ReviewBiochemical and biophysical research communications2014
Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function.
Review in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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
43 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Cardiac complications of congenital disorders of glycosylation (CDG): a systematic review of the literature.Journal of inherited metabolic disease · 2017Pooled it
- Modulating the sialic acid content of endothelial cells affects their adhesion and barrier permeability.Scientific reports · 2026Article
- Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026Review
- SA supplementation during lactation promotes learning and memory by reducing H3K27me3 levels.Journal of advanced research · 2026Article
- Review
- Article
- Parkinson's disease-linked Kir4.2 mutation R28C leads to loss of ion channel function.The Journal of physiology · 2025Article
- Article
- Missense mutations of GPER1 in breast invasive carcinoma: Exploring gene expression, signal transduction and immune cell infiltration with insights from cellular pharmacology.Biomedical reports · 2025Article
- Article
- Cardiomyopathy, an uncommon phenotype of congenital disorders of glycosylation: Recommendations for baseline screening and follow-up evaluation.Molecular genetics and metabolism · 2024Article
- Ion channel trafficking implications in heart failure.Frontiers in cardiovascular medicine · 2024Review
- Integration of Web-Based Tools to Visualize, Integrate, and Interpret Glycogene Expression and Glycomics Data.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Review
- Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023Review
- Article
- Glycans and Carbohydrate-Binding/Transforming Proteins in Axon Physiology.Advances in neurobiology · 2023Article
- Alterations of the Sialylation Machinery in Brugada Syndrome.International journal of molecular sciences · 2022Article
- Association between Empagliflozin Use and Electrocardiographic Changes.Clinics and practice · 2022Article
- Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues.Nature communications · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Voltage-gated ion channels are transmembrane proteins that regulate electrical excitability in cells and are essential components of the electrically active tissues of nerves, muscle and the heart. Potassium channels are one of the largest subfamilies of voltage sensitive channels and are among the most-studied of the voltage-gated ion channels. Voltage-gated channels can be glycosylated and changes in the glycosylation pattern can affect ion channel function, leading to neurological and neuromuscular disorders and congenital disorders of glycosylation (CDG). Alterations in glycosylation can also be acquired and appear to play a role in development and aging. Recent studies have focused on the impact of glycosylation and sialylation on ion channels, particularly for voltage-gated potassium and sodium channels. The terminal step of sialylation often affects channel activation and inactivation kinetics. The presence of sialic acids on O or N-glycans can alter the gating mechanism and cause conformational changes in the voltage-sensing domains due to sialic acid's negative charges. This manuscript will provide an overview of sialic acids, potassium and sodium channel function, and the impact of sialylation on channel activation and deactivation.
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What OpenQuestion holds
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.