Author

L. W. Guddat

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· 5 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:protein structure· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Organism:virus· 2 Assay:cryo-EM· 1 Approach:deep learning· 1

Frequent Co-Authors

X. Yang· 4 shared Z. Rao· 4 shared B. Zhang· 3 shared H. Yang· 3 shared L. Zhang· 3 shared Y. Zhao· 3 shared C. Zhu· 2 shared F. Liu· 2 shared

Activity by Year

2019-2021 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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4 shared papersBiochemistry

X. Yang

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Author profile →

6 papers

Recent·Most cited

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

Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse and widespread in the environment.

M. Monteiro Pedroso, D. Waite, O. Melse, L. Wilson, N. Mitic, R. P. McGeary, I. Antes, L. W. Guddat, P. Hugenholtz, G. Schenk

The paper identifies a broad phylogenetic diversity of B3 MBLs in environmental microbes and shows that a variant (B3-RQK) is sensitive to clavulanic acid due to a lysine residue in its active site.

Protein & Cell · Jun 15, 2020Peer-reviewedBiochemistry

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 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

Structural elements that modulate the substrate specificity of plant purple acid phosphatases: avenues for improved phosphorus acquisition in crops

D. Feder, R. P. McGeary, N. Mitic, T. Lonhienne, A. Furtado, B. L. Schulz, R. J. Henry, S. Schmidt, L. W. Guddat, G. Schenk

The paper identifies structural elements in plant purple acid phosphatases that influence substrate specificity, offering insights for improving phosphorus acquisition in crops.

bioRxiv · Aug 28, 2019Biochemistry