Protection against glycation and similar post-translational modifications of proteins.
Glycation and other non-enzymic post-translational modifications of proteins have been implicated in the complications of diabetes and other conditions. In recent years there has been extensive progress in the search for ways to prevent the modifications and prevent the consequences of the modifications. These areas are covered in this review together with newer ideas on possibilities of reversing the chemical modifications.
Harding
John J
JJ
Nuffield Laboratory of Ophthalmology, University of Oxford, Walton Street, Oxford, OX2 6AW, Great Britain. john.harding@eye.ox.ac.uk
Ganea
Elena
E
D001241:Aspirin / Q000737:chemistry; D002241:Carbohydrates / Q000737:chemistry; D048909:Diabetes Complications / Q000517:prevention & control; D003920:Diabetes Mellitus / Q000209:etiology; D017127:Glycation End Products, Advanced / Q000032:analysis; D006031:Glycosylation; D006801:Humans; D007052:Ibuprofen / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000187:drug effects
D002241:Carbohydrates; D017127:Glycation End Products, Advanced; D011506:Proteins; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; D001241:Aspirin; D007052:Ibuprofen