Dorte Frees
Associate Professor
1 - 5 out of 5Page size: 25
- 2019
- Published
Staphylococcus aureus ClpX localizes at the division septum and impacts transcription of genes involved in cell division, T7-secretion, and SaPI5-excision
Jensen, C., Fosberg, M. J., Thalsø-Madsen, I., Bæk, K. T. & Frees, Dorte, 2019, In: Scientific Reports. 9, 11 p., 16456.Research output: Contribution to journal › Journal article › Research › peer-review
- Published
Antibiotic Resistance and the MRSA Problem
Vestergaard, M., Frees, Dorte & Ingmer, Hanne, 2019, In: Microbiology Spectrum. 7, 2, 23 p.Research output: Contribution to journal › Journal article › Research › peer-review
- Published
Fødevaresikkerhed i udvikling
Ingmer, Hanne, Larsen, M. H., Leisner, Jørgen, Frees, Dorte, Brøndsted, Lone & Dalsgaard, Anders, 2019, In: Dansk Veterinaertidsskrift. 2019, 7, p. 10-13Research output: Contribution to journal › Journal article › Communication
- Published
SosA inhibits cell division in Staphylococcus aureus in response to DNA damage
Bojer, Martin Saxtorph, Wacnik, K., Kjelgaard, P., Gallay, C., Bottomley, A. L., Cohn, M. T., Lindahl, G., Frees, Dorte, Veening, J. W., Foster, S. J. & Ingmer, Hanne, 2019, In: Molecular Microbiology. 112, 4, p. 1116-1130Research output: Contribution to journal › Journal article › Research › peer-review
- Published
The ClpX chaperone controls autolytic splitting of Staphylococcus aureus daughter cells, but is bypassed by β-lactam antibiotics or inhibitors of WTA biosynthesis
Jensen, C., Bæk, K. T., Gallay, C., Thalsø-Madsen, I., Xu, Lijuan, Jousselin, A., Ruiz Torrubia, F., Paulander, W., Pereira, A. R., Veening, J. W., Pinho, M. G. & Frees, Dorte, 2019, In: PLOS Pathogens. 15, 9, 27 p., e1008044.Research output: Contribution to journal › Journal article › Research › peer-review
ID: 4233088
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Planktonic aggregates of Staphylococcus aureus protect against common antibiotics
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The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by rot dependent and independent pathways
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The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus
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