James A. Ferguson

The paper characterizes antigenic differences in H15 influenza virus hemagglutinin by analyzing mAb binding and neutralization against ancestral and drifted strains.

This study examines how glycan evolution in H3 hemagglutinin affects antigenicity and immunogenicity, showing reduced antibody binding and shifted immune response.

This study shows that macaques can elicit human-like broadly neutralizing antibodies against influenza HA stem regions, with similar immunogenetic and structural features.

This paper develops a method to discover monoclonal antibodies directly from immune sera using cryoEM and computational tools, significantly speeding up the process and improving accuracy.

This study identifies a conserved DR motif in CDR H3 of antibodies targeting the influenza virus neuraminidase active site, suggesting a common strategy for broad protection.

The paper shows that genetic variation in human immunoglobulin genes affects antibody responses to influenza HA, informing vaccine design to cover diverse populations.

The paper characterizes glycoproteins of novel fish influenza B-like viruses, revealing differences in receptor binding and antigenic conservation compared to influenza B viruses.

The paper identifies anti-immune complex antibodies generated through repeated HIV Env immunizations and presents their structures using polyclonal epitope mapping.

The paper identifies two human monoclonal antibodies that broadly inhibit PfEMP1's binding to EPCR, a key process in severe malaria pathogenesis.

This study evaluates AF2's ability to predict protein structural ensembles by comparing its results with MD simulations and NMR data for four test proteins.

This study identifies neutralizing antibody epitopes against Lassa virus GPC using electron microscopy, revealing challenges in vaccine-induced responses and opportunities for improved vaccine design.

This paper investigates how mispacking of the F87 sidechain in transthyretin tetramers affects conformational dynamics and aggregation propensity through structural and biophysical analyses.

This study uses NMR relaxation dispersion to characterize the structural dynamics of an amyloidogenic intermediate of transthyretin, revealing conformational fluctuations that promote amyloid formation.