abrahamlabhms.bsky.social
@abrahamlabhms.bsky.social
We are excited to share our new @CellCellPress paper revealing mechanisms of action of promising drugs against the helicase-primase of herpes simplex virus 1 (HSV-1) 🤩 harvardvirology.bsky.social www.cell.com/cell/fulltex...
December 29, 2025 at 8:34 PM
Reposted
Now online! Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly
Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly
Cryo-EM structures of HSV-1 helicase-primase and replication fork complexes reveal mechanisms of drug inhibition, features that explain drug selectivity, and the molecular basis of replication fork complex assembly during herpesvirus DNA replication.
dlvr.it
December 29, 2025 at 7:52 PM
Reposted
#NewResearch

Cryo-EM structures of the full-length Junin virus and Machupo virus spike glycoprotein complexes stabilized in the prefusion conformation - analyses reveal features that regulate glycoprotein pH-dependent membrane fusion activity.

#MicroSky 🦠

www.nature.com/articles/s41...
Molecular organization of the New World arenavirus spike glycoprotein complex - Nature Microbiology
Cryo-EM structures of the full-length Junin virus and Machupo virus spike glycoprotein complexes stabilized in the prefusion conformation. Analyses reveal features that regulate glycoprotein pH-depend...
www.nature.com
August 11, 2025 at 2:40 PM
Excited to share our new @natmicrobiol.nature.com paper revealing the most complete arenavirus glycoprotein complex (GPC) structures to date 🤩 www.nature.com/articles/s41...
Molecular organization of the New World arenavirus spike glycoprotein complex - Nature Microbiology
Cryo-EM structures of the full-length Junin virus and Machupo virus spike glycoprotein complexes stabilized in the prefusion conformation. Analyses reveal features that regulate glycoprotein pH-depend...
www.nature.com
August 9, 2025 at 9:51 AM
Reposted
Now online! Molecular basis for shifted receptor recognition by an encephalitic arbovirus
Molecular basis for shifted receptor recognition by an encephalitic arbovirus
Cryo-EM structures and mutational analyses reveal western equine encephalitis virus E2-E1 glycoprotein polymorphisms that determine shifted receptor usage and allow for sequence-based prediction of strain compatibility with human receptors.
dlvr.it
April 5, 2025 at 12:42 PM
Also sharing the terrific news piece by Jake Miller at HMS News on our latest paper! @cp-cell.bsky.social
hms.harvard.edu/news/how-sma...
How A Small Number of Mutations Can Fuel Outbreaks of Western Equine Encephalitis Virus
Study shows how spike protein changes determine the risk of viral outbreaks
hms.harvard.edu
April 4, 2025 at 8:05 PM
Our study on the molecular basis of shifts in receptor recognition by western equine encephalitis virus (WEEV) in the past century, led by Xiaoyi Fan and @wanyuviridae.bsky.social , is online! 👏🎉
www.cell.com/cell/fulltex...
Molecular basis for shifted receptor recognition by an encephalitic arbovirus
Cryo-EM structures and mutational analyses reveal western equine encephalitis virus E2-E1 glycoprotein polymorphisms that determine shifted receptor usage and allow for sequence-based prediction of st...
www.cell.com
April 4, 2025 at 7:59 PM
Excited to share our @biorxivpreprint.bsky.social exploring how binding of western equine encephalitis virus (WEEV) to its cellular receptors evolved over the past century 🤩 www.biorxiv.org/content/10.1... @harvardmicro.bsky.social
January 2, 2025 at 10:25 PM