Evidence map›Paper›PMID 35287474›Full record

ReviewAnnual review of biochemistry2022

Sensory TRP Channels in Three Dimensions.

Melinda M Diver, John V Lin King, David Julius, Yifan Cheng

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  6. Review
  7. Review
  8. Review
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  10. Review
  11. Review
  12. Article
  13. Article
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  18. Review
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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.

Melinda M DiverDepartment of Physiology, University of California, San Francisco, California, USA; email: david.julius@ucsf.edu.
John V Lin KingDepartment of Physiology, University of California, San Francisco, California, USA; email: david.julius@ucsf.edu.
David JuliusDepartment of Physiology, University of California, San Francisco, California, USA; email: david.julius@ucsf.edu.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, California, USA; email: yifan.cheng@ucsf.edu.

Funding

Natural products as probes of the pain pathwayR35NS105038 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 2018 to 2025
$9.0M
Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Advancing cryo-EM technology to address difficult biological questionsR35GM140847 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Yifan Cheng · 2021 to 2026
$2.1M
Acquisition of an electron microscope for high-resolution single particle cryo-EMS10OD021741 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2016 to 2016
$2.0M
Glacios™ Cryo Transmission Electron Microscope with 200 kV XFEG opticsS10OD026881 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2019 to 2019
$1.8M
Mechanistic studies of the menthol receptor TRPM8: a novel target for analgesic drugsR00AT010478 · NCCIH · SLOAN-KETTERING INST CAN RESEARCH · PI DIVER, MELINDA · 2021 to 2023
$738k
Linux cluster for near atomic resolution single particle cryo-EMS10OD020054 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2015 to 2015
$456k
Mechanistic studies of the menthol receptor TRPM8: a novel target for analgesic drugsK99AT010478 · NCCIH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DIVER, MELINDA · 2019 to 2020
$242k
Howard Hughes Medical InstituteNCCIH NIH HHS K99 AT010478NCCIH NIH HHS R00 AT010478NIGMS NIH HHS R01 GM098672NIGMS NIH HHS R35 GM140847NIH HHS S10 OD020054NIH HHS S10 OD021741NIH HHS S10 OD026881NINDS NIH HHS R35 NS105038
6 · The paper itself

Abstract

Transient receptor potential (TRP) ion channels are sophisticated signaling machines that detect a wide variety of environmental and physiological signals. Every cell in the body expresses one or more members of the extended TRP channel family, which consists of over 30 subtypes, each likely possessing distinct pharmacological, biophysical, and/or structural attributes. While the function of some TRP subtypes remains enigmatic, those involved in sensory signaling are perhaps best characterized and have served as models for understanding how these excitatory ion channels serve as polymodal signal integrators. With the recent resolution revolution in cryo-electron microscopy, these and other TRP channel subtypes are now yielding their secrets to detailed atomic analysis, which is beginning to reveal structural underpinnings of stimulus detection and gating, ion permeation, and allosteric mechanisms governing signal integration. These insights are providing a framework for designing and evaluating modality-specific pharmacological agents for treating sensory and other TRP channel-associated disorders.

Indexed as

Transient Receptor Potential ChannelsCryoelectron MicroscopySignal TransductionTransient Receptor Potential Channelscryo-EMmembrane protein structuresensory biologyTRP channels

Identifiers

PMID35287474
PMCPMC9233036

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.