Author

H. Abou Assi

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 Biophysics· 2

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 2 Assay:DNA methylation· 2 Approach:experimental assay· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Approach:deep learning· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

H. Shi· 3 shared A. Rangadurai· 2 shared B. Liu· 2 shared H. M. Al-Hashimi· 2 shared A. L. Moye· 1 shared A. M. van Oijen· 1 shared B. P. Paudel· 1 shared C. G. Tomlinson· 1 shared

Activity by Year

2020-2020 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiophysics

H. Shi

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Author profile →

4 papers

Recent·Most cited

Measuring thermodynamic preferences to form non-native conformations in nucleic acids using melting experiments reveals a rich sequence-specific DNA conformational landscape

A. Rangadurai, H. Shi, Y. Xu, B. Liu, H. Abou Assi, J. D. Boom, H. Zhou, I. J. Kimsey, H. M. Al-Hashimi

This paper introduces delta-melt, a method using chemical modifications and melting experiments to measure thermodynamic preferences for non-native DNA conformations, revealing sequence-specific variations in conformational stability.

bioRxiv · Dec 26, 2020 · PreprintBiophysics

2'-O-methylation alters the RNA secondary structural ensemble

H. Abou Assi, H. Shi, B. Liu, M. C. Clay, K. Erharter, C. Kreutz, C. Holley, H. Al-Hashimi

This study shows that 2'-O-methylation stabilizes alternative RNA secondary structures and increases the lifetime of excited states in the HIV-1 TAR element.

bioRxiv · May 28, 2020 · PreprintBiochemistry

An RNA dynamic ensemble at atomic resolution

H. Shi, A. Rangadurai, H. Abou Assi, R. Roy, D. A. Case, D. Herschlag, J. D. Yesselman, H. M. Al-Hashimi

This study determines an atomic-resolution RNA ensemble for HIV-1 TAR using structure prediction and NMR refinement, revealing cooperative conformational changes.

bioRxiv · May 13, 2020 · PreprintBiophysics

A mechanism for the extension and unfolding of parallel telomeric G-quadruplexes by human telomerase at single-molecule resolution

B. P. Paudel, A. L. Moye, H. Abou Assi, R. El-Khoury, S. B. Cohen, M. L. Birrento, S. Samosorn, K. Intharapichai, C. G. Tomlinson, M.-P. Teulade-Fichou, C. Gonzalez, J. L. Beck, M. J. Damha, A. M. van Oijen, T. M. Bryan

This study uses single-molecule techniques to show that telomerase can extend and unfold parallel telomeric G-quadruplexes, revealing it acts as a resolvase.

bioRxiv · Feb 26, 2020Biochemistry