title: The status of glycation in protein aggregation.
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.
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; UNESCO Chair on Interdisciplinary Research in Diabetes at University of Tehran, Iran; Faculty of Bio Science, Tarbiat Modares University, Tehran, Iran.
authors.forename: Fereshteh
authors.initials: F
authors.lastname: Taghavi
authors.affiliation: Schools of Biology, University of Tehran, Tehran, Iran.
authors.forename: Mehran
authors.initials: M
authors.lastname: Habibi-Rezaei
authors.affiliation: Department of Biochemistry, Faculty of Medicine, Medical University of Ardabil, Ardabil, Iran.
authors.forename: Mojtaba
authors.initials: M
authors.lastname: Amani
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran.
authors.forename: Ali Akbar
authors.initials: AA
authors.lastname: Saboury
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; UNESCO Chair on Interdisciplinary Research in Diabetes at University of Tehran, Iran; Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran. Electronic address: moosavi@ut.ac.ir.
authors.forename: Ali Akbar
authors.initials: AA
authors.lastname: Moosavi-Movahedi
mesh_terms: D000818:Animals; D006031:Glycosylation / Q000187:drug effects; D006801:Humans; D007700:Kinetics; D066329:Protein Aggregates; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D066329:Protein Aggregates; D011506:Proteins
keywords: Aggregation; Amyloid; Glycation; Non amyloid; Oxidative stress