MGO-Glycation Targets: 494 Proteins Linked to RNA Mis-Splicing

494 proteins were identified as targets of methylglyoxal glycation using a quantitative chemoproteomic approach. The dataset, authored by Yang Xiao and updated in 2026, focuses on the serine/arginine-rich splicing factor 2 (SRSF2), linking site-specific glycation to altered RNA binding and splicing defects. This work provides evidence for a mechanistic link between MGO-glycation and diseases like cancer and neurodegeneration.

Use Cases

• Identify potential protein targets of metabolic glycation based on the list of 494 glycated proteins.
• Investigate the role of glycation in RNA processing pathways, as suggested by the dataset's focus.
• Model the biophysical impact of site-specific glycation on protein-RNA interactions, referencing the study on SRSF2.
• Explore mechanistic links between reactive metabolites and disease progression through mis-splicing events.

Strengths

• Contains a specific list of 494 protein targets identified through chemoproteomic profiling.
• Focuses on a detailed case study of SRSF2, including experimentally corroborated sites of modification.
• Provides a direct link between a specific modification (MGO-glycation) and a functional outcome (RNA mis-splicing).

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• The experimental conditions under which the 494 proteins were glycated are not detailed in the provided metadata.

Provenance

Source

figshare

Collection Method

Quantitative chemoproteomic profiling with an alkyne-functionalized MGO probe.

Freshness

Last updated 2026-05-11 06:13:33; freshness should be verified.