Sign in

Shady Saad

@shadys11.bsky.social
94 followers 109 following 6 posts

HFSP Postdoc in the Wysocka and Jarosz labs @Stanford. Aiming to understand physiological protein assemblies. Alum of ETH Zürich.

PostsRepliesMedia
Reposted by Shady Saad
Raquel Fueyo @fueyoraquel.bsky.social · 01/10/2025
Today in @nature.com, we present our work leveraging functional genomics and human blastoids to uncover a human-specific mechanism in preimplantation development driven by the endogenous retrovirus HERVK. Special thanks to the reviewers whose comments improved our manuscript a lot! rdcu.be/eI3tD
rdcu.be
A human-specific regulatory mechanism revealed in a pre-implantation model
Nature - Genetic manipulation of blastoids reveals the role of recently emerged transposable elements and genes in human development.
1114051
Shady Saad @shadys11.bsky.social · 17/09/2025
I’m very excited to share that Stanford Medicine has highlighted my work med.stanford.edu/news/insight...
med.stanford.edu
Behind the Science: How a ‘speech gene’ could help treat Huntington’s
Stanford Medicine researchers found cells that keep a speech-linked protein called FOXP2 from clumping; its tricks could break apart clumps of proteins that cause devastating brain diseases.
080
Reposted by Shady Saad
Ryan Flynn @raflynn5.bsky.social · 23/04/2025
Excited to share Benson’s and Maria’s work in collab w/Kostas Tzelepis: we found the nucleolar protein NPM1 is a marker of AML and can be targeted therapeutically connecting ‘cell surface RNA biology’ to cancer biology @natbiotech.nature.com www.nature.com/articles/s41...
36522
Reposted by Shady Saad
Cedric Boeckx @cedricboeckx.bsky.social · 22/04/2025
What did the two amino acid substitutions in #FOXP2 that occurred uniquely in the human lineage do? 🧪🧬 🧠 Fascinating new @cp-cell.bsky.social study by @shadys11.bsky.social D. Jarosz & J. Wysocka, uncovering a molecular function for these 2 substitutions in promoting the solubility of FOXP2. (1/n)
cell.com
DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation
DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...
22612
Reposted by Shady Saad
Simon Fisher @profsimonfisher.bsky.social · 22/04/2025
When we first isolated FOXP2 & implicated it in speech disorder, a notable feature was its big stretch of consecutive glutamine (Q) residues, the longest polyQ tract in a native protein. @shadys11.bsky.social et al here use it as a model to reveal how polyQ proteins avoid forming toxic assemblies.🙌🧪
cell.com
DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation
DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...
3228
Shady Saad @shadys11.bsky.social · 21/04/2025
I am incredibly proud to share that my work has officially been published in Cell! @cp-cell.bsky.social This work was a product of years of dedication and countless hours of research in the labs of Joanna Wysocka and Dan Jarosz labs @stanfordmedicine.bsky.social www.cell.com/cell/fulltex...
cell.com
DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation
DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-p...
310424
Reposted by Shady Saad
Cell - a Cell Press journal @cp-cell.bsky.social · 16/04/2025
Now online! DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation
dlvr.it
DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation
DNA binding and phosphorylation protect FOXP2, a transcription factor with the longest polyQ track in the proteome, from aggregation during interphase and mitosis. Harnessing these native solubility-promoting mechanisms utilized by FOXP2 diminishes aggregation and amyloid formation by the pathological form of Huntingtin polyQ.
032