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D L Willins

Showing results (11-20 of 13) with videos related to

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The Journal of Pharmacology and Experimental Therapeutics|June 28, 2000
A highly conserved aspartic acid (Asp-155) anchors the terminal amine moiety of tryptamines and is involved in membrane targeting of the 5-HT(2A) serotonin receptor but does not participate in activation via a "salt-bridge disruption" mechanismK Kristiansen, W K Kroeze, D L Willins, et al.
Annals of the New York Academy of Sciences|February 3, 1999
Serotonergic antagonist effects on trafficking of serotonin 5-HT2A receptors in vitro and in vivoD L Willins, L Alsayegh, S A Berry, et al.
Journal of Neurochemistry|April 27, 1999
Structure and function of the third intracellular loop of the 5-hydroxytryptamine2A receptor: the third intracellular loop is alpha-helical and binds purified arrestinsE I Gelber, W K Kroeze, D L Willins, et al.
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Showing results (11-20 of 13) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 13 results.
The Journal of Pharmacology and Experimental Therapeutics|June 28, 2000
A highly conserved aspartic acid (Asp-155) anchors the terminal amine moiety of tryptamines and is involved in membrane targeting of the 5-HT(2A) serotonin receptor but does not participate in activation via a "salt-bridge disruption" mechanismK Kristiansen, W K Kroeze, D L Willins, et al.
Annals of the New York Academy of Sciences|February 3, 1999
Serotonergic antagonist effects on trafficking of serotonin 5-HT2A receptors in vitro and in vivoD L Willins, L Alsayegh, S A Berry, et al.
Journal of Neurochemistry|April 27, 1999
Structure and function of the third intracellular loop of the 5-hydroxytryptamine2A receptor: the third intracellular loop is alpha-helical and binds purified arrestinsE I Gelber, W K Kroeze, D L Willins, et al.
Pageof 2