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Itaconate-Mediated Modifications

Itaconate is an immunometabolite that drives two distinct protein modifications: cysteine itaconation (S-itaconation) and lysine itaconylation (K-itaconylation).

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Protein‑macromolecule interaction

Protein-macromolecule interactions serve as the fundamental basis for cellular signal transduction, metabolic regulation, immune responses, and gene expression, with their dysregulation frequently associated with cancer, autoimmune diseases, and neurodegenerative disorders.

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Spatial/proximity interaction

Spatial/proximity interaction studies aim to capture the physical proximity between spatially adjacent molecules (protein-protein, protein-nucleic acid, protein-small molecule, etc.)

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Protein‑small molecule interaction

Protein-small molecule interactions constitute the molecular foundation of cellular life and drug discovery, participating extensively in enzymatic catalysis, signal transduction, metabolic regulation, and gene expression.

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Protein‑RNA interaction-Co-IP

RNA Immunoprecipitation (RIP) is a core molecular biology technique for studying intracellular RNA‑protein interactions, serving as a powerful tool for deciphering the dynamic processes of post‑transcriptional regulatory networks and revealing the functional roles of RNA‑binding proteins (RBPs).

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Protein-RNA interaction-Pull‑down

Protein-RNA interactions are central mechanisms of gene expression regulation, governing RNA processing, transport, translation, and degradation.

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Protein-DNA interaction-Pull-down

A biotin‑labeled DNA probe is designed to target a specific genomic or regulatory region of interest.

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Protein-DNA interaction-ChIP (Chromatin Immunoprecipitation)

Chromatin Immunoprecipitation (ChIP) is a classical epigenetic technique for studying in vivo protein‑DNA interactions, serving as a core tool for deciphering gene expression regulatory mechanisms, transcription factor binding sites, and epigenetic modification landscapes.

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FRET (Fluorescence Resonance Energy Transfer)

Fluorescence Resonance Energy Transfer (FRET) is a physical process based on non-radiative dipole-dipole coupling between a donor fluorophore and an acceptor fluorophore.

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