Evidence map›Paper›PMID 24681231›Full record

ReviewCurrent opinion in structural biology2014

Single particle electron cryo-microscopy of a mammalian ion channel.

Maofu Liao, Erhu Cao, David Julius, Yifan Cheng

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed.

  1. Article
  2. Review
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  9. Article
  10. A heuristic derived from analysis of the ion channel structural proteome permits the rapid identification of hydrophobic gates.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
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  18. Dawning of a new era in TRP channel structural biology by cryo-electron microscopy.Pflugers Archiv : European journal of physiology · 2018
    Review
  19. Review
  20. Review
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

4 authors.

Maofu LiaoDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA 94158-2517, USA.
Erhu CaoDepartment of Physiology, University of California, San Francisco, CA 94158-2517, USA.
David JuliusDepartment of Physiology, University of California, San Francisco, CA 94158-2517, USA. Electronic address: David.Julius@ucsf.edu.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA 94158-2517, USA. Electronic address: ycheng@ucsf.edu.

Funding

Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Molecular Mechanisms of Receptor and Channel FunctionR01NS047723 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 2012 to 2016
$2.2M
Exploiting toxins to probe sensory signalingR01NS065071 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 2009 to 2012
$1.3M
GPU Computing Enabled Linux Computer ClusterS10RR026814 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2010 to 2010
$228k
NCRR NIH HHS S10 RR026814NCRR NIH HHS S10RR026814NIGMS NIH HHS R01 GM098672NIGMS NIH HHS R01GM098672NINDS NIH HHS R01 NS047723NINDS NIH HHS R01NS047723NINDS NIH HHS R01 NS065071NINDS NIH HHS R01NS065071
6 · The paper itself

Abstract

The transient receptor potential (TRP) ion channel family is large and functionally diverse, second only to potassium channels. Despite their prominence within the animal kingdom, TRP channels have resisted crystallization and structural determination for many years. This barrier was recently broken when the three-dimensional structure of the vanilloid receptor 1 (TRPV1) was determined by single particle electron cryo-microscopy (cryo-EM). Moreover, this is the first example in which the near atomic resolution structure of an integral membrane protein was elucidated by this technique and in a manner not requiring crystals, demonstrating the transformative power of single particle cryo-EM for revealing high-resolution structures of integral membrane proteins, particularly those of mammalian origin. Here we summarize technical advances, in both biochemistry and cryo-EM, that led to this major breakthrough.

Indexed as

MammalsAnimalsCryoelectron MicroscopyTRPV Cation ChannelsTRPV Cation Channels

Identifiers

PMID24681231
PMCPMC4176607

What OpenQuestion holds

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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.