Evidence map›Paper›PMID 38455030›Full record

ArticleChemical science2024

Inhibition of toxic metal-alpha synuclein interactions by human serum albumin.

Karla Martinez Pomier, Rashik Ahmed, Jinfeng Huang, Giuseppe Melacini

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

  1. In situ NMR and integrative proteomics reveal the interaction signature of serum α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. 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 at 1 institution in 1 country.

Karla Martinez PomierDepartment of Chemistry and Chemical Biology, McMaster University ON L8S 4M1 Canada melacin@mcmaster.ca.ORCID https://orcid.org/0000-0003-1411-3383
Rashik AhmedDepartment of Chemistry and Chemical Biology, McMaster University ON L8S 4M1 Canada melacin@mcmaster.ca.
Jinfeng HuangDepartment of Chemistry and Chemical Biology, McMaster University ON L8S 4M1 Canada melacin@mcmaster.ca.
Giuseppe MelaciniDepartment of Chemistry and Chemical Biology, McMaster University ON L8S 4M1 Canada melacin@mcmaster.ca.ORCID https://orcid.org/0000-0003-1164-2853
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human serum albumin (HSA), the most abundant protein in plasma and cerebrospinal fluid, not only serves as a crucial carrier of various exogenous and endogenous ligands but also modulates the aggregation of amyloidogenic proteins, including alpha synuclein (αSyn), which is associated with Parkinson's disease and other α-synucleinopathies. HSA decreases αSyn toxicity through the direct binding to monomeric and oligomeric αSyn species. However, it is possible that HSA also sequesters metal ions that otherwise promote aggregation. Cu(ii) ions, for example, enhance αSyn fibrillization

Identifiers

PMID38455030
PMCPMC10915811
OpenAlexW4391406286

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.