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The C-terminal basic residues contribute to the chemical- and voltage-dependent activation of TRPA1
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SYSNO ASEP 0356171 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The C-terminal basic residues contribute to the chemical- and voltage-dependent activation of TRPA1 Author(s) Samad, Abdul (FGU-C)
Surá, Lucie (FGU-C)
Benedikt, Jan (FGU-C)
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAI
Minofar, Babak (UEK-B) RID
Teisinger, Jan (FGU-C) RID
Vlachová, Viktorie (FGU-C) RID, ORCID, SAISource Title Biochemical Journal. - : Portland Press - ISSN 0264-6021
Roč. 433, č. 1 (2011), s. 197-204Number of pages 8 s. Language eng - English Country GB - United Kingdom Keywords ankyrin receptor ; transient receptor channel ; voltage sensor Subject RIV FH - Neurology R&D Projects GA305/06/0319 GA ČR - Czech Science Foundation (CSF) GAP301/10/1159 GA ČR - Czech Science Foundation (CSF) IAA600110701 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) 1M0517 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50110509 - FGU-C (2005-2011) AV0Z60870520 - UEK-B (2005-2011) UT WOS 000290055700020 DOI 10.1042/BJ20101256 Annotation The ankyrin transient receptor potential channel TRPA1 is a nonselective cationic channel that is expressed by sensory neurons, where it can be activated by pungent chemicals, such as allyl isothiocyanate (AITC) or highly depolarizing voltages (> +100 mV). In this study, we mutated 27 basic residues all along the C-terminal tail of TRPA1 and explored their role in AITC and voltage-dependent gating. We identify basic residues in the C-terminus that are strongly involved in TRPA1 voltage and chemical sensitivity, some of them may represent possible interaction sites for negatively charged molecules that are generally considered to modulate TRPA1 Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2011
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