5 Papers
Qin Yu is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: MDA5 & ATP hydrolysis. The author has an hindex of 2, co-authored 4 publications. Previous affiliations of Qin Yu include University of Cambridge & ETH Zurich.
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Papers
Cryo-EM Structures of MDA5-dsRNA Filaments at Different Stages of ATP Hydrolysis.
Qin Yu,Kun Qu,Yorgo Modis +2 more
TL;DR: Cryoelectron microscopy (cryo-EM) structures of MDA5-dsRNA filaments with different helical twists and bound nucleotide analogs are determined at resolutions sufficient to build and refine atomic models, providing insights on how ATP hydrolysis contributes to MDA 5-ds RNA recognition.
51
Differential dynamics and direct interaction of bound ligands with lipids in multidrug transporter ABCG2
Ali Rasouli,Qin Yu,Sepehr Dehghani-Ghahnaviyeh,Po-Chao Wen,Julia Kowal,Kaspar P. Locher,Emad Tajkhorshid +6 more
TL;DR: In this paper , the authors showed that lipids as well as the ligand size can impact the drug-binding mode of ABC transporters and demonstrated that phospholipids from the cellular membrane can penetrate into the protein and directly interact with bound drugs.
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MDA5 disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA.
Qin Yu,Qin Yu,Qin Yu,Alba Herrero del Valle,Alba Herrero del Valle,Rahul Singh,Rahul Singh,Yorgo Modis,Yorgo Modis +8 more
TL;DR: In this article, the authors show how the disease-associated MDA5 variant M854K perturbs DsRNA recognition and demonstrate that the K854 sidechain forms polar bonds that constrain the conformation of subdomains, disrupting key steps in the ATPase cycle- RNA footprint expansion and helical twist modulation.
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MDA5 autoimmune disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA
Qin Yu,Qin Yu,Alba Herrero del Valle,Alba Herrero del Valle,Rahul Singh,Rahul Singh,Yorgo Modis,Yorgo Modis +7 more
TL;DR: In this paper, the authors show how the disease-associated MDA5 variant M854K perturbs DsRNA recognition and demonstrate that the side-chain forms polar bonds that constrain the conformation of subdomains, disrupting key steps in the ATPase cycle-RNA footprint expansion.
CryoEM structures of MDA5-dsRNA filaments at different stages of ATP hydrolysis
Qin Yu,Kun Qu,Yorgo Modis +2 more
TL;DR: CryoEM structures of MDA5-dsRNA filaments determined for three catalytic states reveal a flexible, predominantly hydrophobic filament forming interface and show how the ATPase cycle is coupled to changes in helical twist, the mode of RNA binding and the length of the RNA footprint of Mda5.