Category: Lab Notes: Cell Biology

Protein lactylation is an emerging post-translational modification that connects lactate metabolism with protein regulation, gene expression, inflammation, cellular signaling and disease.

Protein ubiquitination is a fundamental post-translational modification that regulates protein degradation, cellular signaling, DNA repair, autophagy, protein trafficking and cellular homeostasis.

Protein deamidation is a chemical modification in which asparagine or glutamine residues are converted into acidic amino acids. Learn how deamidation affects protein structure, stability, aging, proteostasis, disease, and therapeutic proteins.

Protein citrullination is a calcium-dependent post-translational modification that converts arginine into citrulline. Explore PAD enzymes, histone citrullination, NETosis, inflammation, rheumatoid arthritis, autoimmunity, cancer, and citrullination proteomics.

Protein ADP-ribosylation is an important post-translational modification that uses NAD+ to regulate proteins and cellular pathways. Explore mono- and poly-ADP-ribosylation, PARP enzymes, DNA repair, chromatin regulation, cancer, metabolism, inflammation, and cell death.

Protein glycosylation is an important post-translational modification that regulates protein folding, stability, localization, trafficking, cell recognition, signaling, and immune function. Explore N-linked and O-linked glycosylation, O-GlcNAcylation, glycosyltransferases, glycoproteomics, and disease.

Protein lipidation is an important post-translational modification in which lipid groups are attached to proteins to regulate membrane targeting, localization, stability, trafficking, signaling, and protein interactions. Learn about myristoylation, palmitoylation, prenylation, GPI anchoring, and cholesterol modification.

Protein SUMOylation is an important post-translational modification that regulates protein activity, localization, stability, molecular interactions, gene expression, DNA repair, and cellular stress responses. Learn about SUMO proteins, Ubc9, SUMO ligases, SENPs, SUMO–ubiquitin crosstalk, and SUMO proteomics.

Protein methylation is an important post-translational modification that regulates protein function, chromatin structure, gene expression, signaling, and cellular metabolism. Learn about lysine and arginine methylation, methyltransferases, demethylases, histone methylation, methylproteomics, and disease.

Protein acetylation is an important post-translational modification that regulates protein activity, stability, localization, interactions, gene expression, and metabolism. Learn about lysine acetylation, acetyltransferases, deacetylases, histone acetylation, acetylomics, and the role of acetylation in disease.

Protein phosphorylation is a reversible post-translational modification that regulates protein activity, stability, localization, interactions, and cellular signaling. Learn about protein kinases, phosphatases, phosphorylation sites, signaling pathways, phosphoproteomics, disease mechanisms, and therapeutic applications.

Post-translational modifications (PTMs) are biochemical changes that occur during or after protein synthesis and regulate protein structure, activity, stability, localization, interactions, and degradation. This overview introduces the major types of PTMs, their biological functions, mechanisms, role in disease, and methods used to study protein modifications.

Protein folding is the process by which newly synthesized proteins acquire their functional three-dimensional structures. Discover how folding occurs, what influences it, and how cells manage misfolded proteins.

Apoptosis is a controlled form of programmed cell death that removes damaged or unnecessary cells without causing inflammation. Through coordinated activation of extrinsic and intrinsic pathways, apoptosis maintains tissue homeostasis and protects organisms from disease.

ER stress arises when misfolded proteins accumulate in the endoplasmic reticulum, overwhelming its folding capacity. Through IRE1, PERK and ATF6 signalling, the unfolded protein response restores proteostasis, reduces protein load and protects cells from stress‑induced damage.