Evidence map›Paper›PMID 39334857›Full record

ArticleBiomolecules2024

Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis.

Ana P Carapeto, Carlos Marcuello, Patrícia F N Faísca, Mário S Rodrigues

Abstract read
In one paragraph

Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. International journal of molecular sciences · 2026
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  20. International journal of molecular sciences · 2025
    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

4 authors.

Ana P CarapetoBioISI-Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisbon, Portugal.ORCID 0000-0003-2654-6848
Carlos MarcuelloBioISI-Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisbon, Portugal.
Patrícia F N FaíscaBioISI-Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisbon, Portugal.ORCID 0000-0002-2493-2748
Mário S RodriguesBioISI-Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Campo Grande, 1749-016 Lisbon, Portugal.ORCID 0000-0002-0468-1910

Funding

Eurepean Union GA 215 10107914Fundação para a Ciência e a Tecnologia CEECIND/00031/2017/CP1387/CT0028Fundação para a Ciência e a Tecnologia UIDB/04046/2020
6 · The paper itself

Abstract

Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography. Here, we use AFM to study the aggregation process of protein S100A9 in physiological conditions, in the presence of calcium at a molar ratio 4Ca

Indexed as

AmyloidCalciumCalgranulin BMicroscopy, Atomic ForceElastic ModulusHumansProtein AggregatesAmyloidCalciumCalgranulin BProtein AggregatesS100A9 protein, humanatomic force microscopybiomolecular processesfibril topographymechanical propertiesoligomerizationprotein fibrilsS100A9

Identifiers

PMID39334857
PMCPMC11429797

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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.