Author

N. M. Dietzen

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 2 Assay:cryo-EM· 1 Assay:structural biology· 1

Frequent Co-Authors

G. Brannigan· 3 shared J. T. Petroff· 3 shared L. J. Chen· 2 shared M. J. Arcario· 2 shared W. W. Cheng· 2 shared B. Deng· 1 shared D. F. Covey· 1 shared E. Santiago-McRae· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiophysics

G. Brannigan

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3 papers

Recent·Most cited

Lipid nanodisc scaffold and size alters the structure of a pentameric ligand-gated ion channel

V. Dalal, M. J. Arcario, J. T. Petroff, N. M. Dietzen, M. J. Rau, J. A. J. Fitzpatrick, G. Brannigan, W. W. L. Cheng

This study shows that different lipid nanodisc scaffolds and sizes alter the structure of the pentameric ligand-gated ion channel ELIC, with larger nanodiscs promoting more activated conformations.

bioRxiv · Nov 20, 2022Biophysics

Structural mechanism of leaflet-specific phospholipid modulation of a pentameric ligand-gated ion channel

J. T. Petroff, N. M. Dietzen, E. Santiago-McRae, B. Deng, M. S. Washington, L. J. Chen, K. T. Moreland, Z. Deng, M. Rau, J. A. Fitzpatrick, P. Yuan, T. T. Joseph, J. Henin, G. Brannigan, W. W. Cheng

The paper shows phosphatidylglycerol stabilizes the open state of ELIC by binding to a specific outer leaflet site, identified through structural and functional analyses.

bioRxiv · Jun 7, 2022 · PreprintBiophysics

Polyunsaturated fatty acids inhibit a pentameric ligand-gated ion channel through one of two binding sites

N. M. Dietzen, M. J. Arcario, L. J. Chen, J. T. Petroff, K. Krishnan, G. Brannigan, D. F. Covey, W. W. Cheng

This study identifies two fatty acid binding sites in ELIC and shows that DHA selectively inhibits the channel by binding to a specific site in the agonist-bound state.

bioRxiv · Oct 8, 2021Biochemistry