In human cells, large multi-protein transcription co-activators, such as chromatin remodelers or histone acetyltransferases, play critical roles in gene-expression regulation and are often implicated ...

Je m'appelle Eléonore PATTERY, j’ai 23 ans, et je suis actuellement en Master QSE et RSE (Qualité, Sécurité, Environnement / Responsabilité Sociétale des Entreprises). En tant que future professionne...

Postdoctoral Scientist Starting Salary: £41,344 Fixed term: 3 years MRC Laboratory of Molecular Biology, Cambridge, UK We are looking for a postdoc...

On 25 June, Karolinska Institutet will be starting a major recruitment drive for 20 junior researchers with a focus on excellence and mobility. As one of Europe’s leading medical universities, KI offe...

The accurate description and subsequent modeling of protein interactomes require quantification of their affinities at the proteome-wide scale. Here we develop and validate the Holdup Multiplex, a versatile assay with a mass spectrometry (MS) readout for profiling the affinities of a protein for large pools of peptides. The method can precisely quantify, in one single run, thousands of affinity constants over several orders of magnitude. The throughput, dynamic range, and sensitivity can be pushed to the performance limit of the MS readout. We applied the Holdup Multiplex to quantify in a few sample runs the affinities of the 14–3–3s, phosphoreader proteins highly abundant in humans, for 1000 different phosphopeptides. The seven human 14–3–3 isoforms were found to display similar specificities but staggered affinities, with 14–3–3γ being always the best binder and 14–3–3ε and σ being the weakest. Hundreds of new 14–3–3 binding sites were identified. We also identified dozens of 14–3–3 binding sites, some intervening in key signaling pathways, that were either stabilized or destabilized by the phytotoxin Fusicoccin-A. The results were corroborated by X-ray crystallography. Finally, we demonstrated the transferability of the Holdup Multiplex by quantifying the interactions of a PDZ domain for 5400 PBM peptides at once. The approach is applicable to any category of protein-binding ligands that can be quantifiable by mass spectrometry.

Le ministre de la recherche a dit sa « préoccupation », mercredi, après cette décision des autorités américaines. Le chercheur du CNRS aurait subi un contrôle aléatoire à son arrivée, avant que son or...

Ivy League college told to ban masks, expel or suspend students who promote Jew-hate, and put a department under ‘academic receivership’ for five years.

As part of the French Strategy in Artificial Intelligence (AI), the Choose France - CNRS AI Rising Talents program offers exceptionally tal

What is a 3D structure? Some applications The foundations and origins of structural biology Knowing and preparing your sample Choising a structural biology method Expérimental methods : NMR 1 Choose y...