Author

P. Juyoux

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

J. von Velsen· 3 shared E. Pellegrini· 2 shared M. W. Bowler· 2 shared A. Naschberger· 1 shared B. Rupp· 1 shared D. Gobbo· 1 shared F. L. Gervasio· 1 shared I. Galdadas· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

J. von Velsen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The MAP2Ks can use ADP to phosphorylate and activate their substrate MAPKs in vitro

P. Juyoux, J. von Velsen, E. Pellegrini, M. W. Bowler

The paper shows that MAP2Ks can phosphorylate and activate MAPKs using ADP in vitro, suggesting a potential role in maintaining signaling under ATP-depleted conditions.

bioRxiv · Feb 22, 2024Biochemistry

Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation

P. Juyoux, I. Galdadas, D. Gobbo, J. von Velsen, M. Pelosse, M. Tully, O. Vadas, F. L. Gervasio, E. Pellegrini, M. W. Bowler

The paper determines the structure and activation mechanism of the MKK6-p38α complex using cryo-EM and MD simulations, revealing how phosphorylation and interactions drive MAPK specificity.

bioRxiv · Jul 4, 2022Biophysics

Controlled dehydration, structural flexibility, and Gadolinium MRI contrast compound binding in human plasma glycoprotein afamin

A. Naschberger, P. Juyoux, J. von Velsen, B. Rupp, M. Bowler

This paper shows that controlled dehydration of afamin crystals stabilizes a new orthorhombic form, revealing conformational flexibility and Gadoteridol binding sites, while highlighting issues with using single crystal structures for modeling.

bioRxiv · Jun 18, 2019Biochemistry