We are analyzing https://link.springer.com/article/10.1007/s10522-020-09878-8.

Title:
Novel biomarkers for the evaluation of aging-induced proteinopathies | Biogerontology
Description:
Proteinopathies are characterized by aging related accumulation of misfolded protein aggregates. Irreversible covalent modifications of aging proteins may significantly affect the native three dimentional conformation of proteins, alter their function and lead to accumulation of misfolded protein as dysfunctional aggregates. Protein misfolding and accumulation of aberrant proteins are known to be associated with aging-induced proteinopathies such as amyloid ß and tau proteins in Alzheimer’s disease, α-synuclein in Parkinson’s disease and islet amyloid polypeptides in Type 2 diabetes mellitus. Protein oxidation processes such as S-nitrosylation, dityrosine formation and some of the newly elucidated processes such as carbamylation and citrullination recently drew the attention of researchers in the field of Gerontology. Studying over these processes and illuminating their relations between proteinopathies may help to diagnose early and even to treat age related disorders. Therefore, we have chosen to concentrate on aging-induced proteinopathic nature of these novel protein modifications in this review.
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Keywords {🔍}

pubmed, article, google, scholar, cas, central, protein, disease, sci, aging, res, httpsdoiorg, proteins, citrullination, httpsdoiorgs, carbamylation, alzheimers, diabetes, mol, deiminase, amyloid, type, peptidylarginine, chem, human, cell, formation, med, brain, int, biol, biochem, clin, diseases, arginine, content, yanar, simsek, accumulation, modifications, oxidation, dityrosine, chronic, expression, pad, curr, rev, jaisson, mouse, privacy,

Topics {✒️}

month download article/chapter long-chain poly-l-lysine free radical-mediated oxidation dityrosine cross-linked peptides atayik & bahadir simsek s-nitrosylation-dependent inactivation aging-induced proteinopathic nature central nervous system histone n-terminal recognition 4-hydroxynonenal-modified brain proteins smoke-related health effects gut-derived uremic toxins carbamylation-induced protein damage full article pdf altered ubiquitin-proteasome system streptozotocin-induced sporadic alzheimer ufuk çakatay article biogerontology aims protein folding tau protein aggregation degenerative protein modifications privacy choices/manage cookies h2o2-induced dityrosine martinez de toda tyrosine oxidation products article yanar poly-l-lysine age-related increase dityrosine cross-links misfolded protein aggregates protein oxidation processes whey protein isolate akt/protein kinase long-term exposure additional information publisher' islet amyloid polypeptide carbamylation-derived products oxidative protein damage aging-induced proteinopathies ubiquitin-proteasome pathway protein arginine deiminases central role cell culture model red blood cells diverse asian populations islet amyloid polypeptides erythrocyte redox state arginine-rich proteins amyloid beta-proteins author correspondence

Questions {❓}

Delporte C, Zouaoui Boudjeltia K, Furtmuller PG et al (2018) Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: a potential carbamylation route involved in the formation of atherosclerotic plaques?
Simsek B, Cakatay U (2019a) Could ornithine supplementation be beneficial to prevent the formation of pro-atherogenic carbamylated low-density lipoprotein (c-LDL) particles?
Simsek B, Cakatay U (2019b) Could cyanogenic glycoside rich diet cause increased risk for carbamylation-induced protein damage in individuals with chronic inflammatory diseases?

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