ArticleScientific reports2016
Temperature-sensitive gating of TRPV1 channel as probed by atomistic simulations of its trans- and juxtamembrane domains.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 66 citations in OpenAlex.
- Perspectives on TRPV Channels in the Structural and Computational Revolution Era.Advances in experimental medicine and biology · 2026Review
- Molecular dynamics simulation of thermal activation of human TRPV1.Molecular biology research communications · 2026Article
- Veraguamide E, a Marine Cyanobacterial Depsipeptide Targeting σJournal of natural products · 2025Article
- Exploring the influence of pore shape on conductance and permeation.Biophysical journal · 2024Article
- Dynamic molecular portraits of ion-conducting pores characterize functional states of TRPV channels.Communications chemistry · 2024Article
- Temperature sensitive contact modes allosterically gate TRPV3.PLoS computational biology · 2023Article
- Structural Mechanism of Ionic Conductivity of the TRPV1 Channel.Doklady. Biochemistry and biophysics · 2023Article
- Using Metadynamics To Explore the Free Energy of Dewetting in Biologically Relevant Nanopores.The journal of physical chemistry. B · 2022Article
- Article
- Potassium channel blocker crafted by α-hairpinin scaffold engineering.Biophysical journal · 2021Article
- Hydropathicity-based prediction of pain-causing NaV1.7 variants.BMC bioinformatics · 2021Article
- Hydrophobic dewetting in gating and regulation of transmembrane protein ion channels.The Journal of chemical physics · 2020Review
- Electric Field Induced Wetting of a Hydrophobic Gate in a Model Nanopore Based on the 5-HTACS nano · 2020Article
- High-resolution structures of transient receptor potential vanilloid channels: Unveiling a functionally diverse group of ion channels.Protein science : a publication of the Protein Society · 2020Review
- Structural mechanisms of transient receptor potential ion channels.The Journal of general physiology · 2020Review
- Novel TRPV1 Channel Agonists With Faster and More Potent Analgesic Properties Than Capsaicin.Frontiers in pharmacology · 2020Article
- Protein surface topography as a tool to enhance the selective activity of a potassium channel blocker.The Journal of biological chemistry · 2019Article
- Confined Dynamics of Water in Transmembrane Pore of TRPV1 Ion Channel.International journal of molecular sciences · 2019Article
- Cytoplasmic Inter-Subunit Interface Controls Use-Dependence of Thermal Activation of TRPV3 Channel.International journal of molecular sciences · 2019Article
- CHAP: A Versatile Tool for the Structural and Functional Annotation of Ion Channel Pores.Journal of molecular biology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-activated transient receptor potential channel TRPV1 is one of the most studied eukaryotic proteins involved in temperature sensation. Upon heating, it exhibits rapid reversible pore gating, which depolarizes neurons and generates action potentials. Underlying molecular details of such effects in the pore region of TRPV1 is of a crucial importance to control temperature responses of the organism. Despite the spatial structure of the channel in both open (O) and closed (C) states is known, microscopic nature of channel gating and mechanism of thermal sensitivity are still poorly understood. In this work, we used unrestrained atomistic molecular dynamics simulations of TRPV1 (without N- and C-terminal cytoplasmic domains) embedded into explicit lipid bilayer in its O- and C-states. We found that the pore domain with its neighboring loops undergoes large temperature-dependent conformational transitions in an asymmetric way, when fragments of only one monomer move with large amplitude, freeing the pore upon heating. Such an asymmetrical gating looks rather biologically relevant because it is faster and more reliable than traditionally proposed "iris-like" symmetric scheme of channel opening. Analysis of structural, dynamic, and hydrophobic organization of the pore domain revealed entropy growth upon TRPV1 gating, which is in line with current concepts of thermal sensitivity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.