Author

M. U. Fruergaard

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

J. L. Andersen· 2 shared P. Nissen· 2 shared A. Shahsavar· 1 shared A. V. Almeida· 1 shared C. J. F. Nielsen· 1 shared C. Rosada· 1 shared E. M. Quistgaard· 1 shared E. Tranchant· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

J. L. Andersen

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Author profile →

3 papers

Recent·Most cited

Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring

T. A. Gadeberg, M. H. Joergensen, H. G. Olesen, J. Lorentzen, S. L. Harwood, A. V. Almeida, M. U. Fruergaard, R. K. Jensen, P. Kanis, H. Pedersen, E. Tranchant, S. V. Petersen, I. B. Thoegersen, J. A. Lyons, J. J. Enghild, G. R. R. Andersen

This study uses cryo-EM to analyze the structural changes in C3 during hydrolysis, revealing a dynamic opening in the macroglobulin ring that allows domain translocation.

bioRxiv · Apr 15, 2024Biochemistry

Activation and inhibition of the C-terminal kinase domain of p90 ribosomal S6 kinases

M. U. Fruergaard, C. J. F. Nielsen, C. Rosada, L. Iversen, J. L. Andersen, P. Nissen

The paper characterizes the activation mechanism of the C-terminal kinase domain of RSKs and develops constitutively active variants for inhibitor testing.

bioRxiv · Feb 18, 2022Biochemistry

The beryllium fluoride form of the Na+,K+-ATPase and the intermediates of the functional cycle

M. U. Fruergaard, I. Dach, J. L. Andersen, M. Ozol, A. Shahsavar, E. M. Quistgaard, H. Poulsen, N. U. Fedosova, P. Nissen

The paper presents a crystal structure of the Na+,K+-ATPase in the E2-BeFx form, revealing structural insights into its functional cycle and ion binding mechanisms.

bioRxiv · Nov 8, 2021 · PreprintBiochemistry