AbstractTo elucidate the mechanisms underlying acetylcholinesterase (AChE) localization, we analyzed the distribution of AChE and Ache mRNA during myogenesis in cocultures of human muscle and fetal rat spinal cord. We observed a temporal coincidence in alterations of AChE localization and nuclei expressing the message, suggesting developmental regulation at the mRNA level. Nonuniform mRNA staining among nuclei suggests asynchronous regulation, also supporting an earlier proposal that transcription proceeds intermittently. Asynchrony seems to be overridden by generally acting factors during myoblast fusion, when message is up-regulated, and at the onset of muscle contractions, when it becomes restricted to some nuclei in the junctional regio...
In vertebrate neuromuscular junctions, the postsynaptic specializations include the accumulation of ...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...
AbstractTo elucidate the mechanisms underlying acetylcholinesterase (AChE) localization, we analyzed...
Neural signals modulate acetylcholinesterase (AChE) expression in skeletal muscle cells. However, th...
Mammalian acetylcholinesterase (AChE) gene expression is exquisitely regulated in target tissues and...
The AChE gene encodes three mRNAs; R, H and T differing in their choice of C-terminal exons. Of thes...
Acetycholinesterase (AChE) localizes at vertebrate neuromuscular junctions to hydrolyse acetylcholin...
Acetylcholinesterase (AChE) is well known to process different molecular forms via the distinct inte...
Acetylcholinesterase (AChE) is highIy concentrated at vertebrate neuromuscular junctions. Several li...
Presynaptic motor neuron synthesizes and secretes acetylcholinesterase (AChE) at vertebrate neuromus...
Post-transcriptional mechanisms regulating acetylcholinesterase (AChE) expression in muscle and neur...
Acetylcholinesterase (AChE) is responsible for the rapid hydrolysis of acetylcholine into acetic aci...
During myogenesis, marked increases in both acetylcholinesterase (AChE) and its encoding mRNA are ob...
The transcriptional regulation of proline-rich membrane anchor ( PRiMA), an anchoring protein of tet...
In vertebrate neuromuscular junctions, the postsynaptic specializations include the accumulation of ...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...
AbstractTo elucidate the mechanisms underlying acetylcholinesterase (AChE) localization, we analyzed...
Neural signals modulate acetylcholinesterase (AChE) expression in skeletal muscle cells. However, th...
Mammalian acetylcholinesterase (AChE) gene expression is exquisitely regulated in target tissues and...
The AChE gene encodes three mRNAs; R, H and T differing in their choice of C-terminal exons. Of thes...
Acetycholinesterase (AChE) localizes at vertebrate neuromuscular junctions to hydrolyse acetylcholin...
Acetylcholinesterase (AChE) is well known to process different molecular forms via the distinct inte...
Acetylcholinesterase (AChE) is highIy concentrated at vertebrate neuromuscular junctions. Several li...
Presynaptic motor neuron synthesizes and secretes acetylcholinesterase (AChE) at vertebrate neuromus...
Post-transcriptional mechanisms regulating acetylcholinesterase (AChE) expression in muscle and neur...
Acetylcholinesterase (AChE) is responsible for the rapid hydrolysis of acetylcholine into acetic aci...
During myogenesis, marked increases in both acetylcholinesterase (AChE) and its encoding mRNA are ob...
The transcriptional regulation of proline-rich membrane anchor ( PRiMA), an anchoring protein of tet...
In vertebrate neuromuscular junctions, the postsynaptic specializations include the accumulation of ...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of...