Author

T. P. Dao

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· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:statistical model· 1

Frequent Co-Authors

C. A. Castaneda· 5 shared S. K. K. Galagedera· 3 shared A. Chaudhuri· 1 shared A. M. Lehman· 1 shared A. Rajendran· 1 shared C. G. Robb· 1 shared D. A. Kraut· 1 shared E. L. Mallon· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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5 shared papersBiophysics

C. A. Castaneda

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Author profile →

5 papers

Recent·Most cited

Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate

I. M. Valentino, J. G. Llivicota-Guaman, T. P. Dao, E. O. Mulvey, A. M. Lehman, S. K. K. Galagedera, E. L. Mallon, C. A. Castaneda, D. A. Kraut

This study shows that polyubiquitinated substrates modulate UBQLN2 phase separation in a linkage-dependent manner, affecting proteasome activity and deubiquitination.

bioRxiv · Mar 15, 2024Biochemistry

Short N-terminal disordered regions and the proline-rich domain are major regulators of phase transitions for full-length UBQLN1, UBQLN2 and UBQLN4

T. P. Dao, A. Rajendran, S. K. K. Galagedera, W. Haws, C. A. Castaneda

This study shows that the N-terminal disordered regions and proline-rich domain regulate phase separation in UBQLN1, UBQLN2, and UBQLN4, with distinct temperature dependencies.

bioRxiv · Sep 27, 2023Biophysics

Decoding optimal ligand design for multicomponent condensates

S. K. K. Galagedera, T. P. Dao, S. E. Enos, A. Chaudhuri, J. D. Schmit, C. A. Castaneda

This study identifies optimal polyubiquitin ligand architectures that promote UBQLN2 phase separation by analyzing the energetic penalties and spatial configurations of Ub units.

bioRxiv · Mar 13, 2023Biophysics

Ion mobility mass spectrometry unveils global protein conformations in response to conditions that promote and reverse liquid-liquid phase separation

C. G. Robb, T. P. Dao, J. Ujma, C. A. Castaneda, R. Beveridge

This study uses ion mobility mass spectrometry to analyze how protein conformations change during and reverse liquid-liquid phase separation.

bioRxiv · Dec 21, 2022Biophysics

Mechanistic insights into the enhancement or inhibition of phase separation by polyubiquitin chains of different lengths or linkages

T. P. Dao, Y. Yang, M. F. Presti, M. S. Cosgrove, J. B. Hopkins, W. Ma, S. N. Loh, C. A. Castaneda

This study investigates how different polyubiquitin chain lengths and linkages affect UBQLN2's liquid-liquid phase separation, showing that extended chains enhance while compact chains inhibit it.

bioRxiv · Nov 12, 2021Biophysics