Author

S. L. Sterling

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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Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Organism:mouse· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. F. Flynn· 1 shared A. Hajduczki· 1 shared A. R. Lindrose· 1 shared C. C. Broder· 1 shared C. P. Morris· 1 shared C. Peterson· 1 shared C. Smith· 1 shared E. C. Green· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperMicrobiology

A. F. Flynn

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Bma-LAD-2, an intestinal cell adhesion protein, as a potential therapeutic target for lymphatic filariasis

A. F. Flynn, R. T. Taylor, M. E. Pazgier, S. Bennuru, A. R. Lindrose, S. L. Sterling, C. P. Morris, T. K. Maugel, T. B. Nutman, E. Mitre

This study identifies Bma-LAD-2 as an essential protein in adult Brugia malayi worms, showing that its knockdown reduces worm motility, fecundity, and viability, suggesting it as a potential therapeutic target for lymphatic filariasis.

bioRxiv · Sep 9, 2021 · PreprintMicrobiology

A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein

M. G. Joyce, R. S. Sankhala, W.-H. Chen, M. Choe, H. Bai, A. Hajduczki, L. Yan, S. L. Sterling, C. Peterson, E. C. Green, C. Smith, N. de Val, M. Amare, P. Scott, E. D. Laing, , K. Modjarrad

The paper reports the high-resolution structure of the SARS-CoV-2 Spike RBD and identifies a conserved epitope accessible in open conformations, which is targeted by cross-reactive antibodies.

bioRxiv · Mar 15, 2020 · PreprintImmunology