Author

B. Nepal

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:statistical model· 3 Approach:deep learning· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Sepehri· 3 shared T. Lazaridis· 3 shared A. A. Ramanathan· 1 shared A. B. Vaidya· 1 shared A. Shukla· 1 shared J. M. Morrisey· 1 shared L. W. Bergman· 1 shared M. W. Mather· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiophysics

A. Sepehri

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Mutational Analysis of an Antimalarial Drug Target PfATP4

S. Rachuri, B. Nepal, A. Shukla, A. A. Ramanathan, J. M. Morrisey, T. M. Daly, M. W. Mather, L. W. Bergman, S. Kortagere, A. B. Vaidya

The paper models PfATP4 structure using homology and validates predictions through genetic manipulation, identifying key residues for function and resistance.

bioRxiv · Feb 21, 2024 · PreprintMicrobiology

Distinct modes of action of IAPP oligomers on membranes

A. Sepehri, B. Nepal, T. Lazaridis

The paper models and simulates pore formation by IAPP oligomers in membranes, finding distinct structural behaviors between helical and β-structured peptides.

bioRxiv · Jun 24, 2021Biophysics

Lipid interactions of an actinoporin pore-forming oligomer

A. Sepehri, B. Nepal, T. Lazaridis

This study uses molecular dynamics simulations to investigate how actinoporin oligomers interact with lipid membranes, finding that phase coexistence, not specific sphingomyelin recognition, drives membrane targeting.

bioRxiv · Oct 2, 2020Biophysics

Mechanism of negative membrane curvature generationby I-BAR domains

B. Nepal, A. Sepehri, T. Lazaridis

This study shows that I-BAR domains generate negative membrane curvature through their higher oligomeric structure, not their intrinsic dimer curvature.

bioRxiv · Aug 19, 2020Biophysics