Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Dustin K. Williams"'
Publikováno v:
Molecular Pharmacology. 80:1013-1032
Although α7 nicotinic acetylcholine receptors are considered potentially important therapeutic targets, the development of selective agonists has been stymied by the α7 receptor's intrinsically low probability of opening (P(open)) and the concern t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d98f32eed5ff4eff102e4edccfa4c2ed
https://doi.org/10.1124/mol.111.074302
https://doi.org/10.1124/mol.111.074302
Publikováno v:
The Journal of General Physiology
We have identified a means by which agonist-evoked responses of nicotinic receptors can be conditionally eliminated. Modification of α7L119C mutants by the sulfhydryl reagent 2-aminoethyl methanethiosulfonate (MTSEA) reduces responses to acetylcholi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9ef4f5f0c5c8a3ba6daf3b618b9a810
https://doi.org/10.1085/jgp.201010587
https://doi.org/10.1085/jgp.201010587
Publikováno v:
Molecular pharmacology. 82(4)
α7 nicotinic acetylcholine receptors (nAChRs) have been a puzzle since their discovery in brain and non-neuronal tissues. Maximal transient probability of an α7 nAChR being open with rapid agonist applications is only 0.002. The concentration depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dd454df08d03459d8c88d41f07dcc85
https://pubmed.ncbi.nlm.nih.gov/22828799
https://pubmed.ncbi.nlm.nih.gov/22828799
Publikováno v:
Biochemical pharmacology. 82(8)
Neuronal nicotinic acetylcholine receptors (nAChR), recognized targets for drug development in cognitive and neuro-degenerative disorders, are allosteric proteins with dynamic interconversions between multiple functional states. Activation of the nAC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3046f66c5ed5da988e080b1b785c7a97
https://pubmed.ncbi.nlm.nih.gov/21575610
https://pubmed.ncbi.nlm.nih.gov/21575610
We have shown previously that a highly conserved Tyr in the nicotinic acetylcholine receptor (nAChR) ligand-binding domain (LBD) (alpha7 Tyr188 or alpha4 Tyr195) differentially regulates the activity of acetylcholine (ACh) and the alpha7-selective ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd0d3a09901135679f09410334c5fac3
https://europepmc.org/articles/PMC2700159/
https://europepmc.org/articles/PMC2700159/
Publikováno v:
Biochemical Pharmacology. 82:1031
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb745b181ae61a46588caaaf8fe62202
https://doi.org/10.1016/j.bcp.2011.07.024
https://doi.org/10.1016/j.bcp.2011.07.024