M. Fairhead

The paper identifies fragment binders and mutationally intolerant sites in Zika virus NS2B-NS3 protease to develop resistance-resilient antiviral inhibitors.

The paper solves the crystal structure of Arabidopsis thaliana FatA and identifies fragments that target novel regions, enabling the design of new herbicides with improved potency and novel interaction modes.

The paper introduces Di-Gluebodies, covalently-dimerized nanobodies, to improve cryo-EM structure determination of small proteins by providing rigidity and modularity.

This study produces, purifies, and crystallizes 24C-sterol methyltransferase from Candida albicans to support future crystallographic studies.

The paper identifies chemical fragments targeting the Chikungunya virus nsP3 macrodomain through crystallographic screening, revealing novel binding sites and potential inhibitors.

The paper identifies potent nsp3-mac1 inhibitors but finds they do not translate to antiviral activity in cell culture models.

This study identifies fragments binding to EV-D68 3C protease through crystallography and expands them into lead-like compounds, revealing novel binding modes and structural insights for drug design.

The paper identifies 75 fragments that bind to Coxsackievirus A16 2A protease, including 38 unique compounds in the active site, offering a path for broad-spectrum anti-enteroviral inhibitors.

This study uses high-throughput crystallographic fragment screening to identify 46 fragment binding poses on ZIKV NS3Hel, providing templates for antiviral drug design.

The paper describes a set of Golden Gate vectors for efficient recombinant protein production in E. coli, with high cloning efficiency and useful tags and secretion signals.

This study characterizes SARS-CoV-2 NSP15 endoribonuclease, identifies its allosteric properties, and discovers new allosteric sites for inhibitor development.

The paper engineers nanobody interfaces to improve crystal reliability and diversity, resulting in better diffraction and multiple polymorphs.

The paper identifies fragment hits against SARS-CoV-2 main protease using crystallography and mass spectrometry, revealing structural insights for drug design.

The paper uses a scFv to solve the structure of SP140's PHD-bromodomain and suggests strategies to improve scFvs as crystallization chaperones.

This study develops a method for discovering covalent probes using electrophile fragment screening and identifies selective inhibitors for OTUB2 and NUDT7.