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1 ryl-cholinesterase, nor of the high-affinity choline transporter.
2 -dependent, hemicholinium-3 (HC-3)-sensitive choline transporter.
3 icholinium-3 (HC-3)-sensitive, high affinity choline transporter.
4 and that snf-6 encodes a novel acetylcholine/choline transporter.
5 increases in the levels of the highaffinity choline transporter.
6 e presynaptic sodium-dependent high-affinity choline transporter 1 (CHT), which is known to be mutate
7 relatively unique in their expression of the choline transporter 1 (CHT1), which exhibits high-affini
8 se (AChE), choline acetyltransferase (ChAT), choline transporter 1 (CHT1, SLC5A7), vesicular acetylch
9 psis thaliana, 29.6% identity with the yeast choline transporter and 23.4% identity with the yeast UG
10 an increased expression of the high-affinity choline transporter and especially the muscarinic M2 rec
13 cerevisiae expresses a single high affinity choline transporter at the plasma membrane, encoded by t
14 gans encodes a high-affinity plasma-membrane choline transporter believed to be rate limiting for ace
15 mpared with evidence from NP rats, increased choline transporter capacity [as indicated by maximum tr
16 rom choline transported by the high-affinity choline transporter (CHT) and reduced ACh content relati
17 riation in the gene encoding the presynaptic choline transporter (CHT) has been linked to attention-d
19 sodium-dependent, hemicholinium-3-sensitive choline transporter (CHT) is believed to sustain acetylc
20 ion in SLC5A7, which encodes the presynaptic choline transporter (CHT), a critical determinant of syn
21 expression and activity of the high-affinity choline transporter (CHT), a molecule that mediates the
22 etyltransferase (ChAT) and the high-affinity choline transporter (ChT), as measured by reverse transc
23 on of the basal forebrain increased cortical choline transporter (CHT)-mediated choline transport in
24 nce indicating plastic mechanisms regulating choline transporter (CHT)-mediated high-affinity choline
31 onal uptake of choline via the high affinity choline transporter (CHT1) is essential for cholinergic
33 ies with mutants deficient in BetT and other choline transporters demonstrated that BetT was responsi
35 evealed that changes were not due to altered choline transporter expression, but rather due to increa
36 ntiporter belonging to the betaine/carnitine/choline transporter family of secondary transporters.
40 underscore the essential role played by the choline transporter in sustaining acetylcholine neurotra
41 the hypothesis that an increased capacity of choline transporters in the right medial prefrontal cort
44 , which labels the presynaptic high-affinity choline transporter, is responsive additionally to nerve
46 tern blotting techniques, we have identified choline transporter-like 1 (CTL1) as a putative complexi
50 stitution in the first extracellular loop of choline transporter-like protein 2, a member of the chol
52 1 encodes a member of a poorly characterized choline transporter-like protein family in plants and an
53 transporter-like protein 2, a member of the choline transporter-like protein family of membrane glyc
55 to transport choline, and the proportion of choline transporters localized in the membrane of synapt
57 l outcomes arising from different classes of choline transporter mutation with distinct disease proce
58 aptic terminals to acquire the high-affinity choline transporter necessary for high-frequency transmi
59 he trafficking of the Caenorhabditis elegans choline transporter orthologue revealed deficits in tran
62 ive frameshift mutation at the C-terminus of choline transporter that was associated with significant
63 report describes the relative roles of three choline transporters, the ABC transporter CbcXWV and two
65 ergic, activity-triggered delivery of silent choline transporters to the plasma membrane, in which no
67 itions, as BetT1 and CbcXWV were the primary choline transporters under hypo-osmolar conditions where
69 uld directly interact with the high-affinity choline transporter which may impair steady-state and on
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