Cargando…
Collagen Glycation Detected by Its Intrinsic Fluorescence
[Image: see text] Collagen’s long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity...
Autores principales: | Muir, Rhona, Forbes, Shareen, Birch, David J.S., Vyshemirsky, Vladislav, Rolinski, Olaf J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8793138/ https://www.ncbi.nlm.nih.gov/pubmed/34555903 http://dx.doi.org/10.1021/acs.jpcb.1c05001 |
Ejemplares similares
-
Impact of the Flavonoid Quercetin on β-Amyloid
Aggregation Revealed by Intrinsic Fluorescence
por: Alghamdi, Abeer, et al.
Publicado: (2022) -
New Locus for Skin Intrinsic Fluorescence in Type 1 Diabetes Also Associated With Blood and Skin Glycated Proteins
por: Roshandel, Delnaz, et al.
Publicado: (2016) -
Carbamylation and glycation compete for collagen molecular aging in vivo
por: Nicolas, Camille, et al.
Publicado: (2019) -
Lysine–arginine advanced glycation end‐product cross‐links and the effect on collagen structure: A molecular dynamics study
por: Nash, Anthony, et al.
Publicado: (2020) -
Interplay between distribution of live cells and growth dynamics of solid tumours
por: Milotti, Edoardo, et al.
Publicado: (2012)