Evidence map›Paper›PMID 37884348›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2023

Loss of Depalmitoylation Disrupts Homeostatic Plasticity of AMPARs in a Mouse Model of Infantile Neuronal Ceroid Lipofuscinosis.

Kevin P Koster, Eden Flores-Barrera, Emilce Artur de la Villarmois, Adriana Caballero, Kuei Y Tseng, Akira Yoshii

Open access · greenAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. Reversible synaptic deficits in early-stage batten disease.Journal of translational medicine · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Palmitoylation in cardiovascular diseases: Molecular mechanism and therapeutic potential.International journal of cardiology. Heart & vasculature · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. 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

6 authors at 1 institution in 1 country.

Kevin P KosterDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612 kpkoster@uchicago.edu.ORCID 0000-0003-2935-3427
Eden Flores-BarreraDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612.ORCID 0000-0003-4912-3741
Emilce Artur de la VillarmoisDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612.
Adriana CaballeroDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612.
Kuei Y TsengDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612.
Akira YoshiiDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612.
University of Illinois Chicago · US

Funding

Monoaminergic regulation of prefrontal cortex inhibition during adolescenceR01MH086507 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI Kuei-Yuan Tseng · 2010 to 2026
$5.7M
Alzheimer's Disease: simultaneous modulation of NMDAR, BACE1, APP and Fyn activity by palmitoylation-targeting CIRC825R43AG072984 · NIA · CIRCUMVENT PHARMACEUTICALS, INC. · PI WILEY, DEVIN THOMAS · 2021 to 2021
$507k
NIA NIH HHS R43 AG072984NIMH NIH HHS R01 MH086507
6 · The paper itself

Abstract

Protein palmitoylation is the only reversible post-translational lipid modification. Palmitoylation is held in delicate balance by depalmitoylation to precisely regulate protein turnover. While over 20 palmitoylation enzymes are known, depalmitoylation is conducted by fewer enzymes. Of particular interest is the lack of the depalmitoylating enzyme palmitoyl-protein thioesterase 1 (PPT1) that causes the devastating pediatric neurodegenerative condition infantile neuronal ceroid lipofuscinosis (CLN1). While most of the research on Ppt1 function has centered on its role in the lysosome, recent findings demonstrated that many Ppt1 substrates are synaptic proteins, including the AMPA receptor (AMPAR) subunit GluA1. Still, the impact of Ppt1-mediated depalmitoylation on synaptic transmission and plasticity remains elusive. Thus, the goal of the present study was to use the

Indexed as

Neuronal Ceroid-LipofuscinosesReceptors, AMPAAnimalsChildDisease Models, AnimalFemaleHomeostasisHumansLipidsMaleMiceNeuronal PlasticityThiolester HydrolasesLipidsReceptors, AMPAThiolester HydrolasesAMPARdepalmitoylationGluA1homeostatic plasticitypalmitoylationsynchrony

Identifiers

PMID37884348
PMCPMC10711723
OpenAlexW4387965691

What OpenQuestion holds

Textmetadata
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.