Dorte Frees
Associate Professor
1 - 3 out of 3Page size: 50
- 2021
- Published
A Staphylococcus aureus clpX Mutant Used as a Unique Screening Tool to Identify Cell Wall Synthesis Inhibitors that Reverse β-Lactam Resistance in MRSA
Bæk, K. T., Jensen, C., Farha, M. A., Nielsen, T. K., Paknejadi, E., Mebus, Viktor Hundtofte, Vestergaard, M., Brown, E. D. & Frees, Dorte, 2021, In: Frontiers in Molecular Biosciences. 8, 691569.Research output: Contribution to journal › Journal article › Research › peer-review
- Published
Cefoxitin treatment of MRSA leads to a shift in the IL-12/IL-23 production pattern in dendritic cells by a mechanism involving changes in the MAPK signaling
Eld, H. M. S., Nielsen, E. M., Johnsen, Peter Riber, Marengo, M., Kamper, I. W., Frederiksen, L., Bonomi, F., Frees, Dorte, Iametti, S. & Frøkiær, Hanne, 2021, In: Molecular Immunology. 134, p. 1-12 12 p.Research output: Contribution to journal › Journal article › Research › peer-review
- Published
Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase
Alqarzaee, A. A., Chaudhari, S. S., Islam, M. M., Kumar, V., Zimmerman, M. C., Saha, R., Bayles, K. W., Frees, Dorte & Thomas, V. C., 2021, In: Proceedings of the National Academy of Sciences of the United States of America. 118, 47, e2109671118.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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281
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The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus
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