The vanilloid receptor: a molecular gateway to the pain pathway.
By M. Caterina, D. Julius. Annual Review of Neuroscience, 2001
1,571 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Physiology, Sensory Systems
View Paper: https://www.semanticscholar.org/paper/fac8d3aa2766ddc01b09e5c965900232161184f9
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In Cellular and Molecular Neuroscience
In Physiology
In Sensory Systems
Citations in the corpus
- Mustard oils and cannabinoids excite sensory nerve fibres through the TRP channel ANKTM1 (2004, background): “Capsaicin-evoked responses result from an influx of divalent cations directly through the TRPV1 channe”
- Transient receptor potential cation channels in disease. (2007, background): “The first evidence for the involvement of TRP channels in the pain pathway came with the cloning of the vanilloid receptor TRPV1, which is arguably the most extensively studied member of the entire TRP superfamily (58).”
- Endocannabinoid signaling and synaptic function (2012, background): “…VR1 for vanilloid receptor type 1 (Caterina et al., 1997), is a polymodal transient receptor potential (TRP) ion channel largely expressed in afferent peripheral sensory neurons, where its activation regulates synaptic transmission associated with pain sensation (Caterina and Julius, 2001).”
- Distinct subsets of unmyelinated primary sensory fibers mediate behavioral responses to noxious thermal and mechanical stimuli (2009, background): “We therefore focused on the large population of TRPV1 nociceptors (20).”
- Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “**TrpV1 channels also called vanilloid receptors that respond to heat and capsaicin (224) are strongly sensitized by bradykinin and other PLC activators, and it was suggested that PtdIns(4,5)P2 breakdown relieves a tonic inhibition of these channels by PtdIns(4,5)P2 (257).”
- Neuronal control of skin function: the skin as a neuroimmunoendocrine organ. (2006, background): “It has higher affinity to CB1 than CB2 and also binds to the TRPV1 ion channel (974).”