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2 sm, mechanisms underlying the recognition of phenylethanolamines and ATD-mediated allosteric inhibiti
5 and GluN2B ATDs form a heterodimer and that phenylethanolamine binds at the interface between GluN1
10 injection of AAV2 into RVLM of TH-Cre rats, phenylethanolamine N-methyl transferase and VGLUT2 immun
11 ntrol of enzymes relevant to both synthesis (phenylethanolamine N-methyl transferase) and disposition
14 ng VLM neurons (75%) were immunoreactive for phenylethanolamine N-methyl transferease, thus were C1 c
15 amined in PC-12 cells transfected with a rat phenylethanolamine N-methyl-transferase (PNMT) promoter-
17 -fluoromethyl-THIQs) was proposed, and their phenylethanolamine N-methyltransferase (PNMT) and alpha(
18 s synthesized and evaluated as inhibitors of phenylethanolamine N-methyltransferase (PNMT) and as inh
19 abeling experiments using antibodies against phenylethanolamine N-methyltransferase (PNMT) and cholin
20 combinase under the chromaffin cell-specific phenylethanolamine N-methyltransferase (PNMT) gene promo
22 introduced into murine cells expressing the Phenylethanolamine n-methyltransferase (Pnmt) gene, whic
23 21) were synthesized and evaluated for their phenylethanolamine N-methyltransferase (PNMT) inhibitory
24 chain reaction, we detected a single form of phenylethanolamine N-methyltransferase (PNMT) mRNA in hy
26 the most potent and selective inhibitors of phenylethanolamine N-methyltransferase (PNMT) reported t
27 mone epinephrine through its biosynthesis by phenylethanolamine N-methyltransferase (PNMT) via PNMT g
28 es (3-methyl-THIQs) are potent inhibitors of phenylethanolamine N-methyltransferase (PNMT), but are n
30 n of the genes Tyrosine Hydroxylase (Th) and Phenylethanolamine N-methyltransferase (Pnmt), which als
32 -substituted-THIQs) are potent inhibitors of phenylethanolamine N-methyltransferase (PNMT, EC 2.1.1.2
33 M, selectivity (alpha2 Ki/PNMT Ki) = 6.0) of phenylethanolamine N-methyltransferase (PNMT, EC 2.1.1.2
34 9661, 1) is a potent inhibitor of the enzyme phenylethanolamine N-methyltransferase (PNMT, EC 2.1.1.2
35 -759 and -773 bp in the promoter of the rat phenylethanolamine N-methyltransferase (PNMT; EC 2.1.1.2
36 e synthesized and evaluated as inhibitors of phenylethanolamine N-methyltransferase (PNMT; EC 2.1.1.2
38 s labeled with biotinamide were examined for phenylethanolamine N-methyltransferase immunoreactivity
39 nes for nicotinamide N-methyltransferase and phenylethanolamine N-methyltransferase in several specie
40 nes for nicotinamide N-methyltransferase and phenylethanolamine N-methyltransferase in several specie
42 in which the epinephrine-synthesizing enzyme phenylethanolamine N-methyltransferase was knocked out (
43 tent of the epinephrine synthesizing enzyme, phenylethanolamine N-methyltransferase, immunohistochemi
44 ne hydroxylase, dopamine ss-hydroxylase, and phenylethanolamine N-methyltransferase, we used coimmuno
45 e labeled using an antibody directed against phenylethanolamine-N-methyl transferase (PNMT) and the N
46 ) antibody, or adrenergic neurons labeled by phenylethanolamine-N-methyl transferase (PNMT) antibody.
47 against the epinephrine synthesizing enzyme phenylethanolamine-N-methyl transferase (PNMT), whereas
48 agonist) synthesis, tyrosine hydroxylase and phenylethanolamine-N-methyl transferase, both localized
49 NK) and the epinephrine synthesizing enzyme, phenylethanolamine-N-methyltransferase (PNMT) in the sam
51 mber of dopamine-beta-hydroxylase (DBH)- and phenylethanolamine-N-methyltransferase (PNMT)-positive n
52 ownregulated B2AR, tyrosine hydroxylase, and phenylethanolamine-N-methyltransferase expression, but p
53 e synthetic enzymes tyrosine hydroxylase and phenylethanolamine-N-methyltransferase were assayed.
54 tained for c-Fos, dopamine beta-hydroxylase, phenylethanolamine-N-methyltransferase, and glucagon-lik
55 lase, and dopamine beta-hydroxylase, but not phenylethanolamine-N-methyltransferase, indicating inner
56 sine hydroxylase, dopamine beta-hydroxylase, phenylethanolamine-N-methyltransferase, neuronal nitric
57 pa decarboxylase, dopamine beta-hydroxylase, phenylethanolamine-N-methyltransferase, tryptophan hydro
58 gonist structurally unrelated to the classic phenylethanolamine pharmacophore, binds at the same GluN
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