Attended the DCHSB (Duke Center for HIV Structural Biology) 2026 meeting at Duke.
Great discussions on HIV-1 structural biology and Env dynamics.Grateful to Dr. Priyamvada Acharya for organizing.
#DCHSB2026#HIVResearch
BREAKING NEWS
The 2025 #NobelPrize in Physiology or Medicine has been awarded to Mary E. Brunkow, Fred Ramsdell and Shimon Sakaguchi “for their discoveries concerning peripheral immune tolerance.”
When someone says that your biological genome was created by #AI, and that's why your functional role is so advanced. It's quite fascinating, though, but not in this AI era.
https://t.co/IxnuGcR50m
doi: https://t.co/s5YGAthsey
Exciting to see our protein binder design pipeline BindCraft published in its final form in @Nature ! This has been an amazing collaborative effort with Lennart, @csche11h, @sokrypton, @befcorreia and many other amazing lab members and collaborators.
https://t.co/PTMoqQqwcU
The most radically recoded genome yet!
Syn57 is E Coli with only 57 codons, freeing space to encode up to 4 non-canonical amino acids. That, combined with its virus resistance, will make it an incredible tool for biomanufacturing.
From the Chin Lab in @ScienceMagazine
A new study from Dr. Sarika’s Lab at @NImmunology reports that ARL6IP5 induces reticulophagy to reduce ER stress as well as unfolded & misfolded proteins.
A potential therapeutic approach for combating prion disease!
📰in #Autophagy@tandfonline
Read here🔗https://t.co/u6WRZgjCX7
The ARL6IP protein is a transmembrane (TM) protein with four TM domains and two soluble domains (N-terminal or C-terminal). The structure of ARL6IP is quite complex due to the high mobility in local region domains. It seems that it would be playing interchangeable forms from
maintain ER quality and function. This protein is also highly dynamic in nature in the ER. Interestingly, this study revealed that it interacts with one of the CALCOCO1 domains (a soluble reticulophagy receptor) and helps guide unfolded and misfolded (prion-like) proteins to be