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Post-translational modifications of proteins: implications for aging, antigen recognition, and autoimmunity.

January 1, 2004

Biogerontology

Abstract Proteins are complex organic molecules susceptible to numerous post-translational modifications occurring spontaneously during aging or as a consequence of physiologic or pathologic processes. Antigenicity and interactions of proteins with components of the immune system may be profoundly affected by post-translational modifications. Thus, modified self-antigens may be absent (not-tolerated) during early T-cell selection and trigger […]

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Investigation of bone disease using isomerized and racemized fragments of type I collagen.

January 1, 2003

Calcif Tissue Int

Abstract In the collagen type I C-telopeptide an aspartyl-glycine site within the sequence AHDGGR is susceptible to molecular rearrangement. In newly synthesized collagen this site is in the native form, denoted alpha L. During aging a spontaneous reaction occurs resulting in three age-modified forms: an isomerized form (beta L) a racemized form (alpha D), and […]

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Non-enzymatic covalent modifications of proteins: mechanisms, physiological consequences and clinical applications.

January 1, 2002

Matrix Biol

Abstract Given the complexity of the biosynthetic machinery and the delicate chemical composition of proteins, it is remarkable that cells manage to produce and maintain normally functioning proteins under most conditions. However, it is now well known that proteins are susceptible to various non-enzymatic covalent modifications (NECM) under physiological conditions. Such modifications can be of […]

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