Title : Engineering vanilloid-sensitivity into the rat TRPV2 channel.

Pub. Date : 2016 May 13

PMID : 27177419






3 Functional Relationships(s)
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1 Here we use biochemical and electrophysiological approaches to investigate the resiniferatoxin(RTx) binding site in TRPV1 and to explore the functional relationships between TRPV1 and TRPV2. resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
2 Here we use biochemical and electrophysiological approaches to investigate the resiniferatoxin(RTx) binding site in TRPV1 and to explore the functional relationships between TRPV1 and TRPV2. resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
3 Moreover, we show that sensitivity to RTx can be engineered into TRPV2, demonstrating that the gating and permeation properties of this channel are similar to TRPV1. resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus