Buwei Huang

The paper shows short RNAs can form complex structures like icosahedrons and filaments, expanding the known RNA quaternary structures and supporting RNA-based self-assembly in an RNA world.

Conditioning RFdiffusion on edge beta-strand pairing yields specific binders to polar targets, with in silico success above 9.2% versus 0.98% for hotspot-only conditioning.

This paper designs antibodies de novo with atomic precision using RFdiffusion and yeast display, validated by cryo-EM and biophysical methods.

The paper designs high-affinity miniprotein binders targeting Flpp3, a virulence factor of Francisella tularensis, using physics-based and deep-learning methods, achieving sub-nanomolar affinities.

This paper introduces computational methods to design pH-sensitive binders that dissociate under acidic conditions, demonstrating their application in targeting various receptors and proteins.

The paper introduces a multispectral imaging approach for live-cell imaging, enabling accurate unmixing of low signal-to-noise ratio data at video rates.

The paper designs de novo proteins called NeoNectins that specifically bind integrin α5β1, enhancing cell attachment and tissue integration in biomaterials.

The paper designs TrkA agonists that activate neuronal differentiation and neurite outgrowth without triggering pain-related gene expression.

This study uses target-conditioned diffusion to design high-affinity TNFR superfamily antagonists and agonists with switchable specificity.

This paper introduces SNIPR, a synthetic receptor that responds to soluble ligands, enabling targeted CAR T-cell therapy and synthetic cell signaling.

This paper designs high-affinity proteins that bind to convex protein sites using geometrically matching concave scaffolds, achieving low nanomolar to picomolar affinities.

The paper designs EndoTags to trigger endocytosis and degradation of target proteins, enabling tissue-specific targeting and therapeutic applications.

This paper designs small, stable proteins that bind to diverse target proteins using only structural information, achieving nanomolar to picomolar affinities.