Joshua A. Kritzer

This paper designs and evolves an orthogonal HaloTag variant (OrthoTag) that enables multiplexed labeling in cells with high specificity and orthogonality to the original HaloTag.

BoltzMol-1 identifies chemically tractable binders for diverse targets with limited experimental resources using model-driven ranking and physicochemical filtering.

This paper develops N-methylated and stapled peptide ligands for GABARAP with low nanomolar affinity and subfamily selectivity.

This paper introduces RFpeptides, a deep learning framework for designing high-affinity macrocyclic peptides, achieving sub-nanomolar binding affinities and accurate structural predictions.

The paper investigates the binding affinity of GW5074 to LC3B and GABARAP using an AlphaScreen assay, finding micromolar inhibitory potencies and suggesting potential for targeted protein degradation.

This paper shows that activating GABA(A) receptors in lung cancer cells triggers autophagy via GABARAP-Nix interaction, enhancing radiation sensitivity and reducing toxicity in preclinical models.

The paper compares cell penetration of biotherapeutics across human cell lines using a novel assay and identifies factors influencing penetration differences.

The paper develops BenzoHTag, a modified HaloTag variant optimized for faster and more efficient labeling with a fluorogenic dye, improving live-cell assays.