Shady Saad
shadys11.bsky.social
Shady Saad
@shadys11.bsky.social
HFSP Postdoc in the Wysocka and Jarosz labs @Stanford. Aiming to understand physiological protein assemblies. Alum of ETH Zürich.
Pinned
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...
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...
www.cell.com
Reposted by Shady Saad
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
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.
rdcu.be
October 1, 2025 at 6:08 PM
Reposted by Shady Saad
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...
April 23, 2025 at 11:44 AM
Reposted by Shady Saad
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)
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...
www.cell.com
April 22, 2025 at 6:44 AM
Reposted by Shady Saad
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.🙌🧪
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...
www.cell.com
April 22, 2025 at 1:06 PM
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...
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...
www.cell.com
April 21, 2025 at 12:01 PM
Reposted by Shady Saad