Author

T. Schulze

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 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:bacteria (other)· 1 Assay:electrophysiology· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Moroni· 3 shared G. Thiel· 3 shared O. Rauh· 2 shared A. Bertl· 1 shared A. Hartel· 1 shared B. Hertel· 1 shared C. Hemming· 1 shared D. Eckert· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersPathology

A. Moroni

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

SARS-CoV-2 envelope-protein corruption of homeostatic signaling mechanisms in mammalian cells

T. Schulze, A. Hartel, S. Hoeler, C. Hemming, R. Lehn, D. Tandl, T. Greiner, A. Bertl, K. Shepard, A. Moroni, G. Thiel, O. Rauh

This study shows that SARS-CoV-2 envelope protein disrupts cellular homeostasis by forming ion channels, leading to altered Ca2+ and pH levels and membrane depolarization.

bioRxiv · Jun 16, 2021 · PreprintPathology

A small viral potassium ion channel with an inherent inward rectification

D. Eckert, T. Schulze, J. Stahl, O. Rauh, J. L. Van Etten, B. Hertel, I. Schroeder, A. Moroni, G. Thiel

The paper identifies a small viral K+ channel with inherent inward rectification, distinguishing it from canonical Kir channels by showing rectification is a property of the transmembrane domains.

bioRxiv · Feb 24, 2019Biophysics

Structural basis for ion selectivity in TMEM175 K+ channels

J. D. Brunner, R. P. Jakob, T. Schulze, Y. Neldner, A. Moroni, G. Thiel, T. Maier, S. Schenck

This study determines the X-ray structure of a bacterial TMEM175 K+ channel, revealing a unique cation-selective mechanism involving a conserved threonine residue and conformational changes.

bioRxiv · Dec 4, 2018Biochemistry