Evidence map›Paper›PMID 26053890›Full record

ArticleNature methods2015

Quantifying domain-ligand affinities and specificities by high-throughput holdup assay.

Renaud Vincentelli, Katja Luck, Juline Poirson, Jolanta Polanowska, Julie Abdat, Marilyne Blémont, Jeremy Turchetto, François Iv, Kevin Ricquier, Marie-Laure Straub and 10 more

Abstract read
In one paragraph

Article in Nature methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

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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

20 authors.

Renaud VincentelliUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS)-Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Katja Luckquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Juline Poirsonquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Jolanta PolanowskaUnité 1068 Institut national de la santé et de la recherche médicale (INSERM), UMR 7258, CNRS-Aix-Marseille Université, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Marseille, France.
Julie AbdatUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS)-Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Marilyne BlémontUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS)-Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Jeremy TurchettoUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS)-Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
François IvUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS)-Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Kevin RicquierDépartement de Biologie Structurale et Chimie, Unité de Résonance Magnétique Nucléaire des Biomolécules, Institut Pasteur, UMR 3528, CNRS, Paris, France.
Marie-Laure Straubquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Anne Forsterquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Patricia CassonnetDépartement de Virologie, Unité de Génétique Moléculaire des Virus à ARN, Institut Pasteur, UMR 3569, CNRS, Université Paris Diderot, Paris, France.
Jean-Paul BorgUnité 1068 Institut national de la santé et de la recherche médicale (INSERM), UMR 7258, CNRS-Aix-Marseille Université, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Marseille, France.
Yves JacobDépartement de Virologie, Unité de Génétique Moléculaire des Virus à ARN, Institut Pasteur, UMR 3569, CNRS, Université Paris Diderot, Paris, France.
Murielle Massonquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Yves Nominéquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Jérôme ReboulUnité 1068 Institut national de la santé et de la recherche médicale (INSERM), UMR 7258, CNRS-Aix-Marseille Université, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Marseille, France.
Nicolas WolffDépartement de Biologie Structurale et Chimie, Unité de Résonance Magnétique Nucléaire des Biomolécules, Institut Pasteur, UMR 3528, CNRS, Paris, France.
Sebastian Charbonnierquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.
Gilles Travéquipe labellisée Ligue 2015, UMR 7242, CNRS-Université de Strasbourg, École Supérieure de Biotechnologie de Strasbourg, Illkirch, France.

Funding

Papillomavirus E6 Structural ConsortiumR01CA134737 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2010 to 2019
$4.2M
NCI NIH HHS R01 CA134737NCI NIH HHS R01CA134737
6 · The paper itself

Abstract

Many protein interactions are mediated by small linear motifs interacting specifically with defined families of globular domains. Quantifying the specificity of a motif requires measuring and comparing its binding affinities to all its putative target domains. To this end, we developed the high-throughput holdup assay, a chromatographic approach that can measure up to 1,000 domain-motif equilibrium binding affinities per day. After benchmarking the approach on 210 PDZ-peptide pairs with known affinities, we determined the affinities of two viral PDZ-binding motifs derived from human papillomavirus E6 oncoproteins for 209 PDZ domains covering 79% of the human 'PDZome'. We obtained sharply sequence-dependent binding profiles that quantitatively describe the PDZome recognition specificity of each motif. This approach, applicable to many categories of domain-ligand interactions, has wide potential for quantifying the specificities of interactomes.

Indexed as

High-Throughput Screening AssaysPDZ DomainsAmino Acid MotifsChromatographyDNA-Binding ProteinsHumansKineticsLigandsOncogene Proteins, ViralProtein ConformationProtein Interaction MappingProteinsProteomeRepressor ProteinsSystems BiologyDNA-Binding ProteinsE6 protein, Human papillomavirus type 16E6 protein, Human papillomavirus type 18LigandsOncogene Proteins, ViralProteinsProteomeRepressor Proteins

Identifiers

PMID26053890
PMCPMC4521981

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.