Forum 5, 85354, Freising, Germany.
Aphrodite KapurniotuDivision of Peptide Biochemistry, TUM School of Life Sciences, Technische Universität München, Emil-Erlenmeyer-Forum 5, 85354, Freising, Germany.ORCID 0000-0001-6124-7232
Technical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding into amyloid fibrils is linked to more than 40 as yet incurable cell- and neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and type 2 diabetes. So far, however, only one of the numerous anti-amyloid molecules has reached patients. This Minireview gives an overview of molecular strategies and peptide chemistry "tools" to design, develop, and discover peptide-based molecules as anti-amyloid drug candidates. We focus on two major inhibitor rational design strategies: 1) the oldest and most common strategy, based on molecular recognition elements of amyloid self-assembly, and 2) a more recent approach, based on cross-amyloid interactions. We discuss why peptide-based amyloid inhibitors, in particular their advanced generations, can be promising leads or candidates for anti-amyloid drugs as well as valuable tools for deciphering amyloid-mediated cell damage and its link to disease pathogenesis.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesDiabetes Mellitus, Type 2Drug DesignHumansPeptidesProtein AggregatesProtein FoldingAmyloidAmyloid beta-PeptidesPeptidesProtein AggregatesAlzheimer's diseaseamyloid inhibitorsanti-amyloid drugspeptidesprotein aggregation

Identifiers

PMID31529602
PMCPMC7064928
OpenAlexW2973598512

What OpenQuestion holds

Textmetadata
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.