Category: Lab Notes: Cell Biology

Protein glycation is a non-enzymatic modification of proteins caused by sugars and reactive carbonyl compounds. Explore its mechanisms, AGEs, effects on protein structure and function, detection methods, biological significance, and applications.

Protein sulfation is an important modification that regulates protein interactions, cell adhesion, extracellular signaling, immune responses, coagulation, and tissue organization. Explore tyrosine sulfation, glycosaminoglycan sulfation, sulfotransferases, PAPS, and their roles in health and disease.

Post-translational modifications are essential regulators of cell-cycle progression. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control CDKs, cyclins, checkpoints, DNA replication, mitosis, and protein degradation.

Post-translational modifications are essential regulators of cell migration. Discover how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and lipid modifications control cytoskeletal dynamics, focal adhesions, cell polarity, and cancer invasion.

Post-translational modifications are essential regulators of apoptosis. Learn how phosphorylation, ubiquitination, acetylation, SUMOylation, methylation, and other PTMs control p53, BCL-2 proteins, caspases, mitochondrial apoptosis, and cell survival.

Protein nitrosylation is an important redox-dependent post-translational modification, with S-nitrosylation regulating cysteine residues and influencing protein activity, signaling, metabolism, mitochondrial function, immunity, and disease.

Protein carbonylation is an important oxidative post-translational modification associated with reactive oxygen species, oxidative stress, protein damage, aging, mitochondrial dysfunction, inflammation, and disease. Learn how carbonylated proteins form, affect cellular function, and are detected.

Protein succinylation is a metabolic post-translational modification that connects succinyl-CoA metabolism with protein function, mitochondrial activity, epigenetic regulation, gene expression and cellular homeostasis.

Protein cross-linking is a versatile technique used to create covalent connections within or between proteins. Explore its principles, cross-linkers, methods, applications, characterization techniques, advantages, limitations, and emerging developments.

Protein pyroglutamate formation is an N-terminal post-translational modification that affects protein stability, peptide maturation, degradation, aggregation, and biological activity.

Protein AMPylation is a dynamic post-translational modification in which AMP is covalently attached to proteins. Discover its mechanisms, enzymes, substrates, biological functions, and importance in cellular regulation and bacterial pathogenesis.

Protein pupylation is a bacterial post-translational modification system that regulates protein degradation and cellular protein homeostasis. Explore its components, mechanism, biological functions, and importance in Mycobacterium tuberculosis.

Protein S-glutathionylation is a reversible cysteine modification that connects glutathione metabolism with redox signaling, oxidative stress responses, protein function, mitochondrial biology and disease.

Protein formylation is a chemical modification involved in bacterial and mitochondrial protein synthesis, protein maturation, innate immunity, inflammation and cellular signaling.

Lysine malonylation is a metabolic post-translational modification that connects malonyl-CoA metabolism with protein function, mitochondrial activity, epigenetic regulation and cellular homeostasis.