Ting Ran

Jan 21, 2025 | nature.com | Yongzhi Lu |Qi Yang |Ting Ran |Wei Zhang |Deyin Guo |Xinwen Chen | +1 more

Correction to: Nature Communications https://doi.org/10.1038/s41467-024-54462-0, published online 23 November 2024In this article there is an error in Figure 1 where the residue labelling incorrectly read E164 and should be D164. The original article has been corrected.

Nov 22, 2024 | nature.com | Yongzhi Lu |Qi Yang |Ting Ran |Wei Zhang |Deyin Guo |Xinwen Chen | +1 more

AbstractThe RNA-dependent RNA polymerase (RdRp), 3C-like protease (3CLpro), and papain-like protease (PLpro) are pivotal components in the viral life cycle of SARS-CoV-2, presenting as promising therapeutic targets. Currently, all FDA-approved antiviral drugs against SARS-CoV-2 are RdRp or 3CLpro inhibitors. However, the mutations causing drug resistance have been observed in RdRp and 3CLpro from SARS-CoV-2, which makes it necessary to develop antivirals with novel mechanisms.

Jul 3, 2024 | nature.com | Ting Ran |Luke W. Guddat |Yan Gao |Fengjiang Liu

AbstractBedaquiline (BDQ), a first-in-class diarylquinoline anti-tuberculosis drug, and its analogue, TBAJ-587, prevent the growth and proliferation of Mycobacterium tuberculosis by inhibiting ATP synthase1,2. However, BDQ also inhibits human ATP synthase3. At present, how these compounds interact with either M. tuberculosis ATP synthase or human ATP synthase is unclear. Here we present cryogenic electron microscopy structures of M.