Author

J. Rosenau

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· 2 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:ecology & biodiversity· 1 Research Focus:host-pathogen & immune response· 1 Assay:metagenomics· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

S. Kelm· 3 shared M. Waespy· 2 shared N. Dinesh Kumar· 2 shared A. K. Agyapong· 1 shared A. Tweneboah· 1 shared F. Dietz· 1 shared I. A. M. Mahamat· 1 shared I. L. Grothaus· 1 shared

Activity by Year

2021-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiochemistry

S. Kelm

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Author profile →

3 papers

Recent·Most cited

N-glycosylation modulates enzymatic activity of Trypanosoma congolense trans-sialidase

J. Rosenau, I. L. Grothaus, Y. Yang, N. Dinesh Kumar, L. C. Ciacchi, S. Kelm, M. Waespy

This study shows that N-glycans on Trypanosoma congolense trans-sialidase affect substrate affinity but not conversion rate, with molecular dynamics revealing structural interactions that enhance enzyme function.

bioRxiv · Dec 13, 2021Biochemistry

The transmission of African Animal Trypanosomiasis (Nagana) in two districts in the forest zone of Ghana

A. Tweneboah, J. Rosenau, A. K. Agyapong, T. K. Addison, I. A. M. Mahamat, J. S. Weber, S. Kelm, K. Badu

This study investigates trypanosome prevalence and vector density in two Ghanaian districts, finding high infection rates in tsetse flies and pigs with T. congolense as the dominant species.

bioRxiv · Aug 11, 2021 · PreprintEvolutionary Biology

Cooperativity of catalytic and lectin-like domain of T. congolense trans-sialidase modulates its catalytic activity

M. Waespy, T. T. Gbem, N. Dinesh Kumar, S. Solaiyappan Mani, J. Rosenau, F. Dietz, S. Kelm

This study shows that the lectin domain of T. congolense trans-sialidase modulates its catalytic activity by favoring trans-sialylation over hydrolysis when interacting with specific carbohydrates.

bioRxiv · May 28, 2021Biochemistry