Author

T. Drace

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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Microbiology· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Assay:electronic health records· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

T. Boesen· 3 shared T. Santl-Temkiv· 2 shared A. Boggild· 1 shared A. Schramm· 1 shared A. Zipori· 1 shared D. Niedermeier· 1 shared E. D. Bojesen· 1 shared G. Kramer· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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Curved chords = mutual co-authorship

3 shared papersMicrobiology

T. Boesen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Comparative electric and ultrastructural studies of cable bacteria reveal new components of conduction machinery

L. Digel, M. L. Justesen, R. Bonne, N. Fransaert, K. Wouters, P. B. Jensen, L. E. Plum-Jensen, I. P. G. Marshall, L. Nicolas-Asselineau, T. Drace, A. Boggild, J. L. Hansen, A. Schramm, E. D. Bojesen, L. P. Nielsen, , T. Boesen

This study compares electric and ultrastructural features of cable bacteria, revealing conserved conduction mechanisms and novel metabolic structures.

bioRxiv · May 24, 2023 · PreprintMicrobiology

Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity

S. Hartmann, M. Ling, L. S. A. Dreyer, A. Zipori, K. W. Finster, S. Grawe, L. Z. Jensen, S. Borck, N. Reicher, T. Drace, D. Niedermeier, N. C. Jones, S. V. Hoffmann, H. Wex, Y. Rudich, , T. Santl-Temkiv

The paper determines the structure and protein-protein interactions of ice nucleation proteins and shows they are essential for their activity.

bioRxiv · Jan 21, 2022Microbiology

The Ice Nucleating Protein InaZ is Activated by Low Temperature

S. J. Roeters, T. W. Golbek, M. Bregnhoj, T. Drace, S. Alamdari, W. Roseboom, G. Kramer, T. Santl-Temkiv, K. Finster, S. Woutersen, J. Pfaendtner, T. Boesen, T. Weidner

This study investigates how the ice-nucleating protein InaZ from Pseudomonas syringae folds and interacts with water at low temperatures, revealing structural changes that enhance ice nucleation.

bioRxiv · May 15, 2020 · PreprintBiophysics