ArticleJournal of molecular neuroscience : MN1998
Production and functional expression of an epitope-tagged human choline acetyltransferase.
Article in Journal of molecular neuroscience : MN, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed, 4 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
cDNA containing the entire coding region of the human choline acetyltransferase gene (hChAT) was fused to the influenza virus hemagglutinin (HA) epitope preceded by a Kozak sequence. The recombinant HA-hChAT was then inserted into an expression vector under the transcriptional control of the cytomegalovirus (CMV) promoter. After transient transfection into COS-1 cells, expression was assayed by Northern and Western blot analysis and immunofluorescence. The chimeric HA-hChAT protein was compared to native hChAT for its ability to synthesize acetylcholine. It behaves identically to unmodified hChAT showing that the HA epitope does not affect ChAT activity. This approach enables one to distinguish the expression of the HA-hChAT from endogenous ChAT. Genetically engineered cells that express a high level of HA-hChAT could be used as a promising experimental tool for gene transfer and neurografting techniques as well as to produce and study transgenic mice.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.