| Literature DB >> 26751401 |
Fereshteh Taghavi1, Mehran Habibi-Rezaei2, Mojtaba Amani3, Ali Akbar Saboury4, Ali Akbar Moosavi-Movahedi5.
Abstract
Protein crucial function and flexibility directly depend on its whole structure which is determined by the native distribution of structural elements. Any disturbances in a protein architecture leads to many kind of abnormalities and intra- or extracellular accumulation of misfolded proteins which are the basis of conformational diseases. Glycation is one of the most important unwanted post-translational modifications (PTM) which modifies protein three dimensional decoration and triggers its abnormalities. In current review, we take a look at the brief history of protein glycation, its mechanism and kinetics, glycation consequences and toxic products and its involvement in protein chemical modification, aggregation amyloids and fibril formation and different mechanisms induced by such alterations.Entities:
Keywords: Aggregation; Amyloid; Glycation; Non amyloid; Oxidative stress
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Year: 2016 PMID: 26751401 DOI: 10.1016/j.ijbiomac.2015.12.085
Source DB: PubMed Journal: Int J Biol Macromol ISSN: 0141-8130 Impact factor: 6.953