In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR

Non-enzymatic glycation of extracellular matrix with (U-(13)C(5))-d-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH(3)–CH(OH)NHR) substructures. Changes in charged...

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Autores principales: Li, R., Rajan, R., Wong, W. C. V., Reid, D. G., Duer, M. J., Somovilla, V. J., Martinez-Saez, N., Bernardes, G. J. L., Hayward, R., Shanahan, C. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5774432/
https://www.ncbi.nlm.nih.gov/pubmed/29192920
http://dx.doi.org/10.1039/c7cc06624d
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author Li, R.
Rajan, R.
Wong, W. C. V.
Reid, D. G.
Duer, M. J.
Somovilla, V. J.
Martinez-Saez, N.
Bernardes, G. J. L.
Hayward, R.
Shanahan, C. M.
author_facet Li, R.
Rajan, R.
Wong, W. C. V.
Reid, D. G.
Duer, M. J.
Somovilla, V. J.
Martinez-Saez, N.
Bernardes, G. J. L.
Hayward, R.
Shanahan, C. M.
author_sort Li, R.
collection PubMed
description Non-enzymatic glycation of extracellular matrix with (U-(13)C(5))-d-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH(3)–CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes.
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spelling pubmed-57744322018-02-15 In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR Li, R. Rajan, R. Wong, W. C. V. Reid, D. G. Duer, M. J. Somovilla, V. J. Martinez-Saez, N. Bernardes, G. J. L. Hayward, R. Shanahan, C. M. Chem Commun (Camb) Chemistry Non-enzymatic glycation of extracellular matrix with (U-(13)C(5))-d-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH(3)–CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes. Royal Society of Chemistry 2017-12-28 2017-12-01 /pmc/articles/PMC5774432/ /pubmed/29192920 http://dx.doi.org/10.1039/c7cc06624d Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Li, R.
Rajan, R.
Wong, W. C. V.
Reid, D. G.
Duer, M. J.
Somovilla, V. J.
Martinez-Saez, N.
Bernardes, G. J. L.
Hayward, R.
Shanahan, C. M.
In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title_full In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title_fullStr In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title_full_unstemmed In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title_short In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR
title_sort in situ characterization of advanced glycation end products (ages) in collagen and model extracellular matrix by solid state nmr
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5774432/
https://www.ncbi.nlm.nih.gov/pubmed/29192920
http://dx.doi.org/10.1039/c7cc06624d
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