WebDec 1, 2024 · Evidence for cryptic cysteine glutathionylation and irreversible C-glutathionylation is emerging. Abstract. Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct biological processes implicated in health and diseases. Despite challenges in analyzing the dynamic and reversible nature of S-glutathionylation ... WebApr 30, 2024 · Many redox regulated cysteines are cryptic and solvent exposed by changes in protein structure that were induced by EGF treatment. The novel finding that …
Cystinuria: MedlinePlus Medical Encyclopedia
WebMar 1, 2014 · Cryptic cysteines that become exposed under mechanical loads have recently been identified in elastic proteins of the cytoskeleton and the extracellular … WebFeb 8, 2024 · Crystal structures of arsenic-bound p53 mutants reveal a cryptic allosteric site involving three arsenic-coordinating cysteines within the DNA-binding domain, distal to … popular brazilian names for boys
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WebFeb 27, 2024 · A previous study indeed showed stretch-induced mechanical unfolding of immunoglobulin domains of titin to expose cryptic cysteines to S-glutathionylation, which interfered with the ability of titin to refold and left titin in a more extensible state. 14 In acidic pH, the reverse was observed, namely, a prestretch-induced reduction of titin ... WebApr 23, 2012 · In contrast, the N-terminal cysteines of the peptide building blocks, which are the ligation handles, are temporarily protected as thiazolidine rings (the 5-membered N, S heterocycle) and then selectively exposed when needed. WebDec 24, 2024 · Crystal structures of arsenic-bound p53 mutants reveal a cryptic allosteric site involving three arsenic-coordinating cysteines within the DNA-binding domain, distal to the zinc-binding site. Arsenic binding stabilizes the DNA-binding loop-sheet-helix motif alongside the overall β-sandwich fold, endowing p53 mutants with thermostability and ... sharkey productions