Evidence map›Paper›PMID 32093407›Full record

ArticleMolecules (Basel, Switzerland)2020

One- and Two-Electron Oxidations of β-Amyloid

Antonio Francioso, Alessia Baseggio Conrado, Carla Blarzino, Cesira Foppoli, Elita Montanari, Simone Dinarelli, Alessandra Giorgi, Luciana Mosca, Mario Fontana

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. The Peroxymonocarbonate Anion HCOMolecules (Basel, Switzerland) · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. 4,4'-Diaminodiphenyl Sulfone (DDS) as an Inflammasome Competitor.International journal of molecular sciences · 2020
    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

9 authors at 5 institutions in 3 countries.

Antonio FranciosoDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.ORCID 0000-0001-9822-0260
Alessia Baseggio ConradoDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.ORCID 0000-0001-5775-424X
Carla BlarzinoDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.
Cesira FoppoliInstitute of Molecular Biology and Pathology, CNR National Research Council-Rome, 00185 Rome, Italy.
Elita MontanariDepartment of Drug Chemistry and Technology, "Sapienza" University of Rome, 00185 Rome, Italy.
Simone DinarelliInstitute for Structure of Matter, CNR National Research Council-Rome, 00133 Rome, Italy.
Alessandra GiorgiDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.
Luciana MoscaDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.ORCID 0000-0003-2748-9021
Mario FontanaDepartment of Biochemical Sciences, "Sapienza" University of Rome, 00185 Rome, Italy.ORCID 0000-0002-7524-3395
Sapienza University of Rome · ITInstitute of Molecular Biology and Pathology · ITNational Research Council · ITUniversidad de La Laguna · ESUniversity of Dundee · GB

Funding

Sapienza Università di Roma Ateneo 2019
6 · The paper itself

Abstract

The β-amyloid (Aβ) peptide plays a key role in the pathogenesis of Alzheimer's disease. The methionine (Met) residue at position 35 in Aβ C-terminal domain is critical for neurotoxicity, aggregation, and free radical formation initiated by the peptide. The role of Met in modulating toxicological properties of Aβ most likely involves an oxidative event at the sulfur atom. We therefore investigated the one- or two-electron oxidation of the Met residue of Aβ

Indexed as

Protein AggregatesAmyloid beta-PeptidesCarbonatesFree RadicalsHumansOxidation-ReductionPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (23-35)CarbonatesFree RadicalsPeptide Fragmentsperoxycarbonic acidProtein Aggregatescarbonate radical anionmethionine sulfoxideperoxymonocarbonatereactive sulfur speciessulfur centered radicalsulfur radical cationβ-amyloid

Identifiers

PMID32093407
PMCPMC7070857
OpenAlexW3007098756

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.