ArticleProceedings of the National Academy of Sciences of the United States of America1991
Cytosolic rat brain synapsin I is a diacylglycerol kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Calcium-Dependent and Synapsin-Dependent Pathways for the Presynaptic Actions of BDNF.Frontiers in cellular neuroscience · 2017Article
- Bacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Scientific reports · 2013Article
- Synapsins as regulators of neurotransmitter release.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999Review
- Activated protein kinase C alpha associates with annexin VI from skeletal muscle.The Biochemical journal · 1998Article
- Synapsin I is structurally similar to ATP-utilizing enzymes.The EMBO journal · 1998Article
- Isolation and characterization of the human diacylglycerol kinase gene.The Biochemical journal · 1993Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phosphorylation of diacylglycerol (DG), a reaction catalyzed by DG kinase, may be critical in the termination of effector-induced signals mediated by protein kinase C. Synapsin I is a principal target of intracellular protein kinases and is thought to be involved in the release of neurotransmitter from axon terminals. We present several lines of evidence which indicate that rat brain synapsin, in addition to this role, may function as a DG kinase. Purified rat brain DG kinase was digested with trypsin, which produced three major fragments whose sequence was identical to three regions in synapsin I. Using a rabbit anti-synapsin polyclonal antiserum, the elution profile of synapsin immunoreactivity coincided exactly with that of DG kinase activity in column fractions from the final step in the DG kinase purification procedure. As is the case with synapsin, the purified enzyme was a strongly basic protein with an isoelectric point greater than 10.0. Finally, incubating the DG kinase with highly purified bacterial collagenase, an enzyme that partially degrades the proline- and glycine-rich synapsin, resulted in the simultaneous loss of DG kinase activity and synapsin immunoreactivity. We conclude that cytosolic rat brain synapsin is capable of functioning as a DG kinase.
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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 Socratic graph.