Author

M. Dyla

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Approach:experimental assay· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

M. Kjaergaard· 3 shared C. M. T. Neumann· 1 shared D. E. Otzen· 1 shared E. Meldgaard Hogh Quistgaard· 1 shared J. Lauwring Andersen· 1 shared N. S. Gonzalez Foutel· 1 shared P. Nissen· 1 shared S. Basse Hansen· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

8 top collaborators · 18 mutual co-author links

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3 shared papersBiophysics

M. Kjaergaard

Mutual co-authors in cluster

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3 papers

Recent·Most cited

The optimal docking strength for reversibly tethered kinases

M. Dyla, N. S. Gonzalez Foutel, D. E. Otzen, M. Kjaergaard

This study determines the optimal docking strength for kinases to enhance phosphorylation rates under specific conditions.

bioRxiv · Feb 7, 2022Biophysics

The crystal structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation

S. Basse Hansen, M. Dyla, C. M. T. Neumann, E. Meldgaard Hogh Quistgaard, J. Lauwring Andersen, M. Kjaergaard, P. Nissen

The paper presents crystal structures of LMCA1, revealing its primed state for dephosphorylation and a single Ca2+-binding site, with insights into its transport mechanism.

bioRxiv · Jun 23, 2020Biochemistry

Intrinsically disordered linkers control tethered kinases via effective concentration

M. Dyla, M. Kjaergaard

This study shows that phosphorylation kinetics of tethered kinases depend on the length of intrinsically disordered linkers and substrate-specific scaling.

bioRxiv · Apr 4, 2020Biophysics