Evidence map›Paper›PMID 34099182›Full record

ArticleMethods in enzymology2021

Sample preparation of the human TRPA1 ion channel for cryo-EM studies.

Yang Suo, Seok-Yong Lee

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 1 institution in 1 country.

Yang SuoDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, United States.
Seok-Yong LeeDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, United States. Electronic address: seok-yong.lee@duke.edu.
Duke University · US

Funding

Structure, function, and pharmacology of neuronal membrane transport proteinsR35NS097241 · NINDS · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2016 to 2023
$6.1M
NINDS NIH HHS R35 NS097241
6 · The paper itself

Abstract

The transient receptor potential ankyrin 1 (TRPA1) ion channel is a member of the TRP channel family that is involved in sensing noxious stimuli that elicit pain and inflammation. Because of its critical physiological role and therapeutic importance, great efforts have been made to understand the structure and mechanism of TRPA1. Several human TRPA1 structures have been reported using single particle cryo-electron microscopy (cryo-EM) over the last 6 years. Here, we present a protocol for the heterologous expression, large-scale purification, and nanodisc reconstitution of the human TRPA1 channel for cryo-EM and biochemical studies.

Indexed as

Transient Receptor Potential ChannelsCryoelectron MicroscopyCytoskeletal ProteinsHumansPainTRPA1 Cation ChannelCytoskeletal ProteinsTransient Receptor Potential ChannelsTRPA1 Cation ChannelTRPA1 protein, humanCryo-EMIon channelNanodiscRecombinant protein expressionTRPA1 channelTRP channels

Identifiers

PMID34099182
PMCPMC10316410
OpenAlexW3124821739

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.