Author

J. M. Hansen

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· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:imaging· 1 Research Focus:metabolism & bioenergetics· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

F. DiMaio· 2 shared A. Horowitz· 1 shared B. Zens· 1 shared D. P. Farrell· 1 shared E. M. Lynch· 1 shared F. Faessler· 1 shared F. K. Schur· 1 shared G. Usluer· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

F. DiMaio

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Unveiling the ultrastructural landscape of native extracellular matrix via lift-out cryo-FIBSEM and cryo-ET

B. Zens, F. Faessler, J. M. Hansen, R. Hauschild, J. Datler, V.-V. Hodirnau, V. Zheden, J. Alanko, M. Sixt, F. K. Schur

This paper develops a 3D-ECM platform to visualize native extracellular matrix structures using cryo-FIBSEM and cryo-ET, revealing new insights into ECM composition and organization.

bioRxiv · Sep 25, 2023 · PreprintCell Biology

Cryo-EM Structures of CTP Synthase Filaments Reveal Mechanism of pH-Sensitive Assembly During Budding Yeast Starvation

J. M. Hansen, A. Horowitz, E. M. Lynch, D. P. Farrell, J. Quispe, F. DiMaio, J. M. Kollman

The paper uses cryo-EM to study CTP synthase filament assembly in yeast, revealing pH-sensitive mechanisms and their role in starvation response.

bioRxiv · Aug 25, 2021Biochemistry

Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain

G. Usluer, F. Dimaio, S. Yang, J. M. Hansen, J. K. Polka, R. D. Mullins, J. Kollman

The paper reports the cryo-EM structure of AlfA, a bacterial actin, revealing unique ATP-binding interactions and a missing subdomain that explain its distinct assembly dynamics and plasmid segregation function.

bioRxiv · Sep 7, 2017Biophysics