Author

S. Maurer-Stroh

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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Microbiology· 3 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Assay:proteomics· 3 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

B. Wang· 2 shared C.-I. Wang· 2 shared L. Renia· 2 shared A. C. Hurt· 1 shared A. Manglik· 1 shared A. Mirazimi· 1 shared A. Pizzorno· 1 shared A. Torres· 1 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersImmunology

B. Wang

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4 papers

Recent·Most cited

Predicting potentially permissive substitutions that improve the fitness of A(H1N1)pdm09 viruses bearing the H275Y NA substitution

R. Farrukee, V. Gunalan, S. Maurer-Stroh, P. C. Reading, A. C. Hurt

This study predicts and validates permissive mutations that could restore fitness to oseltamivir-resistant A(H1N1)pdm09 viruses with the H275Y NA substitution.

bioRxiv · Mar 21, 2021 · PreprintMicrobiology

Neutralizing antibodies from early cases of SARS-CoV-2 infection offer cross-protection against the SARS-CoV-2 D614G variant.

C. Y.-P. Lee, S. N. Amrun, R. S.-L. Chee, Y. S. Goh, T. M. Mak, S. Octavia, N. Yeo, Z. W. Chang, M. Z. Tay, A. Torres, G. Carissimo, C. M. Poh, S.-W. Fong, B. Wang, S. Lee, , L. F. P. Ng

This study shows that antibodies from early SARS-CoV-2 infections neutralize both the original and D614G variants, though neutralizing capacity decreases over time.

bioRxiv · Oct 8, 2020 · PreprintImmunology

Monoclonal antibodies for the S2 subunit of spike of SARS-CoV cross-react with the newly-emerged SARS-CoV-2

Z. Zheng, V. M. Monteil, S. Maurer-Stroh, C. W. Yew, C. Leong, N. K. Mohd-Ismail, S. C. Arularasu, V. T. K. Chow, R. T. P. Lin, A. Mirazimi, W. Hong, Y.-J. Tan

This study shows that monoclonal antibodies against SARS-CoV's S2 subunit cross-react with SARS-CoV-2, highlighting sequence conservation and potential utility in diagnostics.

Eurosurveillance · Jul 16, 2020Peer-reviewedMicrobiology

Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization

B. Wang, D. Asarnow, W.-H. Lee, C.-W. Huang, B. Faust, P. M. L. Ng, E. Z. X. Ngoh, M. Bohn, D. Bulkley, A. Pizzorno, H. C. Tan, C. Y. Lee, R. A. Minhat, O. Terrier, M. K. Soh, , C.-I. Wang

This study identifies a potent SARS-CoV-2 neutralizing antibody, 5A6, that binds bivalently to two RBDs on the spike protein, showing resistance to key mutations.

bioRxiv · Jul 14, 2020 · PreprintMicrobiology