L. Carrique

This study characterizes the structural and functional interaction between influenza A virus RNA polymerase and host RNA Polymerase II CTD, identifying key residues and their roles in transcription and replication.

The paper determines the structure of the N-RNA/P triple complex in human metapneumovirus, revealing how the polymerase attaches to the RNA template and providing a basis for therapeutic design.

This study characterizes the structure of the full-length Hantaan virus polymerase using cryo-EM, revealing conformational states relevant to replication and transcription.

LipIDens uses MD simulations to interpret lipid-like densities in cryo-EM maps of membrane proteins, revealing protein-lipid interactions.

The paper presents the cryo-EM structure of HHAT, revealing its mechanism for transferring palmitate to SHH and identifying a heme group essential for its function.

This paper identifies CR3022 as a monoclonal antibody that neutralizes SARS-CoV-2 by destroying its prefusion Spike conformation, suggesting therapeutic potential.

The paper identifies a lipid-binding pocket in the SARS-CoV-2 Spike that stabilizes the prefusion trimer and shields neutralizing epitopes, suggesting it as a potential drug target.

This paper identifies an antibody, EY6A, from a convalescent patient that neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1 by binding a conserved epitope on the Spike protein.

This study presents high-resolution cryo-EM structures of immature and mature flaviviruses, revealing structural changes during maturation and the role of pH in conformational rearrangements.

This study identifies parallel mutations in avian influenza viruses associated with high pathogenicity using phylogenetic and statistical methods.