Zobrazeno 1 - 10
of 231
pro vyhledávání: '"John W, Baynes"'
Autor:
Jonathan W.C. Brock, Alicia J. Jenkins, Timothy J. Lyons, Richard L. Klein, Eunsil Yim, Maria Lopes-Virella, Rickey E. Carter, (DCCT/EDIC) Research Group, Suzanne R. Thorpe, John W. Baynes
Publikováno v:
Journal of Lipid Research, Vol 49, Iss 4, Pp 847-855 (2008)
Cardiovascular disease is a major cause of morbidity and premature mortality in diabetes. HDL plays an important role in limiting vascular damage by removing cholesterol and cholesteryl ester hydroperoxides from oxidized low density lipoprotein and f
Externí odkaz:
https://doaj.org/article/94796c5df90a4b698aef377de2232a2c
Autor:
Andrzej S. Januszewski, Nathan L. Alderson, Alicia J. Jenkins, Suzanne R. Thorpe, John W. Baynes
Publikováno v:
Journal of Lipid Research, Vol 46, Iss 7, Pp 1440-1449 (2005)
Chemical modification of proteins by advanced glycation and lipoxidation end products is implicated in the pathogenesis of macrovascular disease in aging and diabetes. To identify biomarkers of the lipoxidative modification of protein, we studied the
Externí odkaz:
https://doaj.org/article/7c839f99536d448fba1d1fb10a849551
Autor:
James P White, John W Baynes, Stephen L Welle, Matthew C Kostek, Lydia E Matesic, Shuichi Sato, James A Carson
Publikováno v:
PLoS ONE, Vol 6, Iss 9, p e24650 (2011)
Muscle wasting that occurs with cancer cachexia is caused by an imbalance in the rates of muscle protein synthesis and degradation. The Apc(Min/+) mouse is a model of colorectal cancer that develops cachexia that is dependent on circulating IL-6. How
Externí odkaz:
https://doaj.org/article/02bbb8ae9825449995d6f5a25b6016af
Autor:
John W Baynes, Marek H. Dominiczak
Now fully revised, this acclaimed textbook efficiently links basic biochemistry with the day-to-day practice of medicine. You will learn basic science concepts and see them illustrated by clinical cases that describe patients you will likely encounte
Publikováno v:
Mass Spectrometry Reviews. 33:98-109
The post-translational modifications (PTMs) of cysteine residues include oxidation, S-glutathionylation, S-nitrosylation, and succination, all of which modify protein function or turnover in response to a changing intracellular redox environment. Suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::394c656ce7ba1cade2403f9942b0b418
https://doi.org/10.1002/mas.21382
https://doi.org/10.1002/mas.21382
Autor:
Norma Frizzell, John W. Baynes
Publikováno v:
Future Medicinal Chemistry. 5:1075-1078
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d53cfa460cdbfccaf1676a8c2c61f2e
https://doi.org/10.4155/fmc.13.73
https://doi.org/10.4155/fmc.13.73
Publikováno v:
Journal of Applied Physiology. 114:824-828
Cachexia, characterized by skeletal muscle mass loss, is a major contributory factor to patient morbidity and mortality during cancer. However, there are no reports on the rate of myofibrillar protein synthesis (MPS) in skeletal muscles that vary in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::353b736ec8a5dd84d762dd9b190f005c
https://doi.org/10.1152/japplphysiol.01141.2012
https://doi.org/10.1152/japplphysiol.01141.2012
Publikováno v:
Biochemical Journal. 445:247-254
2SC [S-(2-succino)-cysteine] is a chemical modification formed by a Michael addition reaction of fumarate with cysteine residues in proteins. Formation of 2SC, termed ‘succination’ of proteins, increases in adipocytes grown in high-glucose medium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb20f1a833792f1a2d60425fdcbc7daa
https://doi.org/10.1042/bj20112142
https://doi.org/10.1042/bj20112142
Publikováno v:
Diabetes
This article outlines evidence that advanced glycation end product (AGE) inhibitors and breakers act primarily as chelators, inhibiting metal-catalyzed oxidation reactions that catalyze AGE formation. We then present evidence that chelation is the mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0813d4bfd4807975905ccb71517dca76
http://europepmc.org/articles/PMC3282805
http://europepmc.org/articles/PMC3282805
Autor:
Linda O'Flaherty, Jennifer M. Taylor, Christopher W. Pugh, Valentine M. Macaulay, Mona El-Bahrawy, Norma Frizzell, Konstantinos Giaslakiotis, Chiara Bardella, Virpi Launonen, Heli J. Lehtonen, Patrick J. Pollard, Ian Tomlinson, Kimberley Howarth, Ian Roberts, Gareth D. H. Turner, Peter J. Ratcliffe, Lauri A. Aaltonen, Adrian L. Harris, Nicola Ternette, Julie Adam, Ashish Chandra, Radu Mihai, David C. Trudgian, Emine Hatipoglu, John W. Baynes, Benedikt M. Kessler
Publikováno v:
The Journal of Pathology. 225:4-11
Germline mutations in the FH gene encoding the Krebs cycle enzyme fumarate hydratase predispose to hereditary leiomyomatosis and renal cell cancer (HLRCC) syndrome. FH-deficient cells and tissues accumulate high levels of fumarate, which may act as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e790694269fd41c74adb056cbc598fc
https://doi.org/10.1002/path.2932
https://doi.org/10.1002/path.2932