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Perfluorooctane sulfonate (PFOS) concentrations and liver DYRK2 manufacturer function biomarkers inside a population
Perfluorooctane sulfonate (PFOS) concentrations and liver function biomarkers within a population with elevated PFOA exposure,” Environmental Health Perspectives, vol. 120, no. 5, pp. 65560, 2012. N. Kudo and Y. Kawashima, “Toxicity and toxicokinetics of perfluorooctanoic acid in humans and animals,” Journal of Toxicological Sciences, vol. 28, no. two, pp. 497, 2003. L. Cui, Q.-F. Zhou, C.-Y. Liao, J.-J. Fu, and G.-B. Jiang, “Studies around the toxicological effects of PFOA and PFOS on rats using 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. Tiny, 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. 4, 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 inside 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 anxiety and tissue harm 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 is absolutely no conflict of interests.[13]AcknowledgmentsThis study was supported by the National All-natural Science Foundation of China (no. 81060056) and Jiangxi Provincial Education Development (no. GJJ12083).[14][15]
NIH Public AccessAuthor ManuscriptBiochim Biophys Acta. Author manuscript; readily available in PMC 2015 January 01.Published in final edited kind 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 Division of Biochemistry, Emory University, Atlanta GAAbstractThe post-translational attachment of one or many ubiquitin molecules to a protein generates a range of targeting signals that happen to be used in numerous diverse techniques in the cell. Ubiquitination can alter the activity, localization, protein-protein interactions or stability of the targeted protein. Additional, an incredibly big quantity of proteins are subject to regulation by ubiquitin-dependent processes, which means that practically all cellular functions are impacted by these pathways. Practically a hundred enzymes from 5 unique gene households (the deubiquitinating enzymes or DUBs), reverse this modification by hydrolyzing the (iso)peptide bond tethering ubiquitin to itself or the target protein. 4 of those families are thiol proteases and a single can be a metalloprotease. DUBs of your Ubiquitin FGFR4 medchemexpress C-terminal Hydrolase (UCH) loved ones act on smaller molecule adducts of ubiquitin, approach the ubiquitin proprotein, and trim ubiquitin from the distal finish of a polyubiquitin chain. Ubiquitin Particular Proteases (USP) have a tendency to recognize and encounter their substrates by interaction of your variable regions of their sequence with all the substrate protei.

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