David A. Agard

This study shows that IRE1α assembly into filaments is dynamically regulated by unfolded proteins and BiP through opposing mechanisms.

This study identifies a tripartite mechanism involving Imp7 and Imp1 that licenses RNA polymerase import into the phage nucleus, showing that nuclear compartment assembly precedes transcriptional and replicative programs.

This study reveals how HSF1 is regulated by Hsp70 and Hsp90 chaperones through structural and mechanistic analyses, showing Hsp90's role in maintaining HSF1 in a pre-activated state.

The paper describes a Kaggle challenge for particle picking in cryo-electron tomography, resulting in improved algorithms and highlighting the need for better annotation quality measures.

This study identifies two mechanisms by which dipeptide esters disrupt lysosomal homeostasis: amyloid fibril formation and proximity labeling via Cathepsin C.

This paper introduces two fluorescence-guided cryo-FIB milling workflows to improve targeting accuracy for cryo-ET, enabling routine capture of structures across spatial scales.

This paper introduces a crossed laser phase plate (xLPP) for cryoEM, demonstrating improved contrast and resolution in imaging biological samples.

AreTomo3 and DenoisET form an automated GPU pipeline that reconstructs cryo-electron tomograms with tile-based contrast transfer function correction, screens their quality, and denoises them during acquisition.

The paper introduces PP7 virus-like particles as a standardized benchmark for cryo-electron tomography, enabling rapid validation and resolution assessment of tomographic pipelines.

This study identifies conserved double-membrane-spanning RNA export pores in arterivirus and coronavirus replication organelles, showing their role in RNA export and encapsidation.

This study demonstrates that Hsp90 presents the glucocorticoid receptor to the CHIP E3 ubiquitin ligase for degradation during its folding cycle.

HetSIREN is a deep learning method for CryoEM conformational state reconstruction and refinement, improving structural accuracy by decoupling pose and CTF information from conformational landscapes.

The paper uses cryo-electron tomography to reveal the structure of cilium inner junctions and shows how protein distribution affects structural stability and assembly.

This paper introduces a deconvolution method called AR-Decon to improve the quality of cryo-EM maps and shows it is robust and broadly applicable.

The paper introduces a phantom sample and annotated 3D volumes for a machine learning challenge to improve cryoET volume annotation.

The paper identifies a lipid-based compartment in early phage infection that protects phage DNA and supports early transcription and translation.

This study identifies Poc1 as a basal body protein that stabilizes triplet microtubules and interconnections, enhancing resistance to ciliary forces.

This study uses co-fractionation mass spectrometry to map host-pathogen and pathogen-pathogen interactions in jumbophages infecting Pseudomonas aeruginosa, revealing over 6000 interactions and novel viral components.

The paper identifies and functionally characterizes MIPs lost in RIB72A/B knockout Tetrahymena cells using proteomics and cryo-electron tomography.

This study identifies a novel non-canonical mechanism by which Hsp70 blocks α-synuclein oligomer formation, independent of ATP and the typical substrate-binding cleft.

Affinity-purification mass spectrometry of 26 SARS-CoV-2 proteins in HEK293T cells yields 332 high-confidence host interactions and 67 druggable human proteins with known compounds.

This study identifies small molecules that target the intrinsically disordered ensemble of α-synuclein, showing they can inhibit misfolding, restore phagocytosis, and block cellular transmission of α-synuclein.

The paper presents atomic structures of the γ-Tubulin Small Complex (γTuSC) and identifies phosphorylation sites that may regulate its function in microtubule nucleation.

The paper investigates how GTP binding and hydrolysis control dynamic instability in PhuZ filaments, revealing structural changes and mechanisms distinct from microtubules.

The paper shows ATP hydrolysis in TRAP1 is sequential and asymmetric, with conformational flipping during the cycle to remodel client proteins.