Lotta Happonen

The paper introduces mE-DIA, a multi-enzyme DIA-MS workflow that improves proteoform detection in proteomics by integrating analysis and interpretation into a single toolset.

This study identifies a ribosome-centered mechanism of resistance to antibacterial PNAs in E. coli, showing that mutations in ribosomal protein uS12 alter 30S assembly and translation-initiation dynamics, reducing PNA efficacy.

The paper maps the structural epitope landscape of pneumolysin and identifies a conserved cross-species neutralising site among cholesterol-dependent cytolysins.

This study identifies SpnA's role in inhibiting the complement system by interacting with C5b67, preventing membrane attack complex assembly.

This paper designs an epitope-centric nanoparticle vaccine against Streptococcus pyogenes using structural mass spectrometry and deep learning to enhance immunogenicity.

This study identifies CDNF's mechanism of action by showing it rescues human dopamine neurons through direct binding to UPR sensors PERK and IRE1α.

This study shows that streptolysin O enhances plasminogen to plasmin conversion by interacting with plasminogen and altering its conformation to increase sensitivity to proteolytic processing.

This study uses multi-modal mass spectrometry to identify a conserved protective epitope in Streptolysin O from S. pyogenes, which could inform vaccine and therapeutic development.

This study shows that increasing Fc flexibility in an IgG1-IgG3 hybrid monoclonal antibody enhances opsonic function and protection against group A streptococci.

This study develops multienzyme deep learning models for de novo peptide sequencing from mass spectrometry data, showing improved generalizability and sequence coverage across diverse protease digests and species.

This study determines the structural interactions between Streptococcus pyogenes M1 protein and human IgG using integrative structural biology, revealing conserved mechanisms to inhibit phagocytosis.