Author

A. P. Sergeeva

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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Organism:Drosophila· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Approach:statistical model· 2 Approach:deep learning· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:synaptic & neural circuits· 1

Frequent Co-Authors

B. Honig· 3 shared L. Shapiro· 3 shared P. S. Katsamba· 3 shared F. Cosmanescu· 2 shared N. C. Morano· 2 shared S. Mannepalli· 2 shared B. Bornstein· 1 shared D. S. Lopez· 1 shared

Activity by Year

2020-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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3 shared papersBiophysics

B. Honig

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Author profile →

3 papers

Recent·Most cited

Cis inhibition of co-expressed DIPs and Dprs shapes neural development

N. C. Morano, D. S. Lopez, H. Meltzer, A. P. Sergeeva, P. S. Katsamba, K. D. Rostam, H. P. Gupta, J. E. Becker, B. Bornstein, F. Cosmanescu, O. Schuldiner, B. Honig, R. S. Mann, L. Shapiro

The paper shows that DIPs and Dprs interact in cis within the same cells, regulating trans interactions and influencing neural development in Drosophila.

PLOS Biology · Mar 3, 2025Peer-reviewedBiochemistry

Free energy perturbation calculations of mutation effects on SARS-CoV-2 RBD::ACE2 binding affinity

A. P. Sergeeva, P. S. Katsamba, J. M. Sampson, F. Bahna, S. Mannepalli, N. C. Morano, L. Shapiro, R. A. Friesner, B. Honig

This study uses free energy perturbation calculations to assess how mutations in SARS-CoV-2 RBD affect binding affinity to ACE2, showing FEP's superior accuracy in identifying stabilizing mutations.

bioRxiv · Aug 1, 2022Biophysics

DIP/Dpr interactions and the evolutionary design of specificity in protein families

A. P. Sergeeva, P. S. Katsamba, F. Cosmanescu, J. J. Brewer, G. Ahlsen, S. Mannepalli, L. Shapiro, B. Honig

The paper investigates how specificity in DIP/Dpr protein interactions is achieved through negative constraints, using computational and experimental methods.

bioRxiv · Jan 13, 2020Biophysics