Диссертация (1145807), страница 26
Текст из файла (страница 26)
Ordentlich A., Barak D., Kronman C. et al. Exploring the active center of humanacetylcholinesterase with stereomers of an organophosphorus inhibitor with twochiral centers // Biochemistry. – 1999. – V.38. – №10. – P.3055-3066.152. Pedersen A.O., Jacobsen J. Reactivity of the thiol group in human and bovinealbumin at pH 3–9, as measured by exchange with 2,2′-dithiodipyridine // Eur.
J.Biochem. – 1980. – V.106. – P.291-295.153. Pedregosa F., Varoquaux G., Gramfort A. et al. Scikit-learn: Machine learningin Python // Journal of Machine Learning Research. – 2011. – V.12. – P.28252830.154. Pen, J., Beintema, J.J. Nomenclature of esterases // Biochem. J. – 1986. – V.240.– P.933.155. Pérez F., Granger B.E.
IPython: a system for interactive scientific computing //Computing in Science & Engineering. – 2007. – V.9. – №3. – P.21-29.156. Peters Jr. T. All about albumin // Biochemistry, genetics, and medicalapplications. London: Academic Press Ltd. – 1996.157.
Quinlan G.J., Martin G.S., Evans T.W. Albumin: biochemical properties andtherapeutic potential // Hepatology. – 2005. – V.41. – P.1211–1219.158. Radilov A., Rembovskiy V., Rybalchenko I. et al. Handbook of the Toxicologyof Chemical Warfare Agents // Ed Gupta R.C. Oxford: Elsevier Inc., – 2009. –P.69-91.159. Rainsford K.D., Ford N.L., Brooks P.M., Watson H.M. Plasma aspirin esterasesin normal individuals, patients with alcoholic liver disease and rheumatoidarthritis: characterization and the importance of the enzymic components // Eur.J.
Clin. Investg. – 1980. – V.10. – P.413-420.160. Read R.W., Riches J.R., Stevens J.A., Stubbs S.J., Black R.M. Biomarkers oforganophosphorus nerve agent exposure: comparison of phosphylatedbutyrylcholinesterase and phosphylated albumin after oxime therapy // ArchToxicol. – 2010. – V.84. – P.25-36.145161. Reichenwallner J, Hinderberger D.
Using bound fatty acids to disclose thefunctional structure of serum albumin // Biochim Biophys Acta. – 2013. –V.1830. – №12. – P.5382-5393.162. Reiner E., Aldridge W.N., Hoskin C.G. Enzymes HydrolysingOrganophosphorus Compounds // Ellis Horwood Ltd., Chichester, UK. – 1989.163. Roche M., Rondeau P., Singh N.R., Tarnus E., Bourdon E. The antioxidantproperties of serum albumin // FEBS Lett. – 2008. – V.582. – P.1783-1787.164.
Sakurai Y., Ma S.F., Watanabe H. et al. Esterase-like activity of serum albumin:characterization of its structural chemistry using p-nitrophenyl esters assubstrates. // Pharm Res. – 2004. – V.21. – №2. – P.285-292.165. Salvi A., Carrupt P., Mayer J.M., Testa B. Esterase-like activity of human serumalbumin toward prodrug esters of nicotinic acid // Drug. Metab. Dispos. – 1997.– V.25. – P.395-398.166. Sand K.M., Bern M., Nilsen J., Noordzij H.T., Sandlie I., Andersen J.T.Unraveling the Interaction between FcRn and Albumin: Opportunities forDesign of Albumin-Based Therapeutics // Front Immunol.
– 2015. – V.5. –№682.167. Sant’Anna C.M.R., Viana A.D., do Nascimento N.M. A semiempirical study ofacetylcholinehydrolysiscatalyzedbyDrosophilamelanogasteracetylcholinesterase // Bioorg. Chem. – 2006. – V.34. – P.77-89.168. Schmidt N.D., Peschon J.J., Segel I.H. Kinetics of enzymes subject to verystrong product inhibition: Analysis using simplified integrated rate equationsand average velocities // Journal of theoretical biology. – 1983. – Т.100. – №4. –С.
597-611.169. Schomburg D., Schomburg I. Springer Handbook of Enzymes // EC NumberIndex. – 2013.170. Sekula B., Zielinski K., Bujacz A. Crystallographic studies of the complexes ofbovine and equine serum albumin with 3,5-diiodosalicylic acid // Int. J. Biol.Macromol. – 2013. – V.60. – P.316-324.171. Sievers F., Wilm A., Dineen D. et al. Fast, scalable generation of high-qualityprotein multiple sequence alignments using Clustal Omega // Mol Syst Biol.2011. – V.7. – P.539.172.
Silva D., Cortez C.M., Cunha-Bastos J., Louro S.R. Methyl parathion interactionwith human and bovine serum albumin // Toxicol. Lett. – 2004. – V.147. – №1.– P.53-61.173. Sogorb M.A., Alvarez-Escalante C., Carrera V., Vilanova E. An in vitroapproach for demonstrating the critical role of serum albumin in the detoxicationof the carbamate carbaryl at in vivo toxicologically relevant concentrations //Arch Toxicol. – 2007. – V.81.
– P.113-119.174. Sogorb M.A., Vilanova E. Enzymes involved in the detoxification oforganophosphorus, carbamate and pyrethroid insecticides through hydrolysis //Toxicol. Lett. – 2002. – V.128. – P.215-228.175. Sogorb M.A., Vilanova E., Carrera V. Hydrolysis of carbaryl by human serumalbumin // Arch. Toxicol. – 2004. – V.78. – №11. – P.629-634.146176. Sogorb M.A., García-Argüelles S., Carrera V., Vilanova E. Serum albumin is asefficient as paraxonase in the detoxication of paraoxon at toxicologicallyrelevant concentrations // Chem.
Res. Toxicol. – 2008. – V.21. – P.1524-1529.177. Sogorb M.A., Vilanova E. Serum albumins and detoxication of anticholinesterase agents // Chemico-Biological Interactions. – 2010. – V.14. –№187. – P.325–329.178. Somani S.M., Romano J.A. Chemical warfare agents: toxicity at low levels //CRC Press, – 2001.179. Strausberg, R.L., Feingold E.A., Grouse L.H. et al. Generation and initialanalysis of more than 15,000 full-length human and mouse cDNA sequences //Proc Natl Acad Sci USA.
– 2002. – №99. – P.16899–16903.180. Strauss A.W., Bennett C.D., Donohue A.M., Rodkey J.A., Alberts A.W. Ratliver pre-proalbumin: complete amino acid sequence of the pre-piece. Analysisof the direct translation product of albumin messenger RNA // Journal ofBiological Chemistry. – 1977. – V.252. – №19. – P.6846-6855.181. Stryer L., Berg J. M., Tymoczko J. L. Biochemistry // International Edition. –2006.182.
Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K. Crystal structureof human serum albumin at 2.5 A resolution // Protein Eng. – 1999. – V.12. –P.439-446.183. Suji G., Sivakami S. Malondialdehyde, a lipid-derived aldehyde alters thereactivity of Cys34 and the esterase activity of serum albumin // Toxicology inVitro. – 2008. – V.22. – №3. – P.618-624.184. Sultatos L.G., Basker K.M., Shao M., Murphy S.D. The interaction of thephosphorothioate insecticides chlorpyrifos and parathion and their oxygenanalogues with bovine serum albumin // Mol. Pharmacol. – 1984. – V.26. – №1.– P.99-104.185. Teodoro M.L., Phillips G.N.
Jr, Kavraki L.E.. Molecular docking: a problemwith thousands of degrees of freedom // Proc. of the 2001 IEEE InternationalConference on Robotics and Automation (ICRA 2001), IEEE press, Seoul,Korea. – 2001. – P.960-966.186. Tildon J.T., Ogilvie J.W. The esterase activity of bovine mercaptalbumin. Thereaction of the protein with p-nitrophenyl acetate // J. Biol. Chem.– 1972. –V.247. – №4. – P.1265-71.187. Tove S.B.
The esterolytic activity of serum albumin // Biochim. Biophys. Acta.– 1962. – V.5. – P.230-235.188. Van Der Walt S., Colbert S.C., Varoquaux G. The NumPy array: a structure forefficient numerical computation // Computing in Science & Engineering. –2011.
– V.13. – №2. – P.22-30.189. Van Gunsteren W.F., Mark A.E. Validation of molecular dynamics simulations// J. Chem. Phys. – 1998. – V.108. – №15. – P.6109-6116.190. Vilanova E., Sogorb M.A. The role of phosphotriesterases in the detoxication oforganophosphorus compounds // Crit. Rev. Toxicol. – 1999. – V.29. – №1. –P.21-57.147191. Walker C.H., Mackness M.I. Esterases: problems of identification andclassification.
// Biochem Pharmacol. – 1983. – V.32. – №22. – P.3265-3269.192. Walker C.H. The classification of esterases which hydrolyse organophosphates:recent developments // Chem Biol Interact. – 1993. – V.87. – №1-3. – P.17-24.193. Wang Z., Ling B., Zhang R., Suo Y., Liu Y., Yu Z,. Liu C. Docking andmolecular dynamics studies toward the binding of new natural phenolic marineinhibitors and aldose reductase // J.
Chem. Inf. Model. – 2009. – V.28. – №2. –P.162-169.194. Watanabe H., Tanase S., Nakajou K., Maruyama T., Kragh-Hansen U., OtagiriM. Role of Arg-410 and Tyr-411 in human serum albumin for ligand bindingand esterase-like activity // Biochem. J. – 2000. – V.20. – №349.
– P.813-819.195. Watanabe T., Narumiya S., Shimizu T., Hayaishi O. Characterization of thebiosynthetic pathway of prostaglandin D2 in human platelet-rich plasma // J.Biol. Chem. – 1982. – V.257. – P.14847-14853.196. Williams A.M., Dickinson R.G. Studies on the reactivity of acyl glucuronidesVI. Modulation of reversible and covalent interaction of diflunisal acylglucuronide and its isomers with human plasma protein in vitro // Biochem.Pharmacol.
– 1994. – V.47. – P.457-467.197. Williams N.H., Harrison J.M., Read R.W., Black R.M. Phosphylated tyrosine inalbumin as a biomarker of exposure to organophosphorus nerve agents // Arch.Toxicol. – 2007. – V.81. – P.627-639198. Wynalda M.A., Fitzpatrick F.A. Albumins stabilize prostaglandin I2 //Prostaglandins. – 1980. – V.20. – P.853-861.199. Xu C., Zhang A., Liu W. Binding of phenthoate to bovine serum albumin andreduced inhibition on acetylcholinesterase // Pest. Biochem. and Physiol. – 2007.– V.88.
– P.176-180.200. Yamaguchi S., Aldini G., Ito S., Morishita N., Shibata T., Vistoli G., Carini M.,Uchida K. Δ12-Prostaglandin J2 as a product and ligand of human serumalbumin: formation of an unusual covalent adduct at His146 // J. Am. Chem.Soc. – 2010. – V.132. – P.824-832.201. Yamasaki K. Albumin-drug interaction and its clinical implication // Biochimicaet Biophysica Acta (BBA)-General Subjects.
– 2013. – V.1830. – №12. –P.5435-5443.202. Yang J., Petersen C.E., Ha C.E., Bhagavan N.V. Structural insights into humanserum albumin-mediated prostaglandin catalysis // Protein Sci. – 2002. – V.11. –P.538-545.203. Yeung D.T., Smith J.R., Sweeney R.E., Lenz D.E., Cerasoli D.M. A gaschromatographic-mass spectrometric approach to examining stereoselectiveinteraction of human plasma proteins with soman // J. Anal. Toxicol. – 2008. –V.32. – №1. – P.86-91.204.
Ylianttila M.S., Pursiainen N.V., Haapalainen A.M., Juffer A.H., Poirier Y.,Hiltunen J.K., Glumoff T. Crystal structure of yeast peroxisomal multifunctionalenzyme: structural basis for substrate specificity of (3R)-hydroxyacyl-CoAdehydrogenase units // J. Mol. Biol. – 2006. – V.358. – №5. – P.1286-1295.148205. Zaidi N., Ajmal M.R., Rabbani G., Ahmad E., Khan R.H.
A comprehensiveinsight into binding of hippuric acid to human serum albumin: a study touncover its impaired elimination through hemodialysis // PLoS One. – 2013. –V.8. – №8.206. Zaloj V., Elber R. Parallel computations of molecular dynamics trajectoriesusing the stochastic path approach // Comput. Phys.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
