Author

S. J. Opella

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

S. H. Park· 2 shared A. Carlin· 1 shared A. Clark· 1 shared A. De Angelis· 1 shared A. L. Oom· 1 shared B. Croker· 1 shared B. Kloss· 1 shared C. A. Aspinwall· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersBiophysics

S. H. Park

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu

J. A. Townsend, O. Fapohunda, Z. Wang, H. Pham, M. T. Taylor, B. Kloss, S. H. Park, S. J. Opella, C. A. Aspinwall, M. T. Marty

The paper uses native mass spectrometry to analyze the oligomerization states of SARS-CoV-2 E protein, poliovirus VP4, and HIV Vpu, revealing differences in their assembly patterns.

bioRxiv · Aug 18, 2023Biophysics

Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity

S. H. Park, H. Siddiqi, D. Castro, A. De Angelis, A. L. Oom, C. Stoneham, M. Lewinski, A. Clark, B. Croker, A. Carlin, J. Guatelli, S. J. Opella

This study investigates the structure of SARS-CoV-2 E protein and its interactions with amilorides, finding that binding affinity correlates with antiviral activity and that residue Asn15 is critical for maintaining the binding site conformation.

bioRxiv · Apr 6, 2021Biochemistry

Correlating the structure and activity of Y. pestis Ail in a bacterial cell envelope

J. E. Kent, L. M. Fujimoto, K. Shn, C. Singh, Y. Yao, S. Park, S. J. Opella, G. V. Plano, F. M. Marassi

This study uses an E. coli model system to investigate the structure and function of Y. pestis Ail in a bacterial cell envelope, revealing its role in virulence and interactions with human serum components.

bioRxiv · Sep 23, 2020Biochemistry