Zobrazeno 1 - 10
of 125
pro vyhledávání: '"J.P. Daniel"'
Autor:
Carswell, Casey L., Hénault, Camille M., Murlidaran, Sruthi, Therien, J.P. Daniel, Juranka, Peter F., Surujballi, Julian A., Brannigan, Grace, Baenziger, John E.
Publikováno v:
In Structure 1 September 2015 23(9):1655-1664
Autor:
Hénault, Camille M., Sun, Jiayin, Therien, J.P. Daniel, daCosta, Corrie J.B., Carswell, Casey L., Labriola, Jonathan M., Juranka, Peter F., Baenziger, John E.
Publikováno v:
In Neuropharmacology September 2015 96 Part B:157-168
Publikováno v:
In BBA - Biomembranes September 2015 1848(9):1806-1817
Autor:
Grace Brannigan, Julian A. Surujballi, Casey L. Carswell, Peter F. Juranka, Camille M. Hénault, J.P. Daniel Therien, John E. Baenziger, Sruthi Murlidaran
Publikováno v:
Structure. 23:1655-1664
Summary The gating of pentameric ligand-gated ion channels is sensitive to a variety of allosteric modulators that act on structures peripheral to those involved in the allosteric pathway leading from the agonist site to the channel gate. One such st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e3dcff6d16681a90f6f91f0255a5bf5
https://doi.org/10.1016/j.str.2015.06.020
https://doi.org/10.1016/j.str.2015.06.020
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1848:1806-1817
Membrane lipids are potent modulators of the nicotinic acetylcholine receptor (nAChR) from Torpedo. Lipids influence nAChR function by both conformational selection and kinetic mechanisms, stabilizing varying proportions of activatable versus non-act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62842adaa077bf4942192714e0d23a23
https://doi.org/10.1016/j.bbamem.2015.03.010
https://doi.org/10.1016/j.bbamem.2015.03.010
Publikováno v:
In Current Topics in Membranes 2017 80:95-137
Autor:
J.P. Daniel Therien, John E. Baenziger
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Although transmembrane helix-helix interactions must be strong enough to drive folding, they must still permit the inter-helix movements associated with conformational change. Interactions between the outermost M4 and adjacent M1 and M3 α-helices of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8819548ef9173edf2cae555ef4a65320
Publikováno v:
Nature Chemical Biology. 9:701-707
The ability of the nicotinic acetylcholine receptor (nAChR) to undergo conformational transitions is exquisitely sensitive to its surrounding lipid environment. Previous work has highlighted a conformational selection mechanism, whereby different lip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65c5e42f325f8e53c5029db98bafcbe0
https://doi.org/10.1038/nchembio.1338
https://doi.org/10.1038/nchembio.1338
Autor:
Jiayin Sun, Casey L. Carswell, Jonathan M. Labriola, Peter F. Juranka, J.P. Daniel Therien, Corrie J.B. daCosta, Camille M. Hénault, John E. Baenziger
Publikováno v:
Neuropharmacology. 96
With the availability of high resolution structural data, increasing attention has focused on the mechanisms by which drugs and endogenous compounds allosterically modulate nicotinic acetylcholine receptor (nAChR) function. Lipids are potent modulato
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dc24cb27b1abced2a23728c31fbe934
https://pubmed.ncbi.nlm.nih.gov/25433148
https://pubmed.ncbi.nlm.nih.gov/25433148
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