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Characterization of calmodulin binding domains in TRPV2 and TRPV5 C-tails
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SYSNO ASEP 0358914 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Characterization of calmodulin binding domains in TRPV2 and TRPV5 C-tails Author(s) Holakovská, Blanka (FGU-C)
Gryčová, Lenka (FGU-C) RID
Bílý, Jan (FGU-C)
Teisinger, Jan (FGU-C) RIDSource Title Amino Acids. - : Springer - ISSN 0939-4451
Roč. 40, č. 2 (2011), s. 741-748Number of pages 8 s. Language eng - English Country AT - Austria Keywords TRPV2 ; TRPV5 ; calmodulin Subject RIV BO - Biophysics R&D Projects IAA600110701 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GAP301/10/1159 GA ČR - Czech Science Foundation (CSF) GPP205/10/P308 GA ČR - Czech Science Foundation (CSF) GD305/03/H148 GA ČR - Czech Science Foundation (CSF) LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50110509 - FGU-C (2005-2011) UT WOS 000286189600042 DOI 10.1007/s00726-010-0712-2 Annotation The transient receptor potential channels TRPV2 and TRPV5 belong to the vanilloid TRP subfamily. In our study we identified calmodulin binding sites on the C-termini of TRPV2 (654-683) and TRPV5 (587-616) corresponding to the consensus CaM binding motif 1-5-10 using in vitro binding assays Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2012
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