Evidence map›Paper›PMID 34975936›Full record

ArticleFrontiers in plant science2021

A Redox-Sensitive Cysteine Is Required for PIN1At Function.

Benjamin Selles, Tiphaine Dhalleine, Alexis Boutilliat, Nicolas Rouhier, Jérémy Couturier

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 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 87% 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

5 authors at 2 institutions in 1 country.

Benjamin SellesUniversité de Lorraine, INRAE, IAM, Nancy, France.
Tiphaine DhalleineUniversité de Lorraine, INRAE, IAM, Nancy, France.
Alexis BoutilliatUniversité de Lorraine, INRAE, IAM, Nancy, France.
Nicolas RouhierUniversité de Lorraine, INRAE, IAM, Nancy, France.
Jérémy CouturierUniversité de Lorraine, INRAE, IAM, Nancy, France.
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRInstitut Universitaire de France · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parvulins are ubiquitous peptidyl-prolyl isomerases (PPIases) required for protein folding and regulation. Among parvulin members, Arabidopsis PIN1At, human PIN1, and yeast ESS1 share a conserved cysteine residue but differ by the presence of an N-terminal WW domain, absent in PIN1At. In this study, we have explored whether the cysteine residue of Arabidopsis PIN1At is involved in catalysis and subject to oxidative modifications. From the functional complementation of yeast

Indexed as

cysteine oxidationparvulinpeptidyl-prolyl cis/trans isomerasesplantthioredoxin

Identifiers

PMID34975936
PMCPMC8716364
OpenAlexW4200408248

What OpenQuestion holds

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LicenceCC BY
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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.