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10.1016/j.redox.2017.10.022 http://scihub22266oqcxt.onion/10.1016/j.redox.2017.10.022 C5684091!5684091 !29132128     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29132128 &cmd=llinks): Failed to open stream: HTTP request failed! 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A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation |pdf=|usr=}}{{29132128 }} gab.com Text A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation JO: Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=29132128 #FOAvip Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. Here, we demonstrate that the irreversible oxidation of a single free Cys suffices to severely perturb the folding energy landscape of a stable globular protein, compromise its kinetic stability, and lead to the formation of amyloids under physiological conditions. Experiments and simulations converge to indicate that this specific oxidation-promoted protein aggregation requires only local unfolding. Indeed, a large scale analysis indicates that many cellular proteins are at risk of undergoing this kind of deleterious transition; explaining how oxidative stress can impact cell proteostasis and subsequently lead to the onset of pathological states. Twit Text FOAVip A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation ????Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=29132128 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29132128 #FOAvip English Wikipedia <ref>{{Cite pmid|29132128 }}</ref> A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation #MMPMID29132128 Marinelli P ; Navarro S ; Graña-Montes R ; Bañó-Polo M ; Fernández MR ; Papaleo E ; Ventura S Redox Biol 2018[Apr]; 14 (ä): 566-575 PMID29132128 show ga Oxidatively modified forms of proteins accumulate during aging. Oxidized protein conformers might act as intermediates in the formation of amyloids in age-related disorders. However, it is not known whether this amyloidogenic conversion requires an extensive protein oxidative damage or it can be promoted just by a discrete, localized post-translational modification of certain residues. Here, we demonstrate that the irreversible oxidation of a single free Cys suffices to severely perturb the folding energy landscape of a stable globular protein, compromise its kinetic stability, and lead to the formation of amyloids under physiological conditions. Experiments and simulations converge to indicate that this specific oxidation-promoted protein aggregation requires only local unfolding. Indeed, a large scale analysis indicates that many cellular proteins are at risk of undergoing this kind of deleterious transition; explaining how oxidative stress can impact cell proteostasis and subsequently lead to the onset of pathological states. |*Protein Stability [MESH] |Amino Acid Sequence [MESH] |Amyloid/*chemistry [MESH] |Cysteine/*chemistry [MESH] |Humans [MESH] |Kinetics [MESH] |Models, Molecular [MESH] |Oxidation-Reduction [MESH] |Protein Aggregates [MESH] |Protein Folding [MESH] |Protein Processing, Post-Translational [MESH] |RNA Splicing Factors/*chemistry [MESH] |Saccharomyces cerevisiae Proteins/*chemistry [MESH]A single cysteine post-translational oxidation suffices to compromise (epmc).pdf DeepDyve Pubget Overpricing