Author

M. B. Borgia

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 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

T. Mittag· 2 shared A. Borgia· 1 shared A. Bremer· 1 shared A. E. Posey· 1 shared A. Sottini· 1 shared B. Fierz· 1 shared B. Schuler· 1 shared D. Mercadante· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiophysics

T. Mittag

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3 papers

Recent·Most cited

Reduction of oligomer size modulates the competition between cluster formation and phase separation of the tumor suppressor SPOP

N. Sabri, M. J. Cuneo, M. R. Marzahn, J. Lee, J. J. Bouchard, S. Vaithiyalingam, M. B. Borgia, J. D. Schmit, T. Mittag

This study shows that reducing SPOP oligomer size shifts its function from cluster formation to phase separation, enhancing ubiquitination activity and providing insights into separation-of-function mutations.

bioRxiv · Feb 11, 2023Biophysics

Quantifying coexistence concentrations in multi-component phase-separating systems using analytical HPLC

A. Bremer, A. E. Posey, M. B. Borgia, W. M. Borcherds, M. Farag, R. V. Pappu, T. Mittag

This paper develops an analytical HPLC method to quantify coexisting phase concentrations in multi-component phase-separating systems, enabling reconstruction of coexistence curves.

bioRxiv · Sep 11, 2022Biophysics

Disordered Proteins Enable Histone Chaperoning on the Nucleosome

P. O. Heidarsson, D. Mercadante, A. Sottini, D. Nettels, M. B. Borgia, A. Borgia, S. Kilic, B. Fierz, R. B. Best, B. Schuler

The paper shows that disordered regions in proteins like H1 enable competitive displacement by histone chaperones such as prothymosin on the nucleosome.

bioRxiv · Apr 17, 2020Biophysics