For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
Inviting an author to review:
Plasma Carnitine Levels in Patients Undergoing Hemodialysis
Find an author and click ‘Invite to review selected article’ near their name.
Search for authorsSearch for similar articles
26
views
140
references
 Top references
cited by
41
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      251
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      TRPV1: A Target for Rational Drug Design

      review-article
      Author(s): 1 , * , 2 , *
      Editor(s): ,
      Publication date (Electronic):
      Journal: Pharmaceuticals
      Publisher: MDPI
      Keywords: TRPV1, capsaicin, vanilloid, pain, nociception

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Transient Receptor Potential Vanilloid 1 (TRPV1) is a non-selective, Ca 2+ permeable cation channel activated by noxious heat, and chemical ligands, such as capsaicin and resiniferatoxin (RTX). Many compounds have been developed that either activate or inhibit TRPV1, but none of them are in routine clinical practice. This review will discuss the rationale for antagonists and agonists of TRPV1 for pain relief and other conditions, and strategies to develop new, better drugs to target this ion channel, using the newly available high-resolution structures.

          Related collections

          Most cited references140

          • Record: found
          • Abstract: found
          • Article: not found

          Structure of the TRPV1 ion channel determined by electron cryo-microscopy

          Maofu Liao, Erhu Cao, David Julius … (2013)
          Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been hampered by a lack of detailed structural information. Here, we exploit advances in electron cryo-microscopy to determine the structure of a mammalian TRP channel, TRPV1, at 3.4Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Like voltage-gated channels, TRPV1 exhibits four-fold symmetry around a central ion pathway formed by transmembrane helices S5–S6 and the intervening pore loop, which is flanked by S1–S4 voltage sensor-like domains. TRPV1 has a wide extracellular ‘mouth’ with short selectivity filter. The conserved ‘TRP domain’ interacts with the S4–S5 linker, consistent with its contribution to allosteric modulation. Subunit organization is facilitated by interactions among cytoplasmic domains, including N-terminal ankyrin repeats. These observations provide a structural blueprint for understanding unique aspects of TRP channel function.
          Article 0 comments Cited 590 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            TRP channels as cellular sensors.

            David Clapham (2003)
            TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.
            Article 0 comments Cited 589 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Impaired nociception and pain sensation in mice lacking the capsaicin receptor.

              M. J. Caterina, A. Leffler, A. Malmberg … (2000)
              The capsaicin (vanilloid) receptor VR1 is a cation channel expressed by primary sensory neurons of the "pain" pathway. Heterologously expressed VR1 can be activated by vanilloid compounds, protons, or heat (>43 degrees C), but whether this channel contributes to chemical or thermal sensitivity in vivo is not known. Here, we demonstrate that sensory neurons from mice lacking VR1 are severely deficient in their responses to each of these noxious stimuli. VR1-/- mice showed normal responses to noxious mechanical stimuli but exhibited no vanilloid-evoked pain behavior, were impaired in the detection of painful heat, and showed little thermal hypersensitivity in the setting of inflammation. Thus, VR1 is essential for selective modalities of pain sensation and for tissue injury-induced thermal hyperalgesia.
              Article 0 comments Cited 569 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Arpad Szallasi: Role: Academic Editor
                Susan M. Huang: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Pharmaceuticals (Basel)
                Journal ID (iso-abbrev): Pharmaceuticals (Basel)
                Journal ID (publisher-id): pharmaceuticals
                Title: Pharmaceuticals
                Publisher: MDPI
                ISSN (Electronic): 1424-8247
                Publication date (Electronic): 23 August 2016
                Publication date Collection: September 2016
                Volume: 9
                Issue: 3
                Electronic Location Identifier: 52
                Affiliations
                [1 ]Institute for Computational Molecular Science, Temple University, Philadelphia, PA 19122, USA
                [2 ]New Jersey Medical School, Rutgers University, Newark, NJ 07103, USA
                Author notes
                [* ]Correspondence: vincenzo.carnevale@ 123456temple.edu (V.C.); tibor.rohacs@ 123456rutgers.edu (T.R.); Tel.: +1-215-204-4214 (V.C.); +1-973-972-4464 (T.R.)
                Article
                Publisher ID: pharmaceuticals-09-00052
                DOI: 10.3390/ph9030052
                PMC ID: 5039505
                PubMed ID: 27563913
                SO-VID: 717d2b15-6ce8-4569-aaa8-c49711909761
                Copyright © © 2016 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 13 July 2016
                Date accepted : 18 August 2016
                Categories
                Subject: Review

                Keywords: trpv1,capsaicin,vanilloid,pain,nociception
                Data availability:
                Keywords: trpv1, capsaicin, vanilloid, pain, nociception

                Comments

                Comment on this article

                scite_

                Similar content251

                See all similar

                Cited by40

                See all cited by

                Most referenced authors2,183

                See all reference authors