Author

P. Shrestha

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 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Approach:deep learning· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

A. W. Smith· 1 shared A. Yaparla· 1 shared B. Wang· 1 shared D. A. Davis· 1 shared D. Yang· 1 shared H. Bulut· 1 shared H. K. Jaeger· 1 shared H. Mitsuya· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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1 shared paperBiophysics

A. W. Smith

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The SAM Domain of EphA2 Inhibits Ligand-Independent Clustering and Activation

X. Shi, R. Lingerak, P. Shrestha, M. Buck, B. Wang, A. W. Smith

This study investigates the role of the SAM domain in EphA2, showing it inhibits ligand-independent clustering and kinase activity in both full-length and intracellular domain constructs.

bioRxiv · Oct 5, 2023 · PreprintBiophysics

Mapping Single-molecule Protein Complexes in 3D with DNA Nanoswitch Calipers

P. Shrestha, D. Yang, W. M. Shih, W. P. Wong

The paper introduces a method to map 3D geometries of single-molecule protein complexes with high resolution using DNA Nanoswitch Calipers and force-based barcoding, achieving agreement with known structures.

bioRxiv · Jul 10, 2023Biophysics

Efficient End-to-end Learning for Cell Segmentation with Machine Generated Incomplete Annotations

P. Shrestha, N. Kuang, J. Yu

This paper introduces a model trained with machine-generated incomplete annotations for cell segmentation, achieving accuracy comparable to fully supervised methods.

bioRxiv · Jul 3, 2022 · PreprintCell Biology

Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300

D. A. Davis, H. Bulut, P. Shrestha, A. Yaparla, H. K. Jaeger, S.-i. Hattori, P. Wingfield, H. Mitsuya, R. Yarchoan

This study shows that SARS-CoV-2 main protease (Mpro) activity and dimerization are regulated by reversible glutathionylation of Cys300, offering a new target for antiviral agents.

bioRxiv · Apr 9, 2021Microbiology