Protection against glycation and similar post-translational modifications of proteins

Biochim Biophys Acta. 2006 Sep;1764(9):1436-46. doi: 10.1016/j.bbapap.2006.08.001. Epub 2006 Aug 5.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Aspirin / chemistry
  • Carbohydrates / chemistry
  • Diabetes Complications / prevention & control
  • Diabetes Mellitus / etiology
  • Glycation End Products, Advanced / analysis
  • Glycosylation*
  • Humans
  • Ibuprofen / chemistry
  • Protein Processing, Post-Translational*
  • Proteins / chemistry
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic / drug effects

Substances

  • Carbohydrates
  • Glycation End Products, Advanced
  • Proteins
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic
  • Aspirin
  • Ibuprofen