يعرض 1 - 3 نتائج من 3 نتيجة بحث عن '"Pendrin Protein"', وقت الاستعلام: 1.17s تنقيح النتائج
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    دورية أكاديمية
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    دورية أكاديمية

    المصدر: Medical Genetics; Том 21, № 6 (2022); 37-48 ; Медицинская генетика; Том 21, № 6 (2022); 37-48 ; 2073-7998

    وصف الملف: application/pdf

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Overexpression of Pendrin in Intercalated Cells Produces Chloride-Sensitive Hypertension. J Am Soc Nephrol. 2013; 24(7): 1104-1113. doi:10.1681/ASN.2012080787.; Karniski L.P., Aronson P.S. Chloride/formate exchange with formic acid recycling: a mechanism of active chloride transport across epithelial membranes. Proceedings of the National Academy of Sciences of the United States of America. 1985; 82(18): 6362-6365. doi:10.1073/pnas.82.18.6362.; Kim H-M., Wangemann P. Failure of fluid absorption in the endolymphatic sac initiates cochlear enlargement that leads to deafness in mice lacking pendrin expression. PLOS ONE. 2010; 5(11): e14041. doi:10.1371/journal.pone.0014041.; Rimoin D.L., Schimke R.N. Genetic disorders of the endocrine glands. C.V. Mosby Co, St. Louis. 1971: 11-65.; Stinckens C., Huygen P.L.M., Van Camp G., Cremers C.W. Pendred syndrome redefined. Report of a new family fluctuating and progressive hearing loss. Advances in otorhinolaryngology. 2002; 61: 131-141.; Napiontek U., Borck G., Muller-Forell W., et al.Intrafamilial variability of the deafness and goiter phenotype in Pendred syndrome caused by a T416P mutation in the SLC26A4 gene. Journal of clinical endocrinology and metabolism. 2004; 89(11): 5347-5351.; Кларов Л.А., Николаева К.Ю., Пшенникова В.Г., и др. Мутации гена SLC26A4 у пациентов с аномалиями внутреннего уха: IP-I, IP-II (Mondini) и/или EVA в Якутии. Медицинская генетика. 2021; 20(9): 14-25. doi:10.25557/2073-7998.2021.09.14-25.; Jonard L., Niasme-Grare M., Bonnet C., et al. Screening of SLC26A4, FOXI1 and KCNJ10 genes in unilateral hearing impairment with ipsilateral enlarged vestibular aqueduct.Int J Pediatr Otorhinolaryngol. 2010 Sep; 74(9): 1049-53. doi:10.1016/j.ijporl.2010.06.002.; Ng P.C., Henikoff S. Predicting the effects of amino acid substitutions on protein function. 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Nat Commun. 2014; 5:3622. doi:10.1038/ncomms4622.; Geertsma E.R., Chang Y.N., Shaik F.R., et al. Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family. Nat Struct Mol Biol. 2015; 22: 803-808. doi:10.1038/nsmb.3091.; Dossena S., Bernardinelli E., Sharma A.K., et al. The Pendrin Polypeptide. In: Dossena, S., Paulmichl, M. (eds) The Role of Pendrin in Health and Disease. Springer, Cham. 2017; 187-220: https://doi.org/10.1007/978-3-319-43287-8_11Test.; Kuwabara M.F., Wasano K., Takahashi S., et al. The extracellular loop of pendrin and prestin modulates their voltage-sensing property. J Biol Chem. 2018; 293(26): 9970-9980. doi:10.1074/jbc.RA118.001831.; Babu M., Greenblatt J.F., Emili A., et al. Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism. Structure. 2010; 18(11): 1450-1462. doi:10.1016/j.str.2010.08.015.; Sharma A.K., Rigby A.C., Alper S.L. STAS Domain Structure and Function. Cell Physiol Biochem. 2011. Nov; 28(3): 407-422. doi:10.1159/000335104.; Sharma A.K., Krieger T., Rigby A.C., et al. Human SLC26A4/Pendrin STAS domain is a nucleotide-binding protein: Refolding and characterization for structural studies. Biochem Biophys Rep. 2016; 8: 184-191. doi:10.1016/j.bbrep.2016.08.022.; Rapp C., Reinhart X.B., Reithmeier A.F. Molecular analysis of human solute carrier SLC26 anion transporter disease-causing mutations using 3-dimensional homology modeling. Biochim Biophys Acta Biomembr. 2017; 1859(12): 2420-2434. doi:10.1016/j.bbamem.2017.09.016.; Bassot C., Minervini G., Leonardi E., Tosatto S.C.E. Mapping pathogenic mutations suggests an innovative structural model for the pendrin (SLC26A4) transmembrane domain. Biochimie. 2017; Jan;132: 109-120. doi:10.1016/j.biochi.2016.10.002.; Pasqualetto E., Aiello R., Gesiot L., et al. Structure of the cytosolic portion of the motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters. J Mol Biol. 2010; 400(3): 448-462. doi:10.1016/j.jmb.2010.05.013.; Tsai H.H., Tsai C.J., Ma B., Nussinov R. In silico protein design by combinatorial assembly of protein building blocks. Protein Sci. 2004; 13(10): 2753-2765. doi:10.1110/ps.04774004.; Bordogna A., Pandini A., Bonati L. Predicting the accuracy of protein-ligand docking on homology models. J Comput Chem. 2011; 32(1): 81-98. doi:10.1002/jcc.21601.; Ng D.P., Poulsen B.E., Deber C.M. Membrane protein misassembly in disease. Biochimica et Biophysica Acta (BBA)-Biomembranes 2012; 1818(4): 1115-22. doi:10.1016/j.bbamem.2011.07.046.; Detro-Dassen S., Schänzler M., Lauks H., et al. Conserved dimeric subunit stoichiometry of SLC26 multifunctional anion exchangers. J Biol Chem. 2008; 283(7): 4177-4188. doi:10.1074/jbc.M704924200.; Farrell B., Skidmore B.L., Rajasekharan V., Brownell W.E. A novel theoretical framework reveals more than one voltage-sensing pathway in the lateral membrane of outer hair cells. J Biol Chem. 2020; 152(7):e201912447. doi:10.1085/jgp.201912447.; Fu C., Zheng H., Zhang S., et al. Mutation screening of the SLC26A4 gene in a cohort of 192 Chinese patients with congenital hypothyroidism. Arch Endocrinol Metab. 2016 Aug; 60(4): 323-7. doi:10.1590/2359-3997000000108.; Park H.J., Lee S.J., Jin H.S., et al. Genetic basis of hearing loss associated with enlarged vestibular aqueducts in Koreans. Clin Genet. 2005; 67(2):160-165. https://doi.org/10.1111/j.1399-0004.2004.00386.xTest; Tsukamoto K., Suzuki H., Harada D., et al. Distribution and frequencies of PDS (SLC26A4) mutations in Pendred syndrome and nonsyndromic hearing loss associated with enlarged vestibular aqueduct: a unique spectrum of mutations in Japanese. Eur J Hum Genet. 2003 Dec; 11(12): 916-22. doi:10.1038/sj.ejhg.5201073.; Yoon J.S., Park H-J., Yoo S-Y., et al. Heterogeneity in the processing defect of SLC26A4 mutants. J Med Genet. 2008 Jul; 45(7): 411-9. doi:10.1136/jmg.2007.054635.; Ishihara K., Okuyama S., Kumano S., et al. Salicylate restores transport function and anion exchanger activity of missense pendrin mutations. Hear Res. 2010 Dec 1; 270(1-2): 110-8. doi:10.1016/j.heares.2010.08.015.; Huang S., Han D., Yuan Y., et al. Extremely discrepant mutation spectrum of SLC26A4 between Chinese patients with isolated Mondini deformity and enlarged vestibular aqueduct. J Transl Med. 2011 Sep 30; 9: 167. doi:10.1186/1479-5876-9-167.; Albert S., Blons H., Jonard L., et al. SLC26A4 gene is frequently involved in nonsyndromic hearing impairment with enlarged vestibular aqueduct in Caucasian populations. Eur J Hum Genet. 2006 Jun; 14(6): 773-9. doi:10.1038/sj.ejhg.5201611.; Rebeh I.B., Yoshimi N., Hadj-Kacem H., et al. Two missense mutations in SLC26A4 gene: a molecular and functional study. Clin Genet. 2010 Jul; 78(1): 74-80. doi:10.1111/j.1399-0004.2009.01360.x.; Wasano K., Takahashi S., Rosenberg S.K., et al. Systematic quantification of the anion transport function of pendrin (SLC26A4) and its disease-associated variants. Hum Mutat. 2020 Jan; 41(1): 316-331. doi:10.1002/humu.23930.; https://www.medgen-journal.ru/jour/article/view/2185Test