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Acetylation is one of the major protein modifications in cells, where the acetyl group from acetyl coenzyme A (acetyl-CoA) is transferred to a polypeptide chain. Protein acetylation can occur at N-terminal as a co-translational covalent modification by N-terminal acetyltransferases (NATs), or on lysine as a reversible post-translational modification (PTM). Like phosphorylation, acetylation also affects protein function by altering the properties of proteins such as hydrophobicity, solubility, protein conformation and affinity with other macromolecules. https://www.cd-biosciences...

The Global Glycomics Market is poised to thrive by 13% CAGR through Advancements in Glycoproteomics

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Protein N-myristoylation is a universal post-translational modification in eukaryotes catalyzed by the enzyme N-myristoyltransferase (NMT), which transfers myristate from myristoyl coenzyme A (Myr-CoA) to the N-terminal glycine of a wide range of substrate proteins, it has been involved in the progression and development of a range of human diseases, such as cancer1, epilepsy, Alzheimer’s disease, Noonan-like syndrome and viral and bacterial infections. Both NMT1 and NMT2 of human NMT isozymes are conveyed in most tissues. N-myristoylation is certainly surpassed by proteolysis to show an N-terminal glycine, the only completely conserved motif across all known NMT substrates. This may happen either co-translationally when methionine aminopeptidase (MetAP) acts on an N-terminal ‘MG’ motif at the ribosome, or post-translationally at an internal site. Besides the importance in health and disease of N-myristoylation, direct identification of the N-myristoylated proteome in cells has been limited to non-native low-throughput systems, for example, over-expression of artificial protein constructs. N-terminally myristoylated proteins are related to many kinds of cellular processes, which includes proliferation, differentiation, and apoptosis, and have been shown to be essential for embryogenesis. https://www.creative-prote...

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