Evidence map›Paper›PMID 33748087›Full record

ReviewFrontiers in bioengineering and biotechnology2021

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.

Nicole Balasco, Carlo Diaferia, Giancarlo Morelli, Luigi Vitagliano, Antonella Accardo

Abstract readReview
In one paragraph

Review in Frontiers in bioengineering and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
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  16. Article
  17. Fluorescence Emission of Self-assembling Amyloid-like Peptides: Solution versus Solid State.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  18. Article
  19. Article
  20. 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

5 authors.

Nicole BalascoInstitute of Biostructures and Bioimaging (IBB), CNR, Naples, Italy.
Carlo DiaferiaDepartment of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", Naples, Italy.
Giancarlo MorelliDepartment of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", Naples, Italy.
Luigi VitaglianoInstitute of Biostructures and Bioimaging (IBB), CNR, Naples, Italy.
Antonella AccardoDepartment of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", Naples, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The discovery that the polypeptide chain has a remarkable and intrinsic propensity to form amyloid-like aggregates endowed with an extraordinary stability is one of the most relevant breakthroughs of the last decades in both protein/peptide chemistry and structural biology. This observation has fundamental implications, as the formation of these assemblies is systematically associated with the insurgence of severe neurodegenerative diseases. Although the ability of proteins to form aggregates rich in cross-β structure has been highlighted by recent studies of structural biology, the determination of the underlying atomic models has required immense efforts and inventiveness. Interestingly, the progressive molecular and structural characterization of these assemblies has opened new perspectives in apparently unrelated fields. Indeed, the self-assembling through the cross-β structure has been exploited to generate innovative biomaterials endowed with promising mechanical and spectroscopic properties. Therefore, this structural motif has become the

Indexed as

amino acid aggregationamyloid aggregatesbiomaterialscross-β structureglutamine rich structurespeptide-based hydrogels

Identifiers

PMID33748087
PMCPMC7966729

What OpenQuestion holds

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Registered trials

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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.