Evidence map›Paper›PMID 33758258›Full record

ArticleScientific reports2021

The nickel-chelator dimethylglyoxime inhibits human amyloid beta peptide in vitro aggregation.

Stéphane L Benoit, Robert J Maier

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
  2. Review
  3. Computational Study of AmyloidβInorganic chemistry · 2024
    Article
  4. Article
  5. Peptide-Based Materials That Exploit Metal Coordination.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. 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

2 authors at 1 institution in 1 country.

Stéphane L BenoitDepartment of Microbiology, The University of Georgia, 805 Biological Sciences Bldg, Athens, GA, 30602, USA.
Robert J MaierDepartment of Microbiology, The University of Georgia, 805 Biological Sciences Bldg, Athens, GA, 30602, USA. rmaier@uga.edu.
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the hallmarks of the most common neurodegenerative disease, Alzheimer's disease (AD), is the extracellular deposition and aggregation of Amyloid Beta (Aβ)-peptides in the brain. Previous studies have shown that select metal ions, most specifically copper (Cu) and zinc (Zn) ions, have a synergistic effect on the aggregation of Aβ-peptides. In the present study, inductively coupled plasma mass spectrometry (ICP-MS) was used to determine the metal content of a commercial recombinant human Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesChelating AgentsCopperDose-Response Relationship, DrugDrug DiscoveryHumansMetalsNickelOximesProtein AggregatesProtein Aggregation, PathologicalZincAmyloid beta-PeptidesChelating AgentsCopperdimethylglyoximeMetalsNickelOximesProtein AggregatesZinc

Identifiers

PMID33758258
PMCPMC7988135
OpenAlexW3136999198

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.