Author

D. Nedrud

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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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 4 Assay:proteomics· 3 Approach:deep learning· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:differential expression· 1 Approach:machine learning (classical)· 1 Assay:protein structure· 1

Frequent Co-Authors

D. Schmidt· 4 shared W. Coyote-Maestas· 3 shared Y. He· 3 shared A. C. Zdechlik· 1 shared A. Suma· 1 shared C. L. Myers· 1 shared D. M. Fowler· 1 shared G. Aslanidi· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersBiochemistry

D. Schmidt

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Author profile →

4 papers

Recent·Most cited

Multiparametric domain insertional profiling of Adeno-Associated Virus VP1

M. D. Hoffmann, A. C. Zdechlik, Y. He, D. Nedrud, G. Aslanidi, W. Gordon, D. Schmidt

The paper inserts large protein domains into AAV capsid protein VP1 to identify engineerable hotspots and assess capsid robustness to structural modifications.

bioRxiv · Apr 19, 2023Biochemistry

Determinants of trafficking, conduction, and disease within a K+ channel revealed through multiparametric deep mutational scanning

W. Coyote-Maestas, D. Nedrud, Y. He, D. Schmidt

The paper uses deep mutational scanning to analyze how mutations affect Kir2.1 channel function, trafficking, and disease, revealing structural and functional determinants of pathogenicity.

bioRxiv · Jan 6, 2022Biochemistry

The biophysical basis of protein domain compatibility

W. Coyote-Maestas, D. Nedrud, A. Suma, Y. He, K. A. Matreyek, D. M. Fowler, V. Carnevale, C. L. Myers, D. Schmidt

The paper uses high-throughput assays and machine learning to model biophysical interactions governing protein domain compatibility in fusion proteins.

bioRxiv · Dec 9, 2020 · PreprintBiophysics

A survey of pairwise epistasis supports an outside-in hierarchy of clade-specifying and function-defining residues in PSD95 PDZ3

D. Nedrud, W. Coyote-Maestas, D. Schmidt

The paper uses deep mutational scanning to analyze epistasis in the PSD95 PDZ3 domain, revealing an outside-in hierarchy of clade-specifying and function-defining residues.

bioRxiv · Jun 26, 2020 · PreprintBiochemistry