{"doi":"10.1111/febs.12302","title":"What do we know about the transient receptor potential vanilloid 2 (<scp>TRPV</scp>2) ion channel?","abstract":"<jats:p>Transient receptor potential (<jats:styled-content style=\"fixed-case\">TRP</jats:styled-content>) ion channels are emerging as a new set of membrane proteins involved in a vast array of cellular processes and regulated by a large number of physical and chemical stimuli, which involves them with sensory cell physiology. The vanilloid <jats:styled-content style=\"fixed-case\">TRP</jats:styled-content> subfamily (<jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>) named after the vanilloid receptor 1 (<jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>1) consists of six members, and at least four of them (<jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>1–<jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>4) have been related to thermal sensation. One of the least characterized members of the <jats:styled-content style=\"fixed-case\">TRP</jats:styled-content> subfamily is <jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>2. Although initially characterized as a noxious heat sensor, <jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>2 now seems to have little to do with temperature sensing but a much more complex physiological profile. Here we review the available information and research progress on the structure, physiology and pharmacology of <jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>2 in an attempt to shed some light on the physiological and pharmacological deorphanization of <jats:styled-content style=\"fixed-case\">TRPV</jats:styled-content>2.</jats:p>","journal":"The FEBS Journal","year":2013,"id":26640,"datarank":6.891510954576753,"base_score":5.176149732573829,"endowment":5.176149732573829,"self_citation_contribution":0.7764224598860744,"citation_network_contribution":6.115088494690679,"self_endowment_contribution":0.7764224598860744,"citer_contribution":6.115088494690679,"corpus_percentile":null,"corpus_rank":null,"citation_count":176,"citer_count":170,"citers_with_citation_signal":155,"citers_with_endowment":155,"datacite_reuse_total":7,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":153651,"name":"Pau Doñate‐Macian","orcid":null,"position":1,"is_corresponding":false},{"id":147913,"name":"Rachelle Gaudet","orcid":null,"position":2,"is_corresponding":false},{"id":153650,"name":"Alex Perálvarez‐Marín","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":7,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23615321","pmcid":"PMC3783526","openalex_id":null,"authors":[],"funders":[{"funder_name":"Spanish Government Young Researcher Grant","grant_id":"MICINN-SAF2010-21385","title":null},{"funder_name":"7th European Community Framework Programme","grant_id":"PIOF-GA-2009-237120","title":null},{"funder_name":"National Institutes of Health","grant_id":"R01GM081340","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01GM081340-03","title":"Structure and Function of TRPV Ion Channels"},{"funder_name":"European Commission","grant_id":"237120","title":"Single Particle Cryo-Electron Microscopy and Biophysical Characterization of Transient Receptor Potential Vanilloid 2 channel: a Three-Dimensional Structure Characterization of a Membrane Nociceptor."},{"funder_name":"Marie Curie International Outgoing Fellowship","grant_id":"","title":null}],"total_grants":6,"fwci":null,"citation_percentile":null,"influential_citations":10,"citation_trend":[],"oa_status":"bronze","license":"Wiley Online Library User Agreement","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/febs.12302","host_type":"BRONZE"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/febs.12302","host_type":"publisher"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.12302","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12302","host_type":"publisher"},{"url":"http://nrs.harvard.edu/urn-3:HUL.InstRepos:12410513","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3783526","host_type":"repository"},{"url":"https://doi.org/10.1111/febs.12302","host_type":""},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1111/febs.12302","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/23615321","host_type":""},{"url":"https://dx.doi.org/10.1111/febs.12302","host_type":""},{"url":"https://doi.org/https://doi.org/10.1111/febs.12302","host_type":""}],"fields_of_study":["Biology","Medicine","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Calcium Channels","Cardiotonic Agents","Cardiovascular Diseases","Gene Expression Regulation","Humans","Mice","Molecular Targeted Therapy","TRPV Cation Channels"],"mesh_terms":["Animals","Humans","Mice","Cardiovascular Diseases","Calcium Channels","Cardiotonic Agents","Gene Expression Regulation","TRPV Cation Channels","Molecular Targeted Therapy"],"keywords":["Pharmacology","Ion channels","Cancer","Neuroscience","immunology","endocrinology","Somatosensation","Calcium Signalling","Trpv2","Muscle Physiology","Cardiotonic Agents","610","TRPV Cation Channels","Mice","Gene Expression Regulation","Cardiovascular Diseases","Animals","Humans","Calcium Channels","Molecular Targeted Therapy"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. Good health"}],"linked_datasets":[{"doi":"10.6084/m9.figshare.20317646.v1","title":"Additional file 5 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.20317646","title":"Additional file 5 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.20317640.v1","title":"Additional file 3 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"Dataset"},{"doi":"10.6084/m9.figshare.20317640","title":"Additional file 3 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"Dataset"},{"doi":"10.6084/m9.figshare.20317637","title":"Additional file 2 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"Dataset"},{"doi":"10.6084/m9.figshare.20317634","title":"Additional file 1 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"Dataset"},{"doi":"10.6084/m9.figshare.20317634.v1","title":"Additional file 1 of Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis","publisher":"figshare","resource_type":"Dataset"}],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"uniprot"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-08T15:04:57.259936Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}