Author

R. Dastvan

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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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Rasouli· 1 shared A. S. Holehouse· 1 shared B. Bothner· 1 shared E. Antony· 1 shared E. Tajkhorshid· 1 shared I. M. Ahmad· 1 shared J. B. Hopkins· 1 shared J. Deveryshetty· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiophysics

A. Rasouli

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Wrapping of single-stranded DNA by Replication Protein A and modulation through phosphorylation

R. Chadda, V. Kaushik, I. M. Ahmad, J. Deveryshetty, A. S. Holehouse, S. T. d. Sigurdsson, B. Bothner, R. Dastvan, S. S. Origanti, E. Antony

This study uses single-molecule techniques to show that RPA partially wraps ssDNA and that phosphorylation at Ser-384 modulates this wrapping.

bioRxiv · Mar 28, 2024 · PreprintBiochemistry

The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.

Y. Kyriukha, M. B. Watkins, J. M. Redington, R. Dastvan, V. N. Uversky, J. B. Hopkins, N. Pozzi, S. Korolev

This study identifies the PALB2 DNA-binding domain as an intrinsically disordered region that promotes DNA compaction through oligomerization, revealing a novel strand exchange mechanism.

bioRxiv · Jun 1, 2023Biophysics

Proton-driven alternating access in a spinster transporter, an emerging family of broad-specificity efflux pumps

R. Dastvan, A. Rasouli, S. Dehghani-Ghahnaviyeh, S. Gies, E. Tajkhorshid

This study identifies conformational states and proton-coupled dynamics of a bacterial Spns transporter, revealing its role in multidrug resistance and substrate specificity.

bioRxiv · Mar 3, 2022 · PreprintBiophysics