Author

U. S. Chio

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· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 4 Research Focus:protein structure prediction· 3 Approach:deep learning· 2 Research Focus:drug response / drug discovery· 2 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. M. Smith· 3 shared A. N. Rizo· 3 shared D. Diwanji· 3 shared G. E. Merz· 3 shared S. Pourmal· 3 shared A. F. Brilot· 2 shared C. M. Azumaya· 2 shared E. Hernandez· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiochemistry

A. M. Smith

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Author profile →

5 papers

Recent·Most cited

Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking

U. S. Chio, E. Palovcak, A. A. A. Autzen, H. E. Autzen, E. N. Munoz, Z. Yu, F. Wang, D. A. Agard, J.-P. Armache, G. Narlikar, Y. Cheng

bioRxiv · Jun 20, 2023 · PreprintBiochemistry

Cryo-EM structure of the human Sirtuin 6-nucleosome complex

U. S. Chio, O. Rechiche, A. R. Bryll, J. Zhu, J. Feldman, C. Peterson, S. Tan, J.-P. Armache

The paper presents the cryo-EM structure of the human SIRT6-nucleosome complex, revealing how SIRT6 deacetylates histone H3 K9 and K56.

bioRxiv · Mar 17, 2023Biochemistry

Computational pipeline provides mechanistic understanding of Omicron variant of concern neutralizing engineered ACE2 receptor traps

S. G. Remesh, G. E. Merz, A. F. Britol, U. S. Chio, A. N. Rizo, T. H. Pospiech, I. Lui, M. T. Laurie, J. Glasgow, C. Q. Le, Y. Zhang, D. Diwanji, E. Hernandez, J. Lopez, K. I. Pawar, , K. A. Verba

The paper develops a computational pipeline combining Rosetta and cryo-EM to analyze ACE2 receptor traps' binding to SARS-CoV-2 variants, showing high affinity and neutralization capabilities against Omicron and Delta.

bioRxiv · Aug 9, 2022Biochemistry

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics

An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation

M. Schoof, B. Faust, R. A. Saunders, S. Sangwan, V. V. Rezelj, N. Hoppe, M. Boone, C. Billesboelle, C. Puchades, C. M. Azumaya, H. T. Kratochvil, M. Zimanyi, I. Deshpande, J. Liang, S. Dickinson, , Barile-H

This paper develops a potent synthetic nanobody that neutralizes SARS-CoV-2 by locking its Spike protein in an inactive conformation, enabling aerosol delivery as a prophylactic or therapeutic agent.

bioRxiv · Aug 8, 2020Biochemistry