Isoaspartyl Post-translational Modification Triggers Autoimmune Responses to Self-proteins

Dysbiosis May Trigger Autoimmune Diseases via Inappropriate Post-Translational Modification of Host Proteins

The gut ecosystem with myriads of microorganisms and the high concentration of immune system cells can be considered as a separate organ on its own. The balanced interaction between the host and microbial cells has been shaped during the long co-evolutionary process. In dysbiotic conditions, however, this balance is compromised and results in abnormal interaction between the host and microbiota...

Computational Prediction of Post-Translational Modification Sites in Proteins

The last several decades have witnessed rapid progresses in identification and functional analysis of post-translational modifications (PTMs) in proteins. Through temporal and spatial modification of proteins by covalent attachment of additional chemical groups and other small proteins, proteolytic cleavage or intein splicing, PTMs greatly expand the proteome diversity and play important roles ...

Post-translational modification of PII signal transduction proteins

The PII proteins constitute one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. Quite remarkably PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and in al...

Post-translational modification and folding of secreted proteins.

The production of a functional protein does not end with the termination of the growing polypeptide chain. This, while clearly true of all proteins, is particularly obvious in the case of secretory proteins. While all proteins must fold to a functional conformation, and many must assemble into some supramolecular structure, secretory proteins must also make their way across membranes and throug...

Post-translational modification of exogenous proteins in Xenopus laevis oocytes.