Evidence map›Paper›PMID 36466161›Full record

ReviewFrontiers in neuroscience2022

How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?

Aditya Iyer, Arshdeep Sidhu, Vinod Subramaniam

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in neuroscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
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  8. ZnJournal of the American Chemical Society · 2025
    Article
  9. Review
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  11. Article
  12. Review
  13. Alpha Synuclein: Neurodegeneration and Inflammation.International journal of molecular sciences · 2023
    Review
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

3 authors at 3 institutions in 2 countries.

Aditya IyerDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.
Arshdeep SidhuNitte University Centre for Science Education and Research, Nitte University (DU), Mangalore, India.
Vinod SubramaniamUniversity of Twente, Enschede, Netherlands.
Nitte University · INUniversity of Groningen · NLUniversity of Twente · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-α-acetylation is a frequently occurring post-translational modification in eukaryotic proteins. It has manifold physiological consequences on the regulation and function of several proteins, with emerging studies suggesting that it is a global regulator of stress responses. For decades,

Indexed as

acetylationalpha-synucleinfibril structurepost-translational modificationsprotein aggregation

Identifiers

PMID36466161
PMCPMC9709446
OpenAlexW4309312361

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.