Author

R. Kirchdoerfer

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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Biophysics· 2 Pharmacology & Toxicology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 3 Research Focus:drug response / drug discovery· 2 Organism:virus· 2 Assay:imaging· 1

Frequent Co-Authors

C. E. Cameron· 2 shared C. Tao· 2 shared D. Dulin· 2 shared J. J. Arnold· 2 shared J. J. Russo· 2 shared M. Chien· 2 shared S. Jockusch· 2 shared S. Kumar· 2 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersBiochemistry

C. E. Cameron

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Interfering with nucleotide excision by the coronavirus 3'-to-5' exoribonuclease

R. Chinthapatla, M. S. Sotoudegan, T. Anderson, I. M. Moustafa, K. T. Passow, S. A. Kennelly, R. Moorthy, D. Dulin, J. Y. Feng, D. A. Harki, R. Kirchdoerfer, C. E. Cameron, J. J. Arnold

This study investigates how SARS-CoV-2's ExoN enzyme processes RNA and identifies modifications that block its activity, offering potential for new antiviral strategies.

bioRxiv · Aug 11, 2022Biochemistry

Structure and immune recognition of the porcine epidemic diarrhea virus spike protein

R. Kirchdoerfer, M. Bhandari, O. Martini, L. M. Sewell, S. Bangaru, K.-J. Yoon, A. Ward

The paper structures the PEDV spike protein using electron microscopy and characterizes the antibody response, revealing structural features and epitope dominance in the S1 region.

Structure · Apr 1, 2021Peer-reviewedBiophysics

The nucleotide addition cycle of the SARS-CoV-2 polymerase

S. C. Bera, M. Seifert, R. Kirchdoerfer, P. van Nies, Y. Wubulikasimu, S. Quack, F. S. Papini, J. J. Arnold, B. Canard, C. E. Cameron, M. Depken, D. Dulin

This study describes the mechanochemical behavior of the SARS-CoV-2 polymerase using magnetic tweezers, revealing three catalytic conformations and a thermal ratchet mechanism for nucleotide incorporation.

bioRxiv · Mar 27, 2021Biophysics

Triphosphates of the Two Components in DESCOVY and TRUVADA are Inhibitors of the SARS-CoV-2 Polymerase

S. Jockusch, C. Tao, X. Li, T. K. Anderson, M. Chien, S. Kumar, J. J. Russo, R. Kirchdoerfer, J. Ju

The paper shows that the triphosphates of tenofovir and emtricitabine inhibit SARS-CoV-2 RNA-dependent RNA polymerase, suggesting potential use of DESCOVY and TRUVADA as PrEP for COVID-19.

bioRxiv · Apr 3, 2020 · PreprintPharmacology & Toxicology

Nucleotide Analogues as Inhibitors of SARS-CoV-2 Polymerase

M. Chien, T. K. Anderson, S. Jockusch, C. Tao, S. Kumar, X. Li, J. J. Russo, R. Kirchdoerfer, Jingyue Ju

This study shows that three nucleotide analogues inhibit SARS-CoV-2 polymerase by being incorporated and blocking further RNA synthesis.

bioRxiv · Mar 12, 2020Pharmacology & Toxicology