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Guillaume Mas

@masgu.bsky.social
104 followers 130 following 14 posts

Research associate @hillerlab.bsky.social #NMR #chaperone #structuralbiology #hsp70

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Guillaume Mas @masgu.bsky.social · 21/09/2026
New in @CommsBio: We discovered a tyrosine motif that creates a switch for J-domain proteins. Phosphorylation of this motif disrupts the fold, causing degradation or loss of Hsp70 activation. Congrats Raju, @annaleder.bsky.social , @chercheurjuteux.com & all coauthors www.nature.com/articles/s42...
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Guillaume Mas @masgu.bsky.social · 20/11/2025
Hey Mathieu, c‘est jamais fun mais on est déjà entrain de préparer la soumission pour un autre journal. Ça va marcher d’une manière ou d’une autre :)
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Guillaume Mas @masgu.bsky.social · 11/08/2025
I have also developed novel algorithms, using opencv, for the quantification of condensates properties in microscropy pictures. Check my github for more information! github.com/mas-gu/llps_...
github.com
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Guillaume Mas @masgu.bsky.social · 11/08/2025
I have created the video showcasing the PDIA6 condensate dynamics and function using Blender and the Molecular Nodes module! Visualizing science like never before. #Blender #MolecularNodes @bradyajohnston.bsky.social
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Guillaume Mas @masgu.bsky.social · 11/08/2025
Our results show PDIA6 condensates recruit key chaperones (BiP, ERdj3, Grp94) to enhance proinsulin folding & prevent misfolding, driven by Ca²⁺. This opens new perspectives for tackling protein misfolding diseases like diabetes! @natcellbio.nature.com
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Guillaume Mas @masgu.bsky.social · 11/08/2025
Thrilled to share my first corresponding author paper as a project leader in @hillerlab.bsky.social ‪ Amazing work from first author @annaleder.bsky.social We discovered multi-chaperone condensates in the ER that revolutionise the current vision of protein folding! www.nature.com/articles/s41...
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Guillaume Mas @masgu.bsky.social · 30/07/2025
Shreyan Datta has demonstrated exceptional performance in our lab. I highly recommend him to anyone seeking an outstanding PhD candidate!
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Guillaume Mas @masgu.bsky.social · 12/06/2025
Great work from @annaleder.bsky.social in my chaperone sub-group at the Hiller Lab!
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Reposted by Guillaume Mas
Magnetic Resonance News @nmr900.bsky.social · 05/06/2025
Two postdoctoral positions in the group of Dr. Malene R. Jensen at the Institute for Structural Biology in Grenoble, France, protein kinase (MAPK) cell signaling pathways (incl NMR, X-ray crystallography and cryo-electron microscopy) www.jensen-nmr.fr #NMRjobs #NMRchat #NMR 🧲
jensen-nmr.fr
> Malene R. Jensen @ IBS Grenoble
Research team of CNRS research director Malene Ringkjøbing Jensen at the Institut de Biologie Structurale, Grenoble, France
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Guillaume Mas @masgu.bsky.social · 05/06/2025
Merci Mathieu!
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Guillaume Mas @masgu.bsky.social · 03/06/2025
Thanks, glad you like it!
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Guillaume Mas @masgu.bsky.social · 02/06/2025
It’s fully adaptable to study other nucleotide-driven machines, dissecting functional cycles, regulation, and cofactor effects with unprecedented resolution. #MolecularMachine
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Guillaume Mas @masgu.bsky.social · 02/06/2025
Applied to the Hsp70 BiP NBD, in-cyclo NMR reveals all 11 microscopic kinetic rates of ATP binding, hydrolysis & product release — showing ADP·Pi release, not ATP hydrolysis, is the rate-limiting step controlling the cycle duration.
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Guillaume Mas @masgu.bsky.social · 02/06/2025
Thrilled to share our new method in-cyclo NMR that lets us watch molecular machines in action — decoding molecular machine kinetics with atomic precision and exceptional time resolution in one go! 🚀 Check it out: doi.org/10.1038/s414... #NMR #StructuralBiology
doi.org
Mechanism of ATP hydrolysis in the Hsp70 BiP nucleotide-binding domain - Nature Communications
Mas et al introduce in-cyclo NMR to quantify all states and kinetic steps of Hsp70 chaperones ATPase cycle. In-cyclo NMR will enable studies of other molecular machines at an unprecedented level of de...
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Guillaume Mas @masgu.bsky.social · 06/04/2025
Great to be back at the @enc-conference.org #ENCISMAR2025 . Enjoying the conference and the beautiful wildlife.
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