ArticleJournal of molecular neuroscience : MN1994
Rapid purification, site-directed mutagenesis, and initial characterization of recombinant RC3/neurogranin.
Article in Journal of molecular neuroscience : MN, 1994. 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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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Neurogranin Regulates Metaplasticity.Frontiers in molecular neuroscience · 2019Article
- Neurogranin phosphorylation fine-tunes long-term potentiation.The European journal of neuroscience · 2011Article
- Neurogranin and synaptic plasticity balance.Communicative & integrative biology · 2010Article
- Neurogranin enhances synaptic strength through its interaction with calmodulin.The EMBO journal · 2009Article
- Targeted disruption of RC3 reveals a calmodulin-based mechanism for regulating metaplasticity in the hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- RC3/neurogranin, a postsynaptic calpacitin for setting the response threshold to calcium influxes.Molecular neurobiology · 1997Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
RC3/Neurogranin is a postnatal-onset, forebrain-specific, thyroid hormone-regulated, protein kinase C (PKC) substrate that binds calmodulin (CaM) and accumulates in dendritic spines. We bacterially expressed and purified RC3 and, for comparison, GAP-43/neuromodulin to near homogeneity using relatively simple procedures. We then raised antisera against recombinant RC3 that does not crossreact with GAP-43 and is suitable for immunohistochemical analysis of brain slices. We also constructed over 30 RC3 sequence variants by PCR-mediated, site-directed mutagenesis, and purified four of these to near homogeneity. The elution profiles displayed by RC3 and sequence variants during purification on CaM-Sepharose columns suggest that two different affinity forms of the RC3.CaM complex coexist when Ca2+ is absent and that GAP-43.CaM interactions are far more sensitive to salt than those that occur between recombinant RC3 and CaM. Variant proteins in which serine 36 was changed failed to serve as a substrate for PKC, implicating this as the target residue.
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Registered trials
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