Publication Spotlight
AlphaFold 3 can accurately model glycans with proper stereochemistry only when using the BAP+CCD syntax, but manually creating these inputs is tedious and error-prone. To streamline the process, JAAG—a lightweight, user-friendly web tool—automates the conversion of glycans drawn by users into BAP+CCD syntax. This makes it easier for scientists to model glycoproteins and glycan–protein interactions, helping even AlphaFold 3 beginners generate reliable, stereochemically valid structures effortlessly.
WIN332 binds to precursors of canonical human N332-glycan-dependent (Type-I) V3-glycan bNAbs but also of a first-of-its-class N332-glycan-independent (Type-II) V3-glycan bNAb. WIN332 elicits N332-glycan-independent antibodies with remarkable sequence and binding similarities with the most potent human type-I and type-II V3-glycan bNAbs. Thus, WIN332 is a promising vaccine candidate to streamline V3-glycan bNAb elicitation.
List of All BioF:GREAT Publications
Publication List
JAAG: a JSON input file Assembler for AlphaFold 3 with Glycan integration
Modeling glycans with AlphaFold 3: capabilities, caveats, and limitations
Rapid elicitation of a new class of neutralizing N332-glycan independent V3-glycan antibodies against HIV-1 in nonhuman primates
Comprehensive evaluation of cleavable bioorthogonal probes for site-specific O-GlcNAc proteomics
https://www.mcponline.org/article/S1535-9476(25)00163-X/fulltext
A vascular-associated fibroblastic cell controls pancreatic islet immunity
An updated sulfate transporter phylogeny uncovers a perennial-specific subgroup associated with lignification.
Novel HIV-1 fusion peptide immunogens using glycan-engineered alphavirus-like particles
https://www.nature.com/articles/s41541-025-01288-6
TBR is an RG-I rhamnose O-acetyltransferase required for epidermal cell adhesion in Arabidopsis thaliana
Deciphering the unique autoregulatory mechanisms and substrate specificity of the understudied DCLK3 kinase linked to neurodegenerative diseases
Human Proteoglycan Linkage Region Glycosyltransferases are Dimeric and Show Unexpected Specificities
https://onlinelibrary.wiley.com/doi/10.1002/anie.202516855
