Author

D. B. Ritchie

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 1 Approach:statistical model· 1 Organism:virus· 1

Frequent Co-Authors

M. T. Woodside· 3 shared K. Neupane· 2 shared M. Zhao· 2 shared S. M. Ileperuma· 2 shared S. Munshi· 2 shared A. Lyons· 1 shared A. Narayan· 1 shared M. T. Halma· 1 shared

Activity by Year

2020-2020 · peak 3/yr

Co-Author Collaboration Network

9 top collaborators · 29 mutual co-author links

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3 shared papersBiophysics

M. T. Woodside

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Author profile →

3 papers

Recent·Most cited

Structural dynamics of the SARS-CoV-2 frameshift-stimulatory pseudoknot reveal topologically distinct conformers

K. Neupane, M. Zhao, A. Lyons, S. Munshi, S. M. Ileperuma, D. B. Ritchie, N. Q. Hoffer, A. Narayan, M. T. Woodside

The paper investigates the structural dynamics of the SARS-CoV-2 frameshift-stimulatory pseudoknot under tension, revealing multiple conformers and their folding mechanisms.

bioRxiv · Dec 28, 2020Biophysics

Conformational Shannon entropy of mRNA structures from force spectroscopy measurements predicts the efficiency of -1 programmed ribosomal frameshift stimulation

M. T. Halma, D. B. Ritchie, M. T. Woodside

The paper shows that -1 PRF efficiency correlates with the conformational heterogeneity of mRNA structures, measured as Shannon entropy, and this correlation depends on force.

bioRxiv · Dec 12, 2020Biophysics

Anti-frameshifting ligand active against SARS coronavirus-2 is resistant to natural mutations of the frameshift-stimulatory pseudoknot

K. Neupane, S. Munshi, M. Zhao, D. B. Ritchie, S. M. Ileperuma, M. T. Woodside

The paper examines how natural mutations in the SARS-CoV-2 pseudoknot affect −1 PRF efficiency and the activity of anti-frameshifting ligands, finding that ligand activity remains resistant to most mutations.

bioRxiv · Jun 29, 2020Biochemistry