Author

U. Schulze-Gahmen

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 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:protein structure prediction· 2 Organism:virus· 2 Research Focus:cell-cell communication· 1 Approach:deep learning· 1

Frequent Co-Authors

G. E. Merz· 2 shared G. M. Jang· 2 shared H. T. Kratochvil· 2 shared I. D. Young· 2 shared J. K. Peters· 2 shared M. Moritz· 2 shared M. Ott· 2 shared N. Herrera· 2 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersBiophysics

G. E. Merz

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Regulation of virion production by the ORF8 signal peptide across SARS-CoV-2 variants

M. M. Khalid, I. Chen, F. S. Soveg, T. Y. Taha, T. Tabata, R. Suryawanshi, A. M. Syed, A. Ciling, M. McCavitt-Malvido, U. Schulze-Gahmen, J. Hayashi, I.-J. Kim, S. W. Fong, J. Batra, G. R. Kumar, , M. Ott

This study shows ORF8 suppresses viral particle production by interacting with Spike and causing Golgi fragmentation, supporting evolutionary pressure to delete ORF8 in SARS-CoV-2 variants.

bioRxiv · Mar 5, 2024 · PreprintMicrobiology

RNA conformational propensities determine cellular activity

M. L. Kelly, R. Roy, A. Geng, L. R. Ganser, A. Manghrani, B. R. Cullen, U. Schulze-Gahmen, D. Herschlag, H. M. Al-Hashimi

The paper alters and measures conformational propensities of HIV-1 TAR RNA to predict binding affinities and cellular activity.

bioRxiv · Dec 5, 2022 · PreprintBiophysics

Structure-function analysis of enterovirus protease 2A in complex with its essential host factor SETD3

C. E. Peters, U. Schulze-Gahmen, M. Eckhardt, G. M. Jang, J. Xu, E. H. Pulido, M. Ott, O. Gozani, K. A. Verba, R. Hüttenhain, J. Carette, N. J. Krogan

The paper reports the cryo-EM structure of SETD3 interacting with enterovirus protease 2A and shows that mutations in the SET domain reduce binding and protect against infection.

bioRxiv · Jun 22, 2022Biophysics

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

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry