Author

K. Henzler-Wildman

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· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:protein structure· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Tonelli· 4 shared A. Lewis· 2 shared V. Kurauskas· 2 shared A. Majumdar· 1 shared A. Osinski· 1 shared C. A. Bingman· 1 shared C. A. Zimprich· 1 shared C. R. Corona· 1 shared

Activity by Year

2021-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersBiochemistry

M. Tonelli

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Reassessing the helix bundle crossing model for gating in a non-selective ion channel

V. Kurauskas, M. Tonelli, K. Henzler-Wildman

The paper uses NMR to show that NaK channels are in an open conformation despite being non-conductive, challenging the helix bundle crossing gating model.

bioRxiv · Apr 18, 2022Biochemistry

Small Molecule Modulation of the Archetypal UbiB protein COQ8

N. H. Murray, A. Lewis, C. R. M. Asquith, J. P. R. Pabon, Z. Fang, N. Ptak, R. W. Smith, J. D. Vasta, C. A. Zimprich, C. R. Corona, M. B. Robers, C. A. Bingman, M. L. Gross, K. Henzler-Wildman, D. J. Pagliarini

The paper develops small molecule inhibitors and activators for COQ8A, a UbiB family protein, using crystallography, NMR, and mass spectrometry to modulate its function in CoQ biosynthesis.

bioRxiv · Mar 22, 2022 · PreprintBiochemistry

The mechanism of RNA capping by SARS-CoV-2

G. J. Park, A. Osinski, G. Hernandez, J. Eitson, A. Majumdar, M. Tonelli, K. Henzler-Wildman, K. Pawlowski, Z. Chen, Y. Li, J. Schoggins, V. S. Tagliabracci

This study reveals how SARS-CoV-2 caps its RNA genome through an unconventional mechanism involving RNAylation and methyltransferase activity, identifying potential antiviral targets.

bioRxiv · Feb 7, 2022Biochemistry

pH-dependent polymorphism of the structure of SARS-CoV-2 nsp7

Y. Lee, M. Tonelli, M. Rahimi, T. K. Anderson, R. N. Kirchdoerfer, K. Henzler-Wildman, W. Lee

This study determines the solution structure of SARS-CoV-2 nsp7 at pH 7.0 using NMR spectroscopy and identifies pH-dependent structural changes in the protein.

bioRxiv · Sep 10, 2021 · PreprintBiochemistry

Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel

A. Lewis, V. Kurauskas, M. Tonelli, K. Henzler-Wildman

This study investigates how bound Na+ and K+ ions affect the structure and dynamics of the NaK channel's selectivity filter, revealing dynamic behavior and allosteric coupling.

bioRxiv · Jun 16, 2021Biophysics