Author

R. K. Flygaard

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Approach:statistical model· 3 Assay:cryo-EM· 2 Organism:human· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

A. Amunts· 2 shared A. Barrientos· 1 shared A. Hassan· 1 shared A. Marechal· 1 shared A. Muhleip· 1 shared A. Naschberger· 1 shared B. K. Hansen· 1 shared C. K. Larsen· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiochemistry

A. Amunts

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Author profile →

4 papers

Recent·Most cited

Structure of mitoribosome reveals mechanism of mRNA binding, tRNA interactions with L1 stalk, roles of cofactors and rRNA modifications

V. Singh, Y. Itoh, S. Del'Olio, A. Hassan, A. Naschberger, R. K. Flygaard, Y. Nobe, K. Izumikawa, S. Aibara, J. Andrell, P. Whitford, A. Barrientos, M. Taoka, A. Amunts

The paper presents a high-resolution structure of the human mitoribosome, revealing mechanisms of mRNA binding, tRNA interactions, and roles of cofactors and rRNA modifications.

bioRxiv · May 24, 2023 · PreprintBiochemistry

Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplex

A. Muhleip, R. K. Flygaard, O. Haapanen, R. Baradaran, T. Gruhl, V. Tobiasson, A. Marechal, V. Sharma, A. Amunts

The paper reveals the structural basis of mitochondrial membrane bending by the I-II-III2-IV2 supercomplex using cryo-EM and molecular dynamics simulations.

bioRxiv · Jun 26, 2022 · PreprintBiochemistry

Cryo-EM structure of the human NKCC1 transporter reveals mechanisms of ion coupling and specificity

C. M. T. Neumann, L. L. Rosenbaek, R. K. Flygaard, M. Habeck, J. L. Karlsen, Y. Wang, K. Lindorff-Larsen, H. H. Gad, R. Hartmann, J. Lyons, R. A. Fenton, P. Nissen

The paper presents a cryo-EM structure of human NKCC1, revealing ion binding sites and mechanisms of ion coupling and specificity.

bioRxiv · Nov 11, 2021Biochemistry

Structure and function of the bacterial protein toxin phenomycin

B. K. Hansen, C. K. Larsen, J. T. Nielsen, E. B. Svenningsen, L. B. Van, K. M. Jacobsen, M. Bjerring, R. K. Flygaard, L. B. Jenner, L. N. Nejsum, D. E. Brodersen, F. A. A. Mulder, T. Toerring, T. B. Poulsen

This study investigates phenomycin's mechanism of toxicity, showing it inhibits translation initiation, requires endosomal escape for toxicity, and identifies a critical structural loop for its activity.

bioRxiv · Nov 29, 2019Cell Biology