Evidence map›Paper›PMID 21290288›Full record

ReviewAdvances in experimental medicine and biology2011

Functional and structural studies of TRP channels heterologously expressed in budding yeast.

Vera Moiseenkova-Bell, Theodore G Wensel

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024
    Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Structure of thermally activated TRP channels.Current topics in membranes · 2014
    Review
  12. 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

2 authors at 2 institutions in 1 country.

Vera Moiseenkova-BellDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA. vxm102@case.edu
Theodore G Wensel
Baylor College of Medicine · USUniversity School · US

Funding

Trasnducin Interactions with Photoreceptor MembranesR01EY007981 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1989 to 2016
$6.1M
RGS Protein Function in Mammalian RetinaR01EY011900 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1998 to 2010
$4.4M
NEI NIH HHS R01 EY007981NEI NIH HHS R01 EY011900
6 · The paper itself

Abstract

The transient receptor potential (TRP) superfamily is one of the largest families of cation channels. The metazoan TRP family has been subdivided into major branches: TRPC, TRPA, TRPM, TRPP, TRPV, TRPML, and TRPN, while the TRPY family is found in fungi. They are involved in many physiological processes and in the pathogenesis of various disorders. An efficient high-yield expression system for TRP channels is a necessary step towards biophysical and biochemical characterization and structural analysis of these proteins, and the budding yeast, Saccharomyces cerevisiae has proven to be very useful for this purpose. In addition, genetic screens in this organism can be carried out rapidly to identify amino acid residues important for function and to generate useful mutants. Here we present an overview of current developments towards understanding TRP channel function and structure using Saccharomyces cerevisiae as an expression system. In addition, we will summarize recent progress in understanding gating mechanisms of TRP channels using endogenously expressing TRPY channels in S. cerevisiae, and insights gained from genetic screens for mutants in mammalian channels. The discussion will focus particular attention of the use of cryo-electron microscopy (cryo-EM) to determine TRP channel structure, and outlines a "divide and concur" methodology for combining high resolution structures of TRP channel domains determined by X-ray crystallography with lower resolution techniques including cryo-EM and spectroscopy.

Indexed as

Cryoelectron MicroscopyProtein ConformationRecombinant ProteinsSaccharomyces cerevisiaeTransient Receptor Potential ChannelsRecombinant ProteinsTransient Receptor Potential Channels

Identifiers

PMID21290288
PMCPMC3615646
OpenAlexW2130033876

What OpenQuestion holds

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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.