Back to Search Start Over

The status of glycation in protein aggregation.

Authors :
Taghavi, Fereshteh
Habibi-Rezaei, Mehran
Amani, Mojtaba
Saboury, Ali Akbar
Moosavi-Movahedi, Ali Akbar
Source :
International Journal of Biological Macromolecules. Jul2017, Vol. 100, p67-74. 8p.
Publication Year :
2017

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
01418130
Volume :
100
Database :
Academic Search Index
Journal :
International Journal of Biological Macromolecules
Publication Type :
Academic Journal
Accession number :
123157848
Full Text :
https://doi.org/10.1016/j.ijbiomac.2015.12.085