ReviewArchives of pharmacal research2019
Palmitoylation-mediated synaptic regulation of AMPA receptor trafficking and function.
Review in Archives of pharmacal research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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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.
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.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Posttranslational modifications of AMPA receptors in synaptic function and memory.Cellular and molecular life sciences : CMLS · 2026Review
- Diet, Metabolism and Synaptic Function: Integrating Evidence Across Models in Neurodegeneration Research.Biomedicines · 2026Review
- Review
- Influence of palmitoylation in axonal transport mechanisms in neurodegenerative diseases.Frontiers in cellular neuroscience · 2025Review
- Palmitoylation of synaptic proteins: roles in functional regulation and pathogenesis of neurodegenerative diseases.Cellular & molecular biology letters · 2024Review
- Roles of AMPA receptors in social behaviors.Frontiers in synaptic neuroscience · 2024Review
- Integrating metabolomics and lipidomics revealed a decrease in plasma fatty acids but an increase in triglycerides in children with drug-refractory epilepsy.Epilepsia open · 2023Article
- S-Palmitoylation of Synaptic Proteins in Neuronal Plasticity in Normal and Pathological Brains.Cells · 2023Review
- The role of s-palmitoylation in neurological diseases: implication for zDHHC family.Frontiers in pharmacology · 2023Review
- Fatty Acids: An Insight into the Pathogenesis of Neurodegenerative Diseases and Therapeutic Potential.International journal of molecular sciences · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Article
- S-Palmitoylation of Synaptic Proteins as a Novel Mechanism Underlying Sex-Dependent Differences in Neuronal Plasticity.International journal of molecular sciences · 2021Article
- Saturated free fatty acids and association with memory formation.Nature communications · 2021Article
- Roles of palmitoylation in structural long-term synaptic plasticity.Molecular brain · 2021Review
- Protein S-Palmitoylation and Lung Diseases.Advances in experimental medicine and biology · 2021Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) is a major glutamate-gated ion channel in the brain and is important for synaptic transmission, synaptic plasticity, and learning. Palmitoylation, a post-translational modification, is a critical process regulating AMPAR trafficking, synaptic function and plasticity, and learning and memory in health and diseases. In this review, we discuss current knowledge on the palmitoylation-dependent regulation of AMPAR trafficking and functions. We focus on the palmitoylation of AMPARs and other synaptic proteins that directly or indirectly interact with AMPARs, including postsynaptic density 95, glutamate receptor-interacting protein/AMPAR-binding protein, A-kinase anchoring protein 79/150, and protein interacting with C kinase 1. Finally, we discuss what future studies should address in the field of palmitoylation-dependent AMPAR trafficking and function with regard to physiology and neurodegenerative diseases.
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Registered trials
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.