Post-translational modifications (PTMs) of proteins are essential for signaling pathways activated by infection such as TLR/NLR/RIG-I signaling pathways. PTMs involve the addition of small proteins or functional groups to specific amino acids within the protein, such as ubiquitination, glycosylation, lipidation, methylation, phosphorylation, and acetylation. PTMs are carried out by specialized enzymes, such as ubiquitin E3 ligase, glycosyltransferase, acetyltransferase, and kinases. PTMs play a crucial role in cellular responses by enhancing protein solubilization, conformation (by altering charge or hydrophobicity), interactions, signaling, and degradation.
Based on the size/chemical properties, PTMs can be broadly classified into four categories: (1) protein-based modification involving ubiquitin (known as ubiquitination), Small ubiquitin-like modifier (SUMO, known as SUMOylation), Interferon-stimulated gene (ISG, known as ISGylation), Neural precursor cell expressed, developmentally down-regulated 8 (NEDD8, known as NEDDylation); (2) carbohydrate molecule-based modification; (3) lipid molecule-based modifications; (4) chemical/ionic group such acetyl, phosphate, and methyl to the nascent proteins.
This Research Topic focuses on the essential PTMs associated with inflammatory signaling pathways during infection. Exploring the advances in inflammatory signaling pathways regulated by PTMs during infection will provide theoretical support for the design of anti-inflammation and anti-infection drugs targeting these post-translational modified protein sites.
We welcome submissions of Original Research, Review, Methods, Mini Review and Clinical Trials on the sub-topics below:
• Ubiquitination and deubiquitination in host-pathogen interactions
• Ubiquitination and phosphorylation interplay during signal transduction
• Other PTMs regulate the activation of inflammatory signaling pathways
• Compounds or monoclonal antibodies targeting PTMs-sites of inflammatory signaling proteins
Post-translational modifications (PTMs) of proteins are essential for signaling pathways activated by infection such as TLR/NLR/RIG-I signaling pathways. PTMs involve the addition of small proteins or functional groups to specific amino acids within the protein, such as ubiquitination, glycosylation, lipidation, methylation, phosphorylation, and acetylation. PTMs are carried out by specialized enzymes, such as ubiquitin E3 ligase, glycosyltransferase, acetyltransferase, and kinases. PTMs play a crucial role in cellular responses by enhancing protein solubilization, conformation (by altering charge or hydrophobicity), interactions, signaling, and degradation.
Based on the size/chemical properties, PTMs can be broadly classified into four categories: (1) protein-based modification involving ubiquitin (known as ubiquitination), Small ubiquitin-like modifier (SUMO, known as SUMOylation), Interferon-stimulated gene (ISG, known as ISGylation), Neural precursor cell expressed, developmentally down-regulated 8 (NEDD8, known as NEDDylation); (2) carbohydrate molecule-based modification; (3) lipid molecule-based modifications; (4) chemical/ionic group such acetyl, phosphate, and methyl to the nascent proteins.
This Research Topic focuses on the essential PTMs associated with inflammatory signaling pathways during infection. Exploring the advances in inflammatory signaling pathways regulated by PTMs during infection will provide theoretical support for the design of anti-inflammation and anti-infection drugs targeting these post-translational modified protein sites.
We welcome submissions of Original Research, Review, Methods, Mini Review and Clinical Trials on the sub-topics below:
• Ubiquitination and deubiquitination in host-pathogen interactions
• Ubiquitination and phosphorylation interplay during signal transduction
• Other PTMs regulate the activation of inflammatory signaling pathways
• Compounds or monoclonal antibodies targeting PTMs-sites of inflammatory signaling proteins