Publications
The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding. EMBO J. 10.15252/embj.201797291
(2017) Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein. Protein Sci. 10.1002/pro.3909
(2020) Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein. bioRxiv. 10.1101/2020.05.17.100685
(2020) A conserved filamentous assembly underlies the structure of the meiotic chromosome axis. Elife. 10.7554/eLife.40372
(2019) Control of bacterial immune signaling by a WYL domain transcription factor. Nucleic Acids Res. 50, 5239-5250
(2022) (2023) (2024) HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-like Enzymes to Mediate Bacteriophage Immunity. Mol Cell. 10.1016/j.molcel.2019.12.009
(2019) Structural Basis for SARS-CoV-2 Nucleocapsid Protein Recognition by Single-Domain Antibodies. Front Immunol. 12, 719037
(2021) (2022) Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity. Mol Cell. 10.1016/j.molcel.2019.12.010
(2020) Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. EMBO J. 35, 2139-2151
(2016) TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. Elife. 10.7554/eLife.07367
(2015)