Evidence map›Paper›PMID 34014518›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

PDZ Sample Quality Assessment by Biochemical and Biophysical Characterizations.

Célia Caillet-Saguy, Sébastien Brûlé, Nicolas Wolff, Bertrand Raynal

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

Célia Caillet-Saguy *Institut Pasteur, Unité Récepteurs-Canaux, CNRS UMR 3571, Paris, France.
Sébastien Brûlé *Institut Pasteur, Plate-forme de Biophysique Moléculaire, CNRS UMR 3528, Paris, France.
Nicolas WolffInstitut Pasteur, Unité Récepteurs-Canaux, CNRS UMR 3571, Paris, France. nicolas.wolff@pasteur.fr.
Bertrand RaynalInstitut Pasteur, Plate-forme de Biophysique Moléculaire, CNRS UMR 3528, Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PDZ domains are small globular domains involved in protein-protein interactions. They participate in a wide range of critical cellular processes. These domains, very abundant in the human proteome, are widely studied by high-throughput interactomics approaches and by biophysical and structural methods. However, the quality of the results is strongly related to the optimal folding and solubility of the domains. We provide here a detailed description of protocols for a strict quality assessment of the PDZ constructs. We describe appropriate experimental approaches that have been selected to overcome the small size of such domains to check the purity, identity, homogeneity, stability, and folding of samples.

Indexed as

BiophysicsPDZ DomainsProtein FoldingBinding SitesElectrophoresis, CapillaryHumansMass SpectrometryMicrotubule-Associated ProteinsModels, MolecularProtein BindingProtein ConformationProtein Serine-Threonine KinasesMAST2 protein, humanMicrotubule-Associated ProteinsProtein Serine-Threonine KinasesBiophysical techniquesFoldingIdentityPDZ domainProtein samplePurityQuality controlQuantificationStabilityStructure

Identifiers

PMID34014518

What Socratic holds

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Registered trials

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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 Socratic graph.