Perfluorooctane sulfonate (PFOS) concentrations and liver function biomarkers in a population
Perfluorooctane sulfonate (PFOS) concentrations and liver function biomarkers inside a population with elevated PFOA exposure,” Environmental Overall health Perspectives, vol. 120, no. five, pp. 65560, 2012. N. Kudo and Y. Kawashima, “Toxicity and toxicokinetics of perfluorooctanoic acid in humans and animals,” Journal of D4 Receptor review toxicological Sciences, vol. 28, no. 2, pp. 497, 2003. L. Cui, Q.-F. Zhou, C.-Y. Liao, J.-J. Fu, and G.-B. Jiang, “Studies on the toxicological effects of PFOA and PFOS on rats utilizing histological observation and chemical evaluation,” Archives of Environmental Contamination and Toxicology, vol. 56, no. 2, pp. 33849, 2009. L. M. Eldasher, X. Wen, M. S. Small, K. M. Bircsak, L. L. Yacovino, and L. M. Aleksunes, “Hepatic and renal Bcrp transporter expression in mice treated with perfluorooctanoic acid,” Toxicology, vol. 306, no. four, pp. 10813, 2013. A. G. Abdellatif, V. Preat, H. S. Taper, and M. Roberfroid, “The modulation of rat liver carcinogenesis by perfluorooctanoic acid, a peroxisome proliferator,” Toxicology and Applied Pharmacology, vol. 111, no. 3, pp. 53037, 1991. V. Bindhumol, K. C. Chitra, and P. P. Mathur, “Bisphenol A induces reactive oxygen species generation in the liver of male rats,” Toxicology, vol. 188, no. 2-3, pp. 11724, 2003. D. Bagchi, J. Balmoori, M. Bagchi, X. Ye, C. B. Williams, and S. J. Stohs, “Comparative effects of TCDD, endrin, naphthalene and chromium (VI) on oxidative strain and tissue damage within the liver and brain tissues of mice,” Toxicology, vol. 175, no. 1, pp. 732, 2002. A. P. Senft, T. P. Dalton, D. W. Nebert, M. B. Genter, R. J. Hutchinson, and H. G. Shertzer, “Dioxin increases reactive[12]Conflict of InterestsThe authors declare that there’s no conflict of interests.[13]AcknowledgmentsThis study was supported by the National All-natural Science Foundation of China (no. 81060056) and Jiangxi Provincial Education Improvement (no. GJJ12083).[14][15]
NIH Public AccessAuthor ManuscriptBiochim Biophys Acta. Author manuscript; obtainable in PMC 2015 January 01.Published in final edited form as: Biochim Biophys Acta. 2014 January ; 1843(1): . doi:10.1016j.bbamcr.2013.06.027.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptRegulation of Proteolysis by Human Deubiquitinating EnzymesZiad M. Eletr and Keith D. Wilkinson Department of Biochemistry, Emory University, Atlanta GAAbstractThe post-translational attachment of 1 or a number of CDK3 review Ubiquitin molecules to a protein generates various targeting signals which might be applied in a lot of different methods in the cell. Ubiquitination can alter the activity, localization, protein-protein interactions or stability of your targeted protein. Additional, an extremely significant quantity of proteins are topic to regulation by ubiquitin-dependent processes, which means that virtually all cellular functions are impacted by these pathways. Almost a hundred enzymes from 5 distinct gene families (the deubiquitinating enzymes or DUBs), reverse this modification by hydrolyzing the (iso)peptide bond tethering ubiquitin to itself or the target protein. 4 of these families are thiol proteases and a single is really a metalloprotease. DUBs on the Ubiquitin C-terminal Hydrolase (UCH) family members act on tiny molecule adducts of ubiquitin, course of action the ubiquitin proprotein, and trim ubiquitin from the distal finish of a polyubiquitin chain. Ubiquitin Certain Proteases (USP) usually recognize and encounter their substrates by interaction of your variable regions of their sequence using the substrate protei.
Posted inUncategorized