FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1608086891> ?p ?o ?g. }

• W1608086891 abstract "P2X2 is an extracellular ATP-gated cation channel which has a voltage-dependent gating property even though it lacks a canonical voltage sensor. It is a trimer in which each subunit has two transmembrane helices and a large extracellular domain. The three inter-subunit ATP binding sites are linked to the pore forming transmembrane (TM) domains by β-strands. We analysed structural rearrangements of the linker strands between the ATP binding site and TM domains upon ligand binding and voltage change, electrophysiologically in Xenopus oocytes, using mutants carrying engineered thiol-modifiable cysteine residues. (1) We demonstrated that the double mutant D315C&I67C (at β-14 and β-1, respectively) shows a 2- to 4-fold increase in current amplitude after treatment with a reducing reagent, dithiothreitol (DTT). Application of the thiol-reactive metal Cd(2+) induced current decline due to bond formation between D315C and I67C. This effect was not observed in wild type (WT) or in single point mutants. (2) Cd(2+)-induced current decline was analysed in hyperpolarized and depolarized conditions with different pulse protocols, and also in the presence and absence of ATP. (3) Current decline induced by Cd(2+) could be clearly observed in the presence of ATP, but was not clear in the absence of ATP, showing a state-dependent modification. (4) In the presence of ATP, Cd(2+) modification was significantly faster in hyperpolarized than in depolarized conditions, showing voltage-dependent structural rearrangements of the linker strands. (5) Experiments using tandem trimeric constructs (TTCs) with controlled number and position of mutations in the trimer showed that the bridging by Cd(2+) between 315 and 67 was not intra- but inter-subunit. (6) Finally, we performed similar analyses of a pore mutant T339S, which makes the channel activation voltage insensitive. Cd(2+) modification rates of T339S were similar in hyperpolarized and depolarized conditions. Taking these results together, we demonstrated that structural rearrangements of the linker region of the P2X2 receptor channel are induced not only by ligand binding but also by membrane potential change." @default.
• W1608086891 created "2016-06-24" @default.
• W1608086891 creator A5048907911 @default.
• W1608086891 creator A5088049227 @default.
• W1608086891 date "2014-09-29" @default.
• W1608086891 modified "2023-09-24" @default.
• W1608086891 title "Voltage- and ATP-dependent structural rearrangements of the P2X2 receptor associated with the gating of the pore" @default.
• W1608086891 cites W131278278 @default.
• W1608086891 cites W1730747168 @default.
• W1608086891 cites W1800266928 @default.
• W1608086891 cites W1965355471 @default.
• W1608086891 cites W1968920700 @default.
• W1608086891 cites W1973534594 @default.
• W1608086891 cites W1974003058 @default.
• W1608086891 cites W1983622758 @default.
• W1608086891 cites W1987474460 @default.
• W1608086891 cites W2001695617 @default.
• W1608086891 cites W2010556099 @default.
• W1608086891 cites W2011524304 @default.
• W1608086891 cites W2014506974 @default.
• W1608086891 cites W2017135735 @default.
• W1608086891 cites W2021184142 @default.
• W1608086891 cites W2031187957 @default.
• W1608086891 cites W2031434196 @default.
• W1608086891 cites W2046803215 @default.
• W1608086891 cites W2057073947 @default.
• W1608086891 cites W2066228392 @default.
• W1608086891 cites W2068104052 @default.
• W1608086891 cites W2087306949 @default.
• W1608086891 cites W2097629649 @default.
• W1608086891 cites W2099163813 @default.
• W1608086891 cites W2105711740 @default.
• W1608086891 cites W2118200955 @default.
• W1608086891 cites W2132267306 @default.
• W1608086891 cites W2135562316 @default.
• W1608086891 cites W2142965147 @default.
• W1608086891 cites W2152301430 @default.
• W1608086891 cites W2156346381 @default.
• W1608086891 cites W2161761928 @default.
• W1608086891 cites W2171763221 @default.
• W1608086891 cites W2172228212 @default.
• W1608086891 doi "https://doi.org/10.1113/jphysiol.2014.278507" @default.
• W1608086891 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4253469" @default.
• W1608086891 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25172943" @default.
• W1608086891 hasPublicationYear "2014" @default.
• W1608086891 type Work @default.
• W1608086891 sameAs 1608086891 @default.
• W1608086891 citedByCount "3" @default.
• W1608086891 countsByYear W16080868912015 @default.
• W1608086891 countsByYear W16080868912016 @default.
• W1608086891 countsByYear W16080868912017 @default.
• W1608086891 crossrefType "journal-article" @default.
• W1608086891 hasAuthorship W1608086891A5048907911 @default.
• W1608086891 hasAuthorship W1608086891A5088049227 @default.
• W1608086891 hasBestOaLocation W16080868911 @default.
• W1608086891 hasConcept C100837961 @default.
• W1608086891 hasConcept C104292427 @default.
• W1608086891 hasConcept C104317684 @default.
• W1608086891 hasConcept C111919701 @default.
• W1608086891 hasConcept C118892022 @default.
• W1608086891 hasConcept C12554922 @default.
• W1608086891 hasConcept C166342909 @default.
• W1608086891 hasConcept C170493617 @default.
• W1608086891 hasConcept C178790620 @default.
• W1608086891 hasConcept C181199279 @default.
• W1608086891 hasConcept C181911157 @default.
• W1608086891 hasConcept C185592680 @default.
• W1608086891 hasConcept C194544171 @default.
• W1608086891 hasConcept C24530287 @default.
• W1608086891 hasConcept C2776403692 @default.
• W1608086891 hasConcept C2779201268 @default.
• W1608086891 hasConcept C2779535977 @default.
• W1608086891 hasConcept C2779546866 @default.
• W1608086891 hasConcept C2779564974 @default.
• W1608086891 hasConcept C2780557392 @default.
• W1608086891 hasConcept C41008148 @default.
• W1608086891 hasConcept C41625074 @default.
• W1608086891 hasConcept C55493867 @default.
• W1608086891 hasConcept C8010536 @default.
• W1608086891 hasConcept C86803240 @default.
• W1608086891 hasConceptScore W1608086891C100837961 @default.
• W1608086891 hasConceptScore W1608086891C104292427 @default.
• W1608086891 hasConceptScore W1608086891C104317684 @default.
• W1608086891 hasConceptScore W1608086891C111919701 @default.
• W1608086891 hasConceptScore W1608086891C118892022 @default.
• W1608086891 hasConceptScore W1608086891C12554922 @default.
• W1608086891 hasConceptScore W1608086891C166342909 @default.
• W1608086891 hasConceptScore W1608086891C170493617 @default.
• W1608086891 hasConceptScore W1608086891C178790620 @default.
• W1608086891 hasConceptScore W1608086891C181199279 @default.
• W1608086891 hasConceptScore W1608086891C181911157 @default.
• W1608086891 hasConceptScore W1608086891C185592680 @default.
• W1608086891 hasConceptScore W1608086891C194544171 @default.
• W1608086891 hasConceptScore W1608086891C24530287 @default.
• W1608086891 hasConceptScore W1608086891C2776403692 @default.
• W1608086891 hasConceptScore W1608086891C2779201268 @default.
• W1608086891 hasConceptScore W1608086891C2779535977 @default.
• W1608086891 hasConceptScore W1608086891C2779546866 @default.
• W1608086891 hasConceptScore W1608086891C2779564974 @default.
• W1608086891 hasConceptScore W1608086891C2780557392 @default.

• next