Evidence map›Paper›PMID 37176115›Full record

ArticleInternational journal of molecular sciences2023

Aβ40 Aggregation under Changeable Conditions.

Jofre Seira Curto, Maria Rosario Fernandez, Josep Cladera, Núria Benseny-Cases, Natalia Sanchez de Groot

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. KLVFF Functionalized Graphene Oxide for AβSmall (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. 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

5 authors at 1 institution in 1 country.

Jofre Seira CurtoUnitat de Bioquímica, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.
Maria Rosario FernandezUnitat de Bioquímica, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0002-1750-7786
Josep CladeraUnitat de Biofísica, Departament de Bioquímica i Biologia Molecular, Centre d'Estudis en Biofísica, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.
Núria Benseny-CasesUnitat de Biofísica, Departament de Bioquímica i Biologia Molecular, Centre d'Estudis en Biofísica, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.
Natalia Sanchez de GrootUnitat de Bioquímica, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0002-0492-5532
Universitat Autònoma de Barcelona · ES

Funding

Agencia de Gestión de Ayudas Universitarias y de Investigación 2022-FISDUR-0072L'Oréal-UNESCO For Women in Science Programme Spanish progamme 2021Ministerio de Ciencia e Innovacion PID2020-117454RA-I00/AEI/10.13039/501100011033Ministerio de Ciencia e Innovacion RYC2019-026752-IMinisterio de Universidades FPU21/03897
6 · The paper itself

Abstract

Homeostasis is crucial for cell function, and disturbances in homeostasis can lead to health disorders. Under normal conditions, intracellular pH is maintained between 7.35 and 7.45. Altered endosomal and lysosomal pH together with a general drop in brain pH are associated with the aggregation of amyloid-β-peptide (Aβ) and the development of Alzheimer's disease. Under acidic conditions, close to the Aβ isoelectric point, the absence of charges favors the formation of intermolecular contacts and promotes aggregation. Here, we analyzed how pH levels affect the aggregation of Aβ40 considering the variations in brain pH and the coexistence of different aggregated conformations. Our results suggest that different macromolecular conformations can interact with each other and influence the aggregation process. In addition, we showed that neutral pH and physiological salt concentrations favor a slow aggregation, resulting in ordered, stable fibrils, with low cytotoxic effects. Overall, we highlight the complexity of the aggregation processes occurring in different physiological and pathological environments.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAcidsHumansHydrogen-Ion ConcentrationMacromolecular SubstancesPeptide FragmentsAcidsAmyloid beta-PeptidesMacromolecular SubstancesPeptide Fragmentsaggregationamyloid-β-peptidecharge repulsion

Identifiers

PMID37176115
PMCPMC10179685
OpenAlexW4376631181

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.