Author

Z. Rao

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Biophysics· 3 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:host-pathogen & immune response· 4 Organism:virus· 3 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Organism:mouse· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2

Frequent Co-Authors

H. Yang· 5 shared L. Zhang· 5 shared X. Yang· 5 shared Y. Zhao· 5 shared B. Zhang· 4 shared H. Wang· 4 shared L. W. Guddat· 4 shared Z. Jin· 4 shared

Activity by Year

2020-2023 · peak 6/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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5 shared papersBiochemistry

H. Yang

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Mecp2 Fine-tunes Quiescence Exit by Targeting Nuclear Receptors

J. Yang, S. Zou, Z. Qiu, M. Lai, Q. Long, H. Chen, P. Lai, S. Zhang, Z. Rao, X. Xie, Y. Gong, A. Liu, M. Li, X. Bai

This study shows Mecp2 negatively regulates quiescence exit by activating metabolic genes and repressing proliferation genes, with nuclear receptors Rara and Nr1h3 playing a key role.

bioRxiv · Jul 24, 2023Cell Biology

Structure of mycobacterial cytochrome bcc in complex with Q203 and TB47, two anti-TB drug candidates

S. Zhou, W. Wang, X. Zhou, Y. Zhang, Y. Lai, Y. Tang, J. Xu, X. Yang, L. W. Guddat, Q. Wang, Y. Gao, Z. Rao, H. Gong

The paper reports the structures of M. tuberculosis cytochrome bcc complexed with two anti-TB drugs, revealing binding sites and interactions that inform inhibitor design.

bioRxiv · Jun 15, 2021Microbiology

Novel inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives

K. Amporndanai, X. Meng, H. Yang, Z.-J. Liu, L. Zhang, Y. Zhao, S. Hasnain, P. O'Neill, Z. Rao, Z. Jin, W. Shang

This study identifies a novel inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives through crystallography and mass spectrometry, revealing a unique covalent adduct formation and by-product generation.

bioRxiv · Mar 11, 2021Biophysics

Double Lock of a Potent Human Monoclonal Antibody against SARS-CoV-2

X. Wang, C. Qin, Y. Wang, Z. Rao, L. Xie, L. Zhu, Y.-Q. Deng, R.-r. Zhang, Z. Cui, C.-Y. Sun, C.-F. Fan, X. Xing, W. Huang, Q. Chen, N.-N. Zhang, , J. Hu

This paper identifies and characterizes a potent human monoclonal antibody, HB27, that blocks SARS-CoV-2 receptor binding and membrane fusion, showing protective effects in mice and non-adverse effects in rhesus macaques.

bioRxiv · Nov 24, 2020 · PreprintBiophysics

Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody

Z. Lv, Y.-Q. Deng, Q. Ye, L. Cao, C.-Y. Sun, C. Fan, W. Huang, S. Sun, Y. Sun, L. Zhu, Q. Chen, N. Wang, J. Nie, Z. Cui, D. Zhu, , X. Wang

A potent neutralizing antibody protected against SARS-CoV-2 in an hACE2 mouse model by blocking viral receptor interaction.

Science · Sep 18, 2020Peer-reviewedBiophysics

Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug Carmofur

Z. Jin, Y. Zhao, Y. Sun, B. Zhang, H. Wang, Y. Wu, Y. Zhu, C. Zhu, T. Hu, X. Du, Y. Duan, J. Yu, X. Yang, X. Yang, K. Yang, , Z. Rao

This study shows Carmofur inhibits SARS-CoV-2 main protease by covalently binding to Cys145 and occupying the S2 subsite, with an EC50 of 24.30 M in cell-based viral replication assays.

bioRxiv · Apr 9, 2020Biochemistry

Structure-Based Design, Synthesis and Biological Evaluation of Peptidomimetic Aldehydes as a Novel Series of Antiviral Drug Candidates Targeting the SARS-CoV-2 Main Protease

W. Dai, B. Zhang, X.-M. Jiang, H. Su, J. Li, Y. Zhao, X. Xie, Z. Jin, J. Peng, F. Liu, C. Li, Y. Li, F. Bai, H. Wang, X. Cheng, , H. Liu

This study designs, synthesizes, and evaluates two peptidomimetic aldehydes as antiviral drug candidates targeting SARS-CoV-2 main protease, showing potent inhibition and anti-infection activity.

bioRxiv · Mar 25, 2020 · PreprintBiochemistry

Structure of RNA-dependent RNA polymerase from 2019-nCoV, a major antiviral drug target

Y. Gao, L. Yan, Y. Huang, F. Liu, Y. Zhao, L. Cao, T. Wang, Q. Sun, Z. Ming, L. Zhang, J. Ge, L. Zheng, Y. Zhang, H. Wang, Y. Zhu, , Z. Rao

The paper reports the cryo-EM structure of 2019-nCoV RdRp complexed with cofactors, revealing key residues and remdesivir binding, aiding antiviral drug design.

bioRxiv · Mar 16, 2020 · PreprintBiochemistry

Structure of Mpro from COVID-19 virus and discovery of its inhibitors

Z. Jin, X. Du, Y. Xu, Y. Deng, M. Liu, Y. Zhao, B. Zhang, X. Li, L. Zhang, C. Peng, Y. Duan, J. Yu, L. Wang, K. Yang, F. Liu, , H. Yang

The paper identifies a mechanism-based inhibitor of the COVID-19 virus main protease through structure-assisted drug design and high-throughput screening.

bioRxiv · Feb 26, 2020Biochemistry