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1 to their performance under normal saline or methylscopolamine.
2 on of binding sites for the antagonist [3H]N-methylscopolamine.
3 asured with the hydrophilic antagonist [3H]N-methylscopolamine.
4 e of action of AC-42 was obtained in [(3)H]N-methylscopolamine ([(3)H]NMS) binding studies, in that b
5 entration of ACh required to inhibit [(3)H]N-methylscopolamine ([(3)H]NMS) binding to M1, left-shifti
8 r toxins that inhibit the binding of [(3)H]N-methylscopolamine ([(3)H]NMS) to cloned M2 receptors.
9 3N by BR384 was competitively inhibited by N-methylscopolamine and allosterically inhibited by gallam
12 ositively cooperative with the antagonist, N-methylscopolamine, at m2 receptors and, in the case of t
13 t affinity (K(i) = 2.24 muM) for the [(3)H]N-methylscopolamine binding site on the M5 receptor, is po
14 ompetition kinetics using whole-cell [(3)H]N-methylscopolamine binding, validating this approach as a
16 ne completely inhibited the binding of [3H]N-methylscopolamine, but yielded a shallow competition iso
19 ic agents modulate the dissociation of [3H]N-methylscopolamine from M2/M5 chimeric and point-mutated
22 -substituted analogues of brucine with [3H]N-methylscopolamine (NMS) and unlabeled acetylcholine at m
23 ties with acetylcholine and the antagonist N-methylscopolamine (NMS) at M(1)minus signM(4) receptors
24 agonists quinuclidinyl benzilate (QNB) and N-methylscopolamine (NMS) bind to the binding pocket of th
25 f kinetics of the radiolabeled antagonists N-methylscopolamine (NMS) in the presence of methoctramine
28 in a significant reduction in apparent N-[3H]methylscopolamine saturation binding affinity in intact
29 en alcuronium and the classical antagonist N-methylscopolamine that is characteristic of M(5) (these
30 ecreased binding of orthosteric antagonist N-methylscopolamine to human M1- and M2-mAChRs, and increa
31 mum M(1)-blockade, the binding of 1 nM [3H]N-methylscopolamine to striatal membranes was reduced by o
33 nic receptor antagonist, atropine, and [3H]N-methylscopolamine was investigated, however, ATP was una
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