Author

A. Hudmon

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Physiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Assay:electrophysiology· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Shestak· 1 shared C. A. Berryhill· 1 shared D. Ross-Kaschitza· 1 shared E. M. Cornett· 1 shared E. V. Zaklyazminskaya· 1 shared F. K. Sahoo· 1 shared G. S. Pitt· 1 shared H. Abriel· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperPhysiology

A. Shestak

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

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

Calmodulin binds to the N-terminal domain of the cardiac sodium channel Nav1.5

Z. Wang, S. H. Vermij, V. Sottas, A. Shestak, D. Ross-Kaschitza, E. V. Zaklyazminskaya, A. Hudmon, G. S. Pitt, J.-S. Rougier, H. Abriel

This study identifies calmodulin as a new binding partner of the Nav1.5 N-terminal domain and shows that mutations in this region impair the interaction, contributing to dominant-negative effects in Brugada Syndrome.

bioRxiv · Jun 2, 2020Physiology