Evidence map›Paper›PMID 36448355›Full record

ArticleChembiochem : a European journal of chemical biology2023

Biochemical and Structural Insights into FIH-Catalysed Hydroxylation of Transient Receptor Potential Ankyrin Repeat Domains.

Benjamin G Saward, Thomas M Leissing, Ian J Clifton, Anthony Tumber, Christopher M Timperley, Richard J Hopkinson, Christopher J Schofield

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

Article in Chembiochem : a European journal of chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 45% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 2 countries.

Benjamin G SawardDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.
Thomas M LeissingDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.
Ian J CliftonDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.
Anthony TumberDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.
Christopher M TimperleyCBR Division, Defence Science and Technology Laboratory (DSTL), Porton Down, Salisbury, SP4 0JQ, UK.
Richard J HopkinsonDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.
Christopher J SchofieldDepartment of Chemistry and the, Ineos Oxford Institute for Antimicrobial Research, Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford, OX1 3TA, UK.ORCID 0000-0002-0290-6565
Mansfield University · USDefence Science and Technology Laboratory · GB

Funding

Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

Transient receptor potential (TRP) channels have important roles in environmental sensing in animals. Human TRP subfamily A member 1 (TRPA1) is responsible for sensing allyl isothiocyanate (AITC) and other electrophilic sensory irritants. TRP subfamily vanilloid member 3 (TRPV3) is involved in skin maintenance. TRPV3 is a reported substrate of the 2-oxoglutarate oxygenase factor inhibiting hypoxia-inducible factor (FIH). We report biochemical and structural studies concerning asparaginyl hydroxylation of the ankyrin repeat domains (ARDs) of TRPA1 and TRPV3 catalysed by FIH. The results with ARD peptides support a previous report on FIH-catalysed TRPV3 hydroxylation and show that, of the 12 potential TRPA1 sequences investigated, one sequence (TRPA1 residues 322-348) undergoes hydroxylation at Asn336. Structural studies reveal that the TRPA1 and TRPV3 ARDs bind to FIH with a similar overall geometry to most other reported FIH substrates. However, the binding mode of TRPV3 to FIH is distinct from that of other substrates.

Indexed as

Ankyrin RepeatRespiratory Distress SyndromeAmino Acid SequenceAnimalsHumansHydroxylationHypoxia-Inducible Factor 1, alpha SubunitMixed Function OxygenasesProtein BindingRepressor ProteinsHypoxia-Inducible Factor 1, alpha SubunitMixed Function OxygenasesRepressor Proteinsankyrinfactor inhibiting HIF (FIH)hypoxia inducible factor HIFoxygenases, demethylasespost translational modificationstransient receptor potential (TRP) channel

Identifiers

PMID36448355
PMCPMC10946520
OpenAlexW4310456508

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.