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Anna Arutyunyan

@immunobananna.bsky.social
125 followers 370 following 16 posts

Postdoc in Lehner lab @sangerinstitute | PhD @sangerinstitute @Cambridge_Uni | BSc @miptru 🇷🇺🇦🇲 Genomics | Synthetic Biology | Immunology | Reproduction

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Reposted by Anna Arutyunyan
Max Stammnitz @maxstammnitz.bsky.social · 02/06/2025
1 plant hormone receptor ☘️ 3,500 mutants, to single-site saturation 🧬 >45,000 binding and abundance measurements 📶 Very happy to present our latest work – where deep mutational scanning meets the world of small molecules.

 www.biorxiv.org/content/10.1...

 With @benlehner.bsky.social [1/7]
biorxiv.org
The genetic architecture of an allosteric hormone receptor
Many proteins function as switches, detecting chemicals and transducing their concentrations into cellular responses. Receptor switches are key to the integration of environmental signals, yet it is n...
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Reposted by Anna Arutyunyan
Taylor Mighell @taylor-mighell.bsky.social · 01/06/2025
GPCR-MAPS is now live! www.biorxiv.org/content/10.1... A new platform for high resolution functional mapping of GPCRs with massive mutagenesis. We identify the core activation network, residues involved in biased signaling, and generate >7,000 full dose response curves. With @benlehner.bsky.social
biorxiv.org
The genetic architecture of G-protein coupled receptor signaling
G-protein coupled receptors (GPCRs) are the most abundant class of human receptors and drug targets. The vast majority of GPCR drugs bind the conserved orthosteric pocket, which can lead to non-specif...
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Anna Arutyunyan @immunobananna.bsky.social · 12/06/2025
Alzheimer’s disease 🧠starts with a molecular domino effect - but what triggers the first piece to fall? In our new study we cracked open the black box of early protein aggregation, and the findings could reshape how we fight neurodegeneration. 🧵👇 www.science.org/doi/10.1126/...
science.org
Massively parallel genetic perturbation suggests the energetic structure of an amyloid-β transition state
The aggregation rates of >140,000 mutants reveal the energetic structure of an amyloid-β nucleation reaction transition state.
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