Author

K. Bugge

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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Biophysics· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Assay:protein structure· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

B. B. Kragelund· 3 shared K. Lindorff-Larsen· 2 shared L. Arleth· 2 shared R. Araya-Secchi· 2 shared A. Barclay· 1 shared A. D. Due· 1 shared A. J. Lenard· 1 shared A. Khondker· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiophysics

B. B. Kragelund

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3 papers

Recent·Most cited

The importance of stereochemistry in the disorder-order continuum of protein-protein interactions

E. A. Newcombe, A. D. Due, A. Sottini, C. B. Fernandes, L. Staby, E. Delaforge, C. R. O. Bartling, I. Brakti, K. Bugge, B. Schuler, K. Skriver, J. G. Olsen, B. B. Kragelund

The paper investigates the role of stereochemistry in disordered protein-protein interactions, finding that chirality is inconsequential in fully disordered complexes but essential when folding and binding are coupled.

bioRxiv · Feb 23, 2024 · PreprintBiophysics

The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate

R. Araya-Secchi, K. Bugge, P. Seiffert, A. Petry, G. W. Haxholm, K. Lindorff-Larsen, S. F. Pedersen, L. Arleth, B. B. Kragelund

This study shows that the prolactin receptor forms a co-structure with JAK2 and PI(4,5)P2, enabling signal transduction by stabilizing the receptor's disordered domain.

bioRxiv · Nov 23, 2022Biophysics

Order and disorder - an integrative structure of the full-length human growth hormone receptor

N. Kassem, R. Araya-Secchi, K. Bugge, A. Barclay, H. Steinocher, A. Khondker, A. J. Lenard, J. Bürck, A. S. Ulrich, M. C. Pedersen, Y. Wang, M. C. Rheinstädter, P. A. Pedersen, K. Lindorff-Larsen, L. Arleth, B. B. Kragelund

This study determines the structure of the full-length human growth hormone receptor using integrated SAXS, X-ray diffraction, NMR, and molecular dynamics simulations, revealing a flexible ensemble of domains.

bioRxiv · Jun 25, 2020Biophysics