ArticleProceedings of the National Academy of Sciences of the United States of America1994
Characterization of a GTP-binding protein implicated in both memory storage and interorganelle vesicle transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 19 citations in OpenAlex.
- The X-ray structure of juvenile hormone diol kinase from the silkworm Bombyx mori.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Crystallization and preliminary X-ray diffraction analysis of calexcitin from Loligo pealei: a neuronal protein implicated in learning and memory.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Calexcitin interaction with neuronal ryanodine receptors.The Biochemical journal · 1999Article
- Calexcitin: a signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances membrane excitability.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Alzheimer and beta-amyloid-treated fibroblasts demonstrate a decrease in a memory-associated GTP-binding protein, Cp20.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phosphorylation state of cp20, a low molecular weight GTP-binding protein that is a high-affinity substrate for protein kinase C, was previously shown to change after associative conditioning of molluscs and mammals and to induce many of the biophysical and structural modifications that accompany memory retention. Here, cp20 was purified from squid optic lobes and biochemically characterized. A monoclonal antibody prepared against squid cp20 reacted with Hermissenda cp20 and a 20-kDa protein in rabbit hippocampus, while a polyclonal antibody also cross-reacted with Sar1p and ADP-ribosylation factor (ARF). A partial peptide sequence of squid cp20 was 50% identical (23/46 amino acids) with Sar1p, a yeast GTP-binding protein involved in vesicle transport, indicating that cp20 is probably a new member of the ARF family. This classification is consistent with our recent demonstration that cp20 affects retrograde movement of intraaxonal organelles or particles and suggests a possible role for particle traffic between intraneuronal organelles in memory acquisition.
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