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Williams Lab
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Williams Lab
@WilliamsLabNEU
Single Molecule Biophysics Lab @Northeastern
Boston, MA 加入时间 Şubat 2017
255 关注334 粉丝
How does the ORF1p perform its multiple functions to facilitate LINE1 retrotransposition? And what enables its ability to also facilitate replication of other retrotransposons? Find out in our newly published paper in @NAR_Open doi.org/10.1093/nar/gk…
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Williams Lab 已转推
🚨 New PhD Program Alert! 🚨
Explore the intersection of physics, biology, and chemistry w/ Northeastern’s Biophysics PhD program. Flexible curriculum, cutting-edge research - shape your path in science
🗓 Priority Deadline: Jan 15
🔗 Apply now: cos.northeastern.edu/biophysics-phd/
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In @VirusesMDPI, our single molecule measurements of basic residue mutants reveal that HIV-1 NC condenses dsDNA via a primarily electrostatic mechanism, which is needed to maintain viral core stability during reverse transcription. doi.org/10.3390/v16060…
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Williams Lab 已转推
New research on #HIV infection — spearheaded by a professor at @Northeastern — could lead to better drugs to treat the virus.
Read more: bit.ly/4bi9Ghw
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Williams Lab 已转推
QAM
Our new @ScienceAdvances paper with the Pathak lab at NCI is described in a story on @NUGlobalNews news.northeastern.edu/2024/04/29/hiv…
Williams Lab@WilliamsLabNEU
What triggers HIV-1 capsid uncoating? In @ScienceAdvances, with the Pathak lab at NCI, we show long dsDNA from reverse transcription is required for uncoating, likely due to mechanical pressure regulated by the nucleocapsid protein. science.org/doi/10.1126/sc…
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What triggers HIV-1 capsid uncoating? In @ScienceAdvances, with the Pathak lab at NCI, we show long dsDNA from reverse transcription is required for uncoating, likely due to mechanical pressure regulated by the nucleocapsid protein. science.org/doi/10.1126/sc…
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The T4 gp32 CTD recruits and stabilizes proteins within the model T4 replication complex. Does it serve other roles? Our new @JMolBiol paper shows that the CTD facilitates rapid removal of gp32 from ssDNA to ensure prompt genomic processing. doi.org/10.1016/j.jmb.…
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Williams Lab 已转推
A cause for celebration. The grand opening ceremony of EXP brought dignitaries, university leaders, and community members together.
Read more: bit.ly/3Sq35LR
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Can the sequence nonspecific single-stranded DNA binding protein E. coli SSB detect DNA damage? @WilliamsLabNEU and @BeuningLabNEU collaborated to show in @BiophysJ that the SSB binding conformation changes in response to DNA damage. doi.org/10.1016/j.bpj.…
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How are T4 gene 32 (gp32) proteins rapidly removed from a stable filament during DNA replication? Our new @NAR_Open paper shows how gp32 can wind ssDNA in multiple conformations to facilitate rapid protein dissociation. doi.org/10.1093/nar/gk… #opticaltweezers #singlemolecule
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V. Adrian Parsegian, who made fundamental contributions to soft condensed matter, biological materials science and biophysics, passed away today.
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@rpodgornik Very sad news. Adrian was a great scientist and colleague.
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Williams Lab 已转推
Jason starts his summer research at Northeastern. Good Luck Jason for a productive summer. Thank you @WilliamsLabNEU for the opportunity.
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We are pleased to announce that the registration for the ‘12th International Retrovirology Symposium: Assembly, Maturation and Uncoating’ is now open!
ramm2023.utah.edu
The conference will be held at Snowbird Utah from Sept 6th to 9th, 2023.
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Part of a great collaboration with the laboratories of @LugerLab, Jim Maher, and Georges Mer!
Williams Lab@WilliamsLabNEU
Like other HMGB proteins, human FACT destabilizes nucleosomes to facilitate transcription. Why is the rest of this large protein needed? doi.org/10.1016/j.celr… shows that the SSRP1 HMGB domain coordinates with the SPT16 domain to facilitate nucleosome reassembly after disruption
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Like other HMGB proteins, human FACT destabilizes nucleosomes to facilitate transcription. Why is the rest of this large protein needed? doi.org/10.1016/j.celr… shows that the SSRP1 HMGB domain coordinates with the SPT16 domain to facilitate nucleosome reassembly after disruption
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The N protein of SARS-CoV-2, the virus responsible for COVID-19, is essential for viral replication, making it an attractive drug target. The N protein contains two primary structural domains. How do they coordinate to compact the viral genome? Find out in doi.org/10.1093/nar/gk…
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