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A systematic survey of archived protein structures has revealed dozens of examples of a previously overlooked covalent ...
The study also found that cysteine residues catalyse peptide synthesis in water by joining together short peptide fragments that the team had previously found in a study published in Nature last year.
There’s a new kind of crosslink in proteins. Instead of an S–S bridge connecting two cysteine residues, it consists of an N–O–S bridge between a lysine and a cysteine. (The “N” comes ...
A new research perspective was published in Aging, titled "Trioxidized cysteine and aging ... including those involving cysteine (Cys) residues in aging proteomes. Specifically, the formation ...
These activities comprise proteases, oxidoreductases and metabolic enzymes that rely on cysteine residues for catalysis and regulation. Functional cysteine residues demonstrate heightened reactivity ...
This amino acid residue is nearly three times as abundant as cysteine in the body: an average of 32 lysines dot every protein. There is tremendous utility in being able to expand the covalent ...
The intramolecular linkage is an N-O-S bridge formed by oxidizing the amine side group of a lysine and the thiol of a cysteine residue. The team that made the discovery, led by Kai Tittmann at the ...
characterized by an imbalance between oxidants and antioxidants - leads to the formation of oxidative posttranslational modifications (PTMs), including those involving cysteine (Cys) residues in ...
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