Evidence map›Paper›PMID 23242152›Full record

ReviewInternational journal of molecular sciences2012

Natural biomolecules and protein aggregation: emerging strategies against amyloidogenesis.

Antonella Sgarbossa

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  6. Review
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  13. Article
  14. Oligomerization Alters Binding Affinity Between Amyloid Beta and a Modulator of Peptide Aggregation.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017
    Article
  15. Review
  16. Article
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  18. 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

1 author at 1 institution in 1 country.

Antonella SgarbossaInstitute of Biophysics, CNR, Italian National Research Council, Via G. Moruzzi 1, 56124 Pisa, Italy. antonella.sgarbossa@pi.ibf.cnr.it.
Istituto di Scienza e Tecnologie dell'Informazione "Alessandro Faedo" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular self-assembly is a fundamental process in all organisms. As primary components of the life molecular machinery, proteins have a vast array of resources available to them for self-assembly in a functional structure. Protein self-assembly, however, can also occur in an aberrant way, giving rise to non-native aggregated structures responsible for severe, progressive human diseases that have a serious social impact. Different neurodegenerative disorders, like Huntington's, Alzheimer's, and spongiform encephalopathy diseases, have in common the presence of insoluble protein aggregates, generally termed "amyloid," that share several physicochemical features: a fibrillar morphology, a predominantly beta-sheet secondary structure, birefringence upon staining with the dye Congo red, insolubility in common solvents and detergents, and protease resistance. Conformational constrains, hydrophobic and stacking interactions can play a key role in the fibrillogenesis process and protein-protein and peptide-peptide interactions-resulting in self-assembly phenomena of peptides yielding fibrils-that can be modulated and influenced by natural biomolecules. Small organic molecules, which possess both hydrophilic and hydrophobic moieties able to bind to peptide/protein molecules through hydrogen bonds and hydrophobic and aromatic interactions, are potential candidates against amyloidogenesis. In this review some significant case examples will be critically discussed.

Indexed as

AmyloidosisNeurodegenerative DiseasesAmyloidAnimalsHumansHydrophobic and Hydrophilic InteractionsPolyphenolsProtein Structure, SecondaryAmyloidPolyphenols

Identifiers

PMID23242152
PMCPMC3546742
OpenAlexW2022570509

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.