Evidence map›Paper›PMID 36133101›Full record

ReviewNanoscale advances2021

Folding and self-assembly of short intrinsically disordered peptides and protein regions.

Pablo G Argudo, Juan J Giner-Casares

Abstract readReview
In one paragraph

Review in Nanoscale advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Self-Assembly of Peptides and Biomolecular Systems Into Functional Nanomaterials.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  3. Article
  4. Article
  5. Intrinsically Disordered Peptide Nanofibers from a Structured Motif Within Proteins.Angewandte Chemie (International ed. in English) · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Self-Assembling Peptides: From Design to Biomedical Applications.International journal of molecular sciences · 2021
    Review
  13. Article
  14. The "Water Problem"(Life (Basel, Switzerland) · 2021
    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.

Pablo G ArgudoUniversité de Bordeaux, CNRS, Bordeaux INP, LCPO 16 Avenue Pey-Berland 33600 Pessac France Pablo.Gomezargudo@enscbp.fr.ORCID https://orcid.org/0000-0001-5964-727X
Juan J Giner-CasaresDepartamento de Química Física y T. Aplicada, Instituto Universitario de Nanoquímica IUNAN, Facultad de Ciencias, Universidad de Córdoba (UCO) Campus de Rabanales, Ed. Marie Curie E-14071 Córdoba Spain.ORCID https://orcid.org/0000-0002-6673-300X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins and peptide fragments are highly relevant building blocks in self-assembly for nanostructures with plenty of applications. Intrinsically disordered proteins (IDPs) and protein regions (IDRs) are defined by the absence of a well-defined secondary structure, yet IDPs/IDRs show a significant biological activity. Experimental techniques and computational modelling procedures for the characterization of IDPs/IDRs are discussed. Directed self-assembly of IDPs/IDRs allows reaching a large variety of nanostructures. Hybrid materials based on the derivatives of IDPs/IDRs show a promising performance as alternative biocides and nanodrugs. Cell mimicking,

Identifiers

PMID36133101
PMCPMC9417027

What OpenQuestion holds

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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.