Evidence map›Paper›PMID 41708000›Full record

ReviewThe Journal of biological chemistry2026

Sialylation in the nervous system: Functions and mechanisms.

Kate Koles, Elena Repnikova, Boris Novikov, Vladislav Panin

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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.

Kate KolesDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
Elena RepnikovaDepartment of Pathology and Laboratory Medicine, Children's Mercy Kansas City and University of Missouri-Kansas City School of Medicine, Kansas City, Missouri, USA.
Boris NovikovDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
Vladislav PaninDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA. Electronic address: panin@tamu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoprotein sialylation represents a critical posttranslational modification with diverse biological roles in animals. This review explores its multifaceted functions in the nervous system, with particular emphasis on neurophysiology, homeostasis, and associated neurological disorders. The sialylation pathway modulates key neural processes through effects on glycoprotein stability, localization, activity, and molecular interactions. Examples include its crucial role in the regulation of neuronal excitability by modulating the functions of voltage-gated ion channels. Recent studies have uncovered remarkably rapid, activity-dependent changes in synaptic sialylation, suggesting dynamic sialylation-mediated regulation of neural transmission and highlighting the importance of neuraminidases in these processes. Beyond synaptic function, sialylation mediates neuron-glia interactions through multiple mechanisms. It modulates immune functions regulated by siglecs and complement pathways while controlling microglial activation and neuroinflammation. The critical importance of proper sialylation is underscored by severe neurological manifestations associated with genetic defects in the sialylation pathway, including cognitive impairment, ataxia, and epilepsy. Furthermore, aberrant sialylation of glycoproteins and gangliosides has been implicated in neurodegenerative diseases (Alzheimer's and Parkinson's), brain cancers, and psychiatric disorders including schizophrenia and autism. Preclinical research has identified promising therapeutic strategies targeting sialylation. Studies demonstrate that polysialic acid administration reduces neurodegeneration, while siglec modulation alleviates age-related cognitive decline. Recent discoveries, including sialylated glycoRNA and insights from Drosophila models revealing unique sialylation-mediated glia-neuron crosstalk, have significantly expanded our understanding of this important regulatory system. These advances position sialylation as a promising therapeutic target for neurological disorders.

Indexed as

GlycoproteinsN-Acetylneuraminic AcidNervous SystemSialic AcidsAnimalsHumansNervous System DiseasesNeuronsProtein Processing, Post-TranslationalGlycoproteinsN-Acetylneuraminic AcidSialic Acidsglycosylationnervous systemneurodegenerationneurological disordersneurotransmissionsialic acidsialylation

Identifiers

PMID41708000
PMCPMC13010963

What OpenQuestion holds

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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.