Evidence map›Paper›PMID 24894720›Full record

ReviewThe Journal of membrane biology2014

Application of amphipols for structure-functional analysis of TRP channels.

Kevin W Huynh, Matthew R Cohen, Vera Y Moiseenkova-Bell

Open access · greenAbstract readComparative StudyReview
In one paragraph

Review in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Dawning of a new era in TRP channel structural biology by cryo-electron microscopy.Pflugers Archiv : European journal of physiology · 2018
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Amphipols for each season.The Journal of membrane biology · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kevin W HuynhDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH, 44106, USA.
Matthew R Cohen
Vera Y Moiseenkova-Bell
Case Western Reserve University · US

Funding

Structural Insights into TRPV Channel GatingR01GM103899 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI MOISEENKOVA-BELL, VERA · 2013 to 2021
$3.2M
NIGMS NIH HHS 1R01GM103899-01A1NIGMS NIH HHS R01 GM103899
6 · The paper itself

Abstract

Amphipathic polymers (amphipols), such as A8-35 and SApol, are a new tool for stabilizing integral membrane proteins in detergent-free conditions for structural and functional studies. Transient receptor potential (TRP) ion channels function as tetrameric protein complexes in a diverse range of cellular processes including sensory transduction. Mammalian TRP channels share ~20 % sequence similarity and are categorized into six subfamilies: TRPC (canonical), TRPV (vanilloid), TRPA (ankyrin), TRPM (melastatin), TRPP (polycystin), and TRPML (mucolipin). Due to the inherent difficulties in purifying eukaryotic membrane proteins, structural studies of TRP channels have been limited. Recently, A8-35 was essential in resolving the molecular architecture of the nociceptor TRPA1 and led to the determination of a high-resolution structure of the thermosensitive TRPV1 channel by cryo-EM. Newly developed maltose-neopentyl glycol (MNG) detergents have also proven to be useful in stabilizing TRP channels for structural analysis. In this review, we will discuss the impacts of amphipols and MNG detergents on structural studies of TRP channels by cryo-EM. We will compare how A8-35 and MNG detergents interact with the hydrophobic transmembrane domains of TRP channels. In addition, we will discuss what these cryo-EM studies reveal on the importance of screening different types of surfactants toward determining high-resolution structures of TRP channels.

Indexed as

AnimalsCell MembraneHumansHydrophobic and Hydrophilic InteractionsPolymersPropylaminesSolubilityStructure-Activity RelationshipSurface-Active AgentsTransient Receptor Potential Channelsamphipol A8-35PolymersPropylaminesSurface-Active AgentsTransient Receptor Potential Channels

Identifiers

PMID24894720
PMCPMC4198461
OpenAlexW2001552312

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.