Evidence map›Paper›PMID 38861081›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Purification of Recombinant N-terminal Histidine-Tagged Arabidopsis thaliana Phosphoglycolate Phosphatase 1, Glycolate Oxidase 1 and 2, and Hydroxypyruvate Reductase 1.

Mathieu Jossier, Céline Oury, Nathalie Glab, Michael Hodges

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. 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
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.

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

4 authors.

Mathieu JossierUniversité Paris-Saclay, CNRS, INRAe, Université Paris Cité, Université d'Evry, Institute of Plant Sciences Paris-Saclay (IPS2), Gif-sur-Yvette, France. mathieu.jossier@universite-paris-saclay.fr.
Céline OuryUniversité Paris-Saclay, CNRS, INRAe, Université Paris Cité, Université d'Evry, Institute of Plant Sciences Paris-Saclay (IPS2), Gif-sur-Yvette, France.
Nathalie GlabUniversité Paris-Saclay, CNRS, INRAe, Université Paris Cité, Université d'Evry, Institute of Plant Sciences Paris-Saclay (IPS2), Gif-sur-Yvette, France.
Michael HodgesUniversité Paris-Saclay, CNRS, INRAe, Université Paris Cité, Université d'Evry, Institute of Plant Sciences Paris-Saclay (IPS2), Gif-sur-Yvette, France. michael.hodges@cnrs.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To measure the kinetic properties of photorespiratory enzymes, it is necessary to work with purified proteins. Protocols to purify photorespiratory enzymes from leaves of various plant species require several time-consuming steps. It is now possible to produce large quantities of recombinant proteins in bacterial cells. They can be rapidly purified as histidine-tagged recombinant proteins by immobilized metal affinity chromatography using Ni

Indexed as

Alcohol OxidoreductasesArabidopsis ProteinsEscherichia coliHydroxypyruvate ReductasePhosphoric Monoester HydrolasesRecombinant ProteinsArabidopsisChromatography, AffinityHistidineAlcohol OxidoreductasesArabidopsis Proteinsglycollate oxidaseHistidineHydroxypyruvate Reductasephosphoglycolate phosphatasePhosphoric Monoester HydrolasesRecombinant ProteinsEscherichia coliGlycolate oxidaseHis-tagged recombinant proteinHydroxypyruvate reductaseImmobilized metal affinity chromatographyPhosphoglycolate phosphatasePhotorespirationRapid one-step protein purification

Identifiers

PMID38861081

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.