Evidence map›Paper›PMID 27875296›Full record

ArticleThe Journal of biological chemistry2016

The N-terminal Ankyrin Repeat Domain Is Not Required for Electrophile and Heat Activation of the Purified Mosquito TRPA1 Receptor.

Sabeen Survery, Lavanya Moparthi, Per Kjellbom, Edward D Högestätt, Peter M Zygmunt, Urban Johanson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. iScience · 2024
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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

6 authors at 1 institution in 1 country.

Sabeen SurveryFrom the Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, SE-221 00 Lund, Sweden and.ORCID http://orcid.org/0000-0001-6740-5430
Lavanya MoparthiFrom the Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, SE-221 00 Lund, Sweden and.ORCID http://orcid.org/0000-0002-6030-3084
Per KjellbomFrom the Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, SE-221 00 Lund, Sweden and.ORCID http://orcid.org/0000-0001-5813-0033
Edward D Högestättthe Clinical Chemistry and Pharmacology, Department of Laboratory Medicine, Lund University, SE-221 85 Lund, Sweden.ORCID http://orcid.org/0000-0002-4890-2463
Peter M Zygmuntthe Clinical Chemistry and Pharmacology, Department of Laboratory Medicine, Lund University, SE-221 85 Lund, Sweden peter.zygmunt@med.lu.se.ORCID http://orcid.org/0000-0002-5102-8199
Urban JohansonFrom the Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, SE-221 00 Lund, Sweden and urban.johanson@biochemistry.lu.se.ORCID http://orcid.org/0000-0001-8862-128X
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Temperature sensors are crucial for animals to optimize living conditions. The temperature response of the ion channel transient receptor potential A1 (TRPA1) is intriguing; some orthologs have been reported to be activated by cold and others by heat, but the molecular mechanisms responsible for its activation remain elusive. Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. The proteins' similar intrinsic fluorescence properties and corresponding quenching when activated by allyl isothiocyanate or heat suggest lipid bilayer-independent conformational changes outside the N-terminal domain. The results show that AgTRPA1 is an inherent thermo- and chemoreceptor, and analogous to what has been reported for the human TRPA1 ortholog, the N-terminal domain may tune the response but is not required for the activation by these stimuli.

Indexed as

Ankyrin RepeatAmino Acid SequenceAnimalsBinding SitesCold TemperatureCrystallography, X-RayCulicidaeHot TemperatureHumansIon Channel GatingProtein BindingProtein ConformationSequence Homology, Amino AcidTransient Receptor Potential ChannelsTransient Receptor Potential Channelsfluorescenceheat sensingpainpatch clamprepellentsthermosensortransient receptor potential channels (TRP channels)tryptophan

Identifiers

PMID27875296
PMCPMC5207195
OpenAlexW2550367067

What OpenQuestion holds

Textmetadata
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.