Author

J. Z. Vilseck

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· 3 Approach:statistical model· 3 Approach:deep learning· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Research Focus:protein design· 1 Assay:protein sequence· 1

Frequent Co-Authors

A. Hudmon· 1 shared C. A. Berryhill· 1 shared E. M. Cornett· 1 shared F. K. Sahoo· 1 shared J. J. Ziarek· 1 shared J. Meng· 1 shared J. N. Hanquier· 1 shared K. Sanders· 1 shared

Activity by Year

2022-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiochemistry

A. Hudmon

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Author profile →

4 papers

Recent·Most cited

Chemically induced partial unfolding of the multifunctional Apurinic/apyrimidinic endonuclease 1

R. Rai, O. Dawodu, J. Meng, S. M. Johnson, J. Z. Vilseck, M. R. Kelley, J. J. Ziarek, M. M. Georgiadis

This study investigates how the redox inhibitor APX3330 induces reversible partial unfolding of APE1, revealing structural changes relevant to its redox function.

Protein Science · May 15, 2025Peer-reviewedBiochemistry

A {lambda}-dynamics investigation of insulin Wakayama and other A3 variant binding affinities to the insulin receptor

M. P. Barron, J. Z. Vilseck

This paper uses {lambda}-dynamics to compute binding free energies of insulin variants with A3 mutations, showing high agreement with experimental data and revealing structural changes in insulin-IR interactions.

bioRxiv · Mar 15, 2024 · PreprintBiophysics

In silico {lambda}-dynamics predicts protein binding specificities to modified RNAs

M. Angelo, W. Zhang, J. Z. Vilseck, S. T. Aoki

This paper uses in silico λ-dynamics to predict antibody binding specificities to RNA modifications, showing high agreement with experimental results.

bioRxiv · Jan 26, 2024Biochemistry

Substrate selectivity of the PRDM9 lysine methyltransferase domain.

J. N. Hanquier, K. Sanders, C. A. Berryhill, F. K. Sahoo, A. Hudmon, J. Z. Vilseck, E. M. Cornett

This study identifies PRDM9's substrate selectivity, showing it preferentially methylates non-histone proteins over histones, with structural and biochemical validation.

bioRxiv · Oct 12, 2022Biochemistry