Zobrazeno 1 - 8
of 8
pro vyhledávání: '"George S Yeargans"'
Autor:
Norbert W. Seidler, George S Yeargans
Publikováno v:
Life Sciences. 70:1789-1799
Protein denaturation occurs at sites of inflammation. We hypothesized that denatured protein may provide a more susceptible target for glycation, which is a known mediator of inflammation. We examined the effects of thermal denaturation on the suscep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d6fdfa52e9597f8631cd36bb512b399
https://doi.org/10.1016/s0024-3205(02)01474-1
https://doi.org/10.1016/s0024-3205(02)01474-1
Autor:
George S Yeargans, Brad Cucchetti, Catherine Fitzgerald, Norbert W. Seidler, Timothy A. Swearengin, David McWhorter
Publikováno v:
Journal of Enzyme Inhibition. 15:79-89
Glyceraldehyde 3-phosphate (Glyc3P), a glycolytic intermediate, non-enzymatically glycosy-lated (or glycated) and inhibited the pig heart cytoplasmic aspartate aminotransferase (cAAT). Glyc3P (5.0 mM) decreased cAAT activity by 47% after 1 min at 23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::43647bdb690b4f12c2a1a00940b76b56
https://doi.org/10.1080/14756369909030342
https://doi.org/10.1080/14756369909030342
Publikováno v:
Life Sciences. 54:149-157
The physiological and biochemical demands on contracting muscle make this tissue particularly susceptible to molecular and cellular damage. We looked at membrane structures in cardiac and skeletal muscle and in erythrocytes for exercise-induced lipid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6c282a3dae228e84e8efb5242732331
https://doi.org/10.1016/0024-3205(94)00584-2
https://doi.org/10.1016/0024-3205(94)00584-2
Autor:
George S Yeargans, Norbert W. Seidler
Publikováno v:
Biochemical and biophysical research communications. 320(1)
Acrolein-modified proteins are markers of disorders such as Alzheimer's disease (AD). Acrolein (H2C=HC-CH=O), which can be produced by the oxidative properties of amyloid-beta (Abeta) peptide, localizes to areas immediately surrounding early Abeta ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f3239bf0e9b178a9f8b4d413d150bce
https://pubmed.ncbi.nlm.nih.gov/15207723
https://pubmed.ncbi.nlm.nih.gov/15207723
Publikováno v:
Archives of biochemistry and biophysics. 427(1)
Protein glycation, which promotes aggregation, involves the unwanted reaction of carbohydrate oxidation products with proteins. Glycation of lens alpha-crystallin occurs in vivo and may contribute to cataractogenesis. Anti-glycation compounds such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5800b5925a6837861b1ccf9f26d5d581
https://pubmed.ncbi.nlm.nih.gov/15178493
https://pubmed.ncbi.nlm.nih.gov/15178493
Publikováno v:
Life sciences. 75(11)
Carnosine, a histidine-containing dipeptide, is a potential treatment for Alzheimer's disease. There is evidence that carnosine prevents oxidation and glycation, both of which contribute to the crosslinking of proteins; and protein crosslinking promo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c34edca8db7194f4f8c57e8af60e6ba
https://pubmed.ncbi.nlm.nih.gov/15234195
https://pubmed.ncbi.nlm.nih.gov/15234195
Autor:
Norbert W. Seidler, George S Yeargans
Publikováno v:
Biochemical and biophysical research communications. 300(1)
Glycation alters protein structure and decreases biological activity. Glycated proteins, which accumulate in affected tissue, are reliable markers of disease. Carnosine, which prevents glycation, may also play a role in the disposal of glycated prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0470fe8ffcd18d56783bd7accefdd994
https://pubmed.ncbi.nlm.nih.gov/12480523
https://pubmed.ncbi.nlm.nih.gov/12480523
Publikováno v:
Journal of enzyme inhibition and medicinal chemistry. 17(1)
Acrolein is a reactive lipid peroxidation byproduct, which is found in ischemic tissue. We examined the effects of acrolein on cytosolic aspartate aminotransferase (cAAT), which is an enzyme that was previously shown to be inhibited by glycating agen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a286f4ed2a8deddb50883b66af20836
https://pubmed.ncbi.nlm.nih.gov/12365456
https://pubmed.ncbi.nlm.nih.gov/12365456