Author

S. M. Costello

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· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:protein structure· 2 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

S. Marqusee· 3 shared A. W. Nguyen· 2 shared C.-L. Hsieh· 2 shared J. A. Maynard· 2 shared J. S. McLellan· 2 shared S. R. Shoemaker· 2 shared A. L. Bohanon· 1 shared A. M. DiVenere· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

S. Marqusee

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Identification of a conserved neutralizing epitope present on spike proteins from all highly pathogenic coronaviruses

Y. Huang, A. W. Nguyen, C.-L. Hsieh, R. Silva, O. S. Olaluwoye, R. Wilen, T. S. Kaoud, L. R. Azouz, A. N. Qerqez, K. C. Le, A. L. Bohanon, A. M. DiVenere, Y. Liu, D. Amengor, S. R. Shoemaker, , J. A. Maynard

The paper identifies a conserved neutralizing epitope on the S2 domain of SARS-CoV, SARS-CoV-2, and MERS-CoV spike proteins that is targeted by antibody 3A3.

eLife · Mar 21, 2023Peer-reviewedBiochemistry

Evolution avoids a pathological stabilizing interaction in the immune protein S100A9

J. L. Harman, P. N. Reardon, S. M. Costello, G. D. Warren, S. R. Phillips, P. J. Connor, S. Marqusee, M. J. Harms

The paper identifies a mutation in S100A9 that stabilizes a non-functional conformation, revealing an evolutionary constraint on stabilizing mutations.

bioRxiv · May 9, 2022 · PreprintBiophysics

The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes

S. M. Costello, S. R. Shoemaker, H. T. Hobbs, A. W. Nguyen, C.-L. Hsieh, J. A. Maynard, J. S. McLellan, J. E. Pak, S. Marqusee

The paper identifies an alternative open-trimer conformation of the SARS-CoV-2 spike ectodomain that exposes novel epitopes and is modulated by temperature, binding, and sequence variants.

bioRxiv · Jul 11, 2021Biophysics