Počet záznamů: 1
Structural modeling and patch-clamp analysis of pain-related mutation TRPA1-N855S reveal inter-subunit salt bridges stabilizing the channel open state
- 1.0444242 - FGÚ 2016 RIV NL eng J - Článek v odborném periodiku
Zíma, V. - Witschas, Katja - Hynková, Anna - Zímová, Lucie - Barvík, I. - Vlachová, Viktorie
Structural modeling and patch-clamp analysis of pain-related mutation TRPA1-N855S reveal inter-subunit salt bridges stabilizing the channel open state.
Neuropharmacology. Roč. 93, Jun (2015), s. 294-307. ISSN 0028-3908. E-ISSN 1873-7064
Grant CEP: GA ČR(CZ) GA305/09/0081; GA ČR(CZ) GBP304/12/G069; GA MŠMT(CZ) EE2.3.30.0025; GA ČR(CZ) GA15-15839S
Institucionální podpora: RVO:67985823
Klíčová slova: ankyrin receptor subtype 1 * S4-S5-linker * mutagenesis
Kód oboru RIV: ED - Fyziologie
Impakt faktor: 4.936, rok: 2015
Within the S4-S5 linker of human TRPA1, a gain-of-function mutation, N855S, was recently found to underlie familial episodic pain syndrome. Here, we derive a structural model of TRPA1 by combining homology modeling, molecular dynamics simulations, point mutagenesis and electrophysiology and clarify the structural basis for this channelopathy
Trvalý link: http://hdl.handle.net/11104/0246808
Počet záznamů: 1