Functional organization of PLC signaling microdomains in neurons
Trends in Neurosciences, ISSN: 0166-2236, Vol: 27, Issue: 1, Page: 41-47
2004
- 71Citations
- 95Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations71
- Citation Indexes71
- 71
- CrossRef62
- Captures95
- Readers95
- 95
Review Description
Our understanding of receptor transduction systems has grown impressively in recent years as a result of intense efforts to characterize signaling molecules and cascades in neurons. A large body of evidence has recently accrued regarding the fast and effective signal transfer that occurs during phosphoinositide signaling. In particular, dissection of the Drosophila phototransduction pathway has enabled a greater understanding of the molecular organization of phospholipase C (PLC) signaling. Supramolecular complexes organize the correct repertoires of receptors, enzymes and ion channels into individual signaling pathways. Such mechanisms involve localization of signaling molecules to sites of action by scaffold and anchoring proteins, ensuring speed and specificity of signal transduction events. However, not all PLC signals nucleate around scaffold proteins, although mechanisms for selectivity and discrimination remain. This article reviews recent advances on the molecular organization and functional consequences of PLC signaling domains, which link membrane receptors to ion channels, including TRP and KCNQ channels.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0166223603003722; http://dx.doi.org/10.1016/j.tins.2003.10.013; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0348047605&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/14698609; https://linkinghub.elsevier.com/retrieve/pii/S0166223603003722; https://dx.doi.org/10.1016/j.tins.2003.10.013
Elsevier BV
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