Consortium formed by Harvard Medical School, Dana-Farber Cancer Institute, Boston Children’s Hospital, & Massachusetts General Hospital. @harvardmed 🟦☁️ @HC2EM
Check our new preprint! We uncover the full molecular mechanism of rotavirus membrane penetration and cytosolic escape using cryo-ET, live-cell imaging, and single-molecule assays. (1/3)
🔗 https://t.co/WzTyzMVGWM
Excited to share our latest work led by our postdoc Dan Zhao! We uncovered how the bifunctional complex of Mnl1 mannosidase and protein disulfide isomerase (Pdi1) initiates ERAD. A long-sought ERAD reductase is finally discovered! https://t.co/0HaCgvHRVL
Huge congratulations!
Excited about mechanistic biology and processes in the cell's nucleus? Join our lab as a post-doctoral researcher! We have a state-of-the-art cryo-EM facility at HMS, a brand-new lab space, and a vibrant community at HMS! DM/email me or check https://t.co/CydU5ziAK6
Excited to share our @biorxivpreprint led by @xiaoyi_fann and @wanyuviridae exploring how binding of western equine encephalitis virus (WEEV) to its cellular receptors evolved over the past century 🤩 https://t.co/i1OzCGWkpr @HarvardMicro
1/n) Best way to start 2025! Thrilled to share our Nature paper about the structures of axonemal components from sperm flagella and from epithelial cilia of the oviduct and brain ventricles. Great collaboration with
@TzviyaZBM and @alanbrownhms
https://t.co/RvmQd3PfYz
Ever wondered how transcription choreographs histone modifications? Our work reveals the basis of co-transcriptional H3K36me3 by SETD2. We visualize how a histone writer coordinates with the transcription machinery! This is the magnus opus of @MarkertJon https://t.co/g27t5Rw5RY
A nice piece on one our @CellCellPress papers published earlier this year about mechanisms of herpes simplex virus polymerase drug resistance related to conformational dynamics. 🕺
https://t.co/gNJMBrfMdr
Excited to share our most recent paper at @CellCellPress in which we used #CryoEM to study conformational dynamics as a determinant of drug selectivity and resistance for the herpes simplex virus DNA polymerase. https://t.co/Zi7N7Ul4q7
We are excited to share our @NatureComms paper by postdoc Pan @an32169364 and @VirologyHarvard grad student Wanyu @wanyuviridae on the structural binding mode of eastern equine encephalitis virus (EEEV) and Semliki forest virus (SFV) with receptor VLDLR
https://t.co/tNBC7Gao7z
A new paper from Benjamin Ebert, Nathanael Gray, @eric_fischer, @fischerlab1, @LiYender, Michelle Ma, and @M_MurtazaHassan reports a trans-labeling mechanism “template-assisted covalent modification”, which enables proximity-driven pharmacology https://t.co/VvAJdpgDIf
STK19 is a bona fide transcription-coupled repair factor. Check out the preprint with @FrogWalterLab ➡️https://t.co/z5muiBdZVt
We achieved a major technical milestone: 1.9 Å resolution structure of an RNA polymerase II transcription complex. Txn goes sub-2 Å!
Excited to share our story on polymerization in ZBTB transcription factors, which was published in the July 11 issue of @MolecularCell! https://t.co/qlzxfF0PR4 1/n
Excited to share @biorxivpreprint in collaboration with Rachel Fearns at BU in which we determined the cryo-EM structure of the Nipah virus polymerase complex! The complex assembles with a tobacco pipe-like shape with a flexible stem (do you see it?)😃😅https://t.co/9LWOaxMXND
The 20S proteasome plays a key protease role in many regulatory processes. Yet, how its ordered biogenesis and temporally timed catalytic site activation works has remained elusive. In our latest work, we provide evidence for how that occurs! @NatureSMB https://t.co/CpJUUkUsvU