Author

M. Vistrup-Parry

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· 2

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Assay:protein structure· 2 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

K. Stromgaard· 2 shared A. T. Soerensen· 1 shared C. Bartling· 1 shared C. Ma· 1 shared C. P. Pedersen· 1 shared D. E. Otzen· 1 shared J. N. Pedersen· 1 shared K. L. Madsen· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersBiochemistry

K. Stromgaard

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2 papers

Recent·Most cited

Bi-directional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners

N. R. Christensen, C. P. Pedersen, V. Sereikaite, J. N. Pedersen, M. Vistrup-Parry, A. T. Soerensen, D. E. Otzen, L. Arleth, K. Teilum, K. L. Madsen, K. Stromgaard

This study identifies the minimal peptide responsible for stargazin-mediated LLPS of PSD-95 and shows that pharmacological inhibitors can promote LLPS formation.

bioRxiv · Mar 3, 2021Biochemistry

Site-specific phosphorylation of PSD-95 dynamically regulates the post-synaptic density as observed by phase separation

M. Vistrup-Parry, X. Chen, T. Johansen, S. Bach, S. Buch-Larsen, C. Bartling, C. Ma, L. Clemmensen, M. L. Nielsen, M. Zhang, K. Stromgaard

The paper introduces site-specific phosphorylations in PSD-95 and shows how they affect phase separation with interaction partners, revealing opposing effects on condensate formation.

bioRxiv · Mar 3, 2021 · PreprintBiochemistry