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- W2196758431 endingPage "74" @default.
- W2196758431 startingPage "67" @default.
- W2196758431 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." @default.
- W2196758431 created "2016-06-24" @default.
- W2196758431 creator A5027517298 @default.
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- W2196758431 creator A5059229164 @default.
- W2196758431 creator A5081290326 @default.
- W2196758431 creator A5089344970 @default.
- W2196758431 date "2017-07-01" @default.
- W2196758431 modified "2023-10-11" @default.
- W2196758431 title "The status of glycation in protein aggregation" @default.
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