Anthony A. Kossiakoff

The paper identifies and characterizes Inside-Out (I-O) proteins on cancer cell surfaces, showing their dynamic trafficking and link to stress response mechanisms.

This paper develops a conformation-specific antibody, K27-IgG, to detect K27-linked polyubiquitin and identifies DNAJB1 as a reader and UBE2Q1 as a writer for this ubiquitin chain type.

The paper identifies an unconventional HxD motif in coronaviruses that functions as a coatomer-binding signal, revealing alternative pathways for viral morphogenesis.

This study presents the cryo-EM structure of PLCε, revealing its N-terminal domains and their role in membrane engagement and activity.

The paper characterizes HLA-B*73:01, revealing its unique peptide binding motif, restricted peptidome, and distinct interaction with KIR2DL2, suggesting evolutionary advantages in pathogen resistance.

This study determines the structure of the human vault cage with PARP4 and NAD+, revealing binding interfaces and NAD+ pockets, and shows proteomics differences in PARP4-depleted vaults.

This paper introduces a modular CAR-Fab platform that improves cancer immunotherapy by enabling rapid target redirection and reducing antigen loss variant escape.

The paper develops a synthetic antibody fragment that binds to 10 claudin subtypes, opening tight junctions and modulating paracellular permeability.

This study presents cryo-EM structures of AftB from Mycobacterium chubuense, revealing its architecture and mechanism for terminal arabinosylation in mycobacterial cell wall biosynthesis.

This study determines the cryo-EM structures of PimE from Mycobacterium abscessus and elucidates its mechanism of action, providing insights for anti-TB drug development.

This paper introduces engineered protein-G variants and Fab scaffolds to create modular, plug-and-play antibody-based assemblies for versatile cell biology applications.

This study uses cryo-EM and single-molecule FRET to show conformational coupling between the extracellular and transmembrane domains of an aGPCR, revealing how ECR dynamics influence receptor function.

This study presents cryo-EM structures of Clostridium perfringens enterotoxin bound to claudin-4, revealing its pore assembly mechanism and potential therapeutic strategies.

The paper develops a synthetic Fab module (NabFab) that binds nanobodies with high affinity, enabling high-resolution cryo-EM studies of membrane proteins.