iiinova — where your digital self keeps evolving

Eugene Serebryany @eserebry.bsky.social · 05/07/2026

Congratulations, Amir!! Wishing you great reviews and great ways to follow it up, too!

Eugene Serebryany @eserebry.bsky.social · 26/06/2026

Are you on the faculty job market? Interested in coming to work here at Stony Brook? (You should be!) Physiology & Biophysics (my home department) is looking to add faculty at the Asst/Assoc Prof level: apply.interfolio.com/148377

apply.interfolio.com

Apply - Interfolio {{$ctrl.$state.data.pageTitle}} - Apply - Interfolio

023

Eugene Serebryany @eserebry.bsky.social · 15/06/2026

Delighted to share our newly In-Press paper reporting evidence of a tantalizing intramolecular misfolding event in disulfide-bridged dimers of lens gamma-D crystallin. It is revealed by mutating the N-terminal Cys residues. www.jbc.org/article/S002...

010

Eugene Serebryany @eserebry.bsky.social · 09/01/2026

Thank you so much for pointing out that paper!! Fascinating how/why this mistranslation occurs. Our WT had only one peak by intact ESI-MS, though, and it had the expected WT mass (Figure S1). I'm so glad we checked that--and, of course, grateful to Liz for the construct!

010

Eugene Serebryany @eserebry.bsky.social · 09/01/2026

Proud to share our newest preprint. We introduced conformational constraints (disulfides) into alpha-synclein and measured effects on aggregation. There were surprises, including a possible new amyloid polymorph and a substoichiometric chaperone-like aggregation inhibitor. doi.org/10.64898/202...

doi.org

Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synuclein

Intrinsically disordered proteins can aggregate in many distinct conformations (polymorphs). Polymorphs are a striking example of fold-switching: one primary structure able to form distinct tertiary s...

151

Eugene Serebryany @eserebry.bsky.social · 30/12/2025

Proud to share a new manuscript from my group: www.biorxiv.org/content/10.6... We found an unexpected intramolecular conformational rearrangement that triggers aggregation of a lens crystallin. This could be a weak link that leads to age-onset cataract, and hence a potential target for preventing it

biorxiv.org

| bioRxiv

bioRxiv - the preprint server for biology, operated by Cold Spring Harbor Laboratory, a research and educational institution

000

Eugene Serebryany @eserebry.bsky.social · 25/09/2025

I particularly like the 8-fingered amphibian...

020

Eugene Serebryany @eserebry.bsky.social · 17/09/2025

The Laufer Center for Physical & Quantitative Biology is recruiting for an endowed professorship! It is a great community to be part of. Asst. or Assoc., or even Full Prof. candidates are welcome! apply.interfolio.com/173357

apply.interfolio.com

Apply - Interfolio {{$ctrl.$state.data.pageTitle}} - Apply - Interfolio

000

Eugene Serebryany @eserebry.bsky.social · 15/09/2025

Proud to share the first paper fully from the Serebryany Lab, now officially In Press! Here we report a simple but previously overlooked approach to biomanufacturing seamlessly cyclized peptides. Big congrats to my talented Ph.D. student, Ali Behboodian. authors.elsevier.com/a/1lmU%7E_1l...

authors.elsevier.com

040