Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jenny K. Ngo"'
Publikováno v:
Redox Biology, Vol 1, Iss 1, Pp 258-264 (2013)
The elimination of oxidatively modified proteins is a crucial process in maintaining cellular homeostasis, especially during stress. Mitochondria are protein-dense, high traffic compartments, whose polypeptides are constantly exposed to superoxide, h
Externí odkaz:
https://doaj.org/article/c9bcd188b8594f188fc47d8277fd224e
Publikováno v:
Redox Biology
Redox Biology, Vol 1, Iss 1, Pp 258-264 (2013)
Redox Biology, Vol 1, Iss 1, Pp 258-264 (2013)
The elimination of oxidatively modified proteins is a crucial process in maintaining cellular homeostasis, especially during stress. Mitochondria are protein-dense, high traffic compartments, whose polypeptides are constantly exposed to superoxide, h
Autor:
Sataro Goto, Erika Koltai, Albert W. Taylor, Zsolt Radak, Jenny K. Ngo, Kelvin J.A. Davies, Nikolett Hart
Publikováno v:
American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 303:R127-R134
A decline in mitochondrial biogenesis and mitochondrial protein quality control in skeletal muscle is a common finding in aging, but exercise training has been suggested as a possible cure. In this report, we tested the hypothesis that moderate-inten
Autor:
Kelvin J.A. Davies, Jenny K. Ngo
Publikováno v:
Muscle Aging, Inclusion-Body Myositis and Myopathies
Publikováno v:
Ngo, Jenny K; Pomatto, Laura CD; Bota, Daniela A; Koop, Alison L; & Davies, Kelvin JA. (2011). Impairment of lon-induced protection against the accumulation of oxidized proteins in senescent wi-38 fibroblasts.. The journals of gerontology. Series A, Biological sciences and medical sciences, 66(11), 1178-1185. doi: 10.1093/gerona/glr145. UC Office of the President: Research Grants Program Office (RGPO). Retrieved from: http://www.escholarship.org/uc/item/6695c9sw
Oxidative damage to mitochondrial proteins is thought to contribute to the aging process, but the Lon protease normally degrades such proteins. In early-passage WI-38 human lung fibroblasts, Lon expression is rapidly induced during H(2)O(2) stress, w
Autor:
Gennady Ermak, Betul Catalgol, Tilman Grune, Anke Licht, Kelvin J.A. Davies, Jenny K. Ngo, Andrew M. Pickering
Publikováno v:
Free radical biologymedicine. 51(7)
We report an entirely new role for the HSP70 chaperone in dissociating 26S proteasome complexes (into free 20S proteasomes and bound 19S regulators), preserving 19S regulators, and reconstituting 26S proteasomes in the first 1-3 hours following mild
Autor:
Kelvin J.A. Davies, Jenny K. Ngo
Publikováno v:
Free radical biologymedicine. 46(8)
The targeted removal of damaged proteins by proteolysis is crucial for cell survival. We have shown previously that the Lon protease selectively degrades oxidized mitochondrial proteins, thus preventing their aggregation and cross-linking. We now sho
Autor:
Jenny K. Ngo, Kelvin J.A. Davies
Publikováno v:
Annals of the New York Academy of Sciences. 1119
Mitochondria are a major intracellular source of free radicals and related oxidants. It is generally agreed that the mitochondrial production of such reactive oxygen and nitrogen species increases with age. Antioxidant systems in the mitochondria pla
Publikováno v:
Bota, Daniela A; Ngo, Jenny K; & Davies, Kelvin JA. (2005). Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death.. Free radical biology & medicine, 38(5), 665-677. doi: 10.1016/j.freeradbiomed.2004.11.017. UC Office of the President: Research Grants Program Office (RGPO). Retrieved from: http://www.escholarship.org/uc/item/3348s0gq
Lon now emerges as a major regulator of multiple mitochondrial functions in human beings. Lon catalyzes the degradation of oxidatively modified matrix proteins, chaperones the assembly of inner membrane complexes, and participates in the regulation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f097c2d34ab18f83db68ef1988a0248f
http://www.escholarship.org/uc/item/3348s0gq
http://www.escholarship.org/uc/item/3348s0gq