Ning Gao

The paper identifies the role of FACT-(H3-H4) complex in stimulating Pol activity to coordinate DNA synthesis with nucleosome assembly during replication.

The paper identifies CLCC1 as a client of Torsin ATPases, showing they organize CLCC1 to maintain ER bilayer and lipid homeostasis, with implications for MASH development.

This study determines the Cryo-EM structure of the PHB complex and shows it organizes m-AAA proteases in mitochondrial microdomains to regulate proteolytic homeostasis.

The paper uses cryo-EM to study bacterial GTPases in ribosome assembly and translation initiation, revealing their role as placeholders in subunit maturation and translation regulation.

This study determines the cryo-EM structure of the flotillin complex, revealing its role in membrane microdomain organization and phosphorylation-regulated assembly.

This paper reports the cryo-EM structure of a phycobilisome with a bicylindrical core from Synechococcus elongatus PCC 7942, revealing structural adaptations that maintain stability and energy transfer efficiency.

The paper presents the cryo-EM structure of Xenopus IgX, revealing a hexameric assembly that informs strategies for engineering human IgM and IgG hexamers with therapeutic applications.

This study determines the cryo-EM structure of stomatin, revealing its role in organizing functional membrane microdomains and identifying associated proteins involved in cell migration and vesicle trafficking.

This study determines the cryo-EM structure of the erlin1/2 complex and reveals its role in sequestering membrane proteins and organizing functional microdomains on the ER.

This study reports cryo-EM structures of nucleosomes with deoxyinosine and their complexes with DNA glycosylase AAG, revealing how AAG accesses damaged sites on nucleosomes through structural dynamics.

This study reveals the structural and functional mechanism of CLPB, a mitochondrial AAA+ disaggregase, showing its unique assembly and substrate translocation properties.

The paper reports the cryo-EM structure of a potent SARS-CoV-2 NAb, BD-368-2, showing it blocks ACE2 binding and induces structural changes in the spike trimer, distinct from other NAbs.

The paper uses disome-seq to detect ribosome collisions during translation, revealing their role in recruiting co-translational chaperones for protein folding.