Author

D. H. Russell

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· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Organism:E. coli· 1 Assay:protein structure· 1 Assay:proteomics· 1 Organism:virus· 1

Frequent Co-Authors

A. Laganowsky· 2 shared B. Sankaran· 1 shared C. A. Fierkee· 1 shared C.-W. Lin· 1 shared D. Clemmer· 1 shared D. P. Barondeau· 1 shared H. M. Sun· 1 shared H. Rye· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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2 shared papersBiochemistry

A. Laganowsky

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4 papers

Recent·Most cited

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions

J. Lyu, T. Zhang, M. Marty, D. Clemmer, D. H. Russell, A. Laganowsky

The paper uses native mass spectrometry and mutant cycles to study the thermodynamics of MsbA-LPS interactions, revealing entropy-driven binding and conformational changes.

bioRxiv · Jul 3, 2023Biochemistry

Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time

T. Walker, H. M. Sun, T. Gunnels, V. Wysocki, A. Laganowsky, H. Rye, D. H. Russell

This paper uses variable-temperature electrospray ionization native mass spectrometry to study the thermodynamics of ATP binding to the GroEL complex, revealing enthalpy-entropy compensation and cooperativity.

bioRxiv · Sep 13, 2022Biophysics

A Novel Y-Shaped, S-O-N-O-S-Bridged Crosslink between Three Residues C22, C44, and K61 Is a Redox Switch of the SARS-CoV-2 Main Protease

K. S. Yang, S.-T. A. Kuo, L. R. Blankenship, Y. J. Sheng, B. Sankaran, P. Li, C. A. Fierkee, D. H. Russell, X. Yan, S. Xu, W. R. Liu

The paper identifies a novel Y-shaped crosslink in SARS-CoV-2 MPro that acts as a redox switch, regulating its catalytic activity and offering new targets for antiviral drug development.

bioRxiv · Apr 29, 2022 · PreprintBiochemistry

Recapitulating the frataxin activation mechanism in an engineered bacterial cysteine desulfurase supports the architectural switch model

S. Patra, C.-W. Lin, M. K. Ghosh, S. M. Havens, S. A. Cory, D. H. Russell, D. P. Barondeau

The paper engineers a bacterial cysteine desulfurase to recapitulate the frataxin activation mechanism, supporting the architectural switch model by showing FXN compensates for lost subunit interactions.

bioRxiv · Oct 6, 2020 · PreprintBiochemistry