Author

S. McSweeney

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· 3 Biophysics· 1 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Organism:Arabidopsis· 1 Assay:ChIP-seq· 1 Assay:cryo-EM· 1

Frequent Co-Authors

J. Shanklin· 3 shared Q. Liu· 3 shared B. Andi· 2 shared C. Pang· 2 shared J. Chai· 2 shared P. Zhu· 2 shared A. Ebrahim· 1 shared A. T. Cheung· 1 shared

Activity by Year

2020-2021 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

J. Shanklin

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Author profile →

5 papers

Recent·Most cited

AlphaFold Protein Structure Database for Sequence-Independent Molecular Replacement

L. Chai, P. Zhu, J. Chai, C. Pang, B. Andi, S. McSweeney, J. Shanklin, Q. Liu

The paper tests if AlphaFold-predicted protein structures can be used for sequence-independent molecular replacement in crystallography, successfully determining two unknown contaminant structures.

bioRxiv · Sep 10, 2021Biochemistry

CREB5 reprograms nuclear interactions to promote resistance to androgen receptor targeting therapies

J. H. Hwang, R. Arafeh, J.-H. Seo, S. C. Baca, M. Ludwig, T. E. Arnoff, C. Richter, H. E. Bergom, S. McSweeney, J. P. Rennhack, S. A. Klingenberg, A. T. Cheung, J. Kwon, J. So, S. Kregel, , W. Hahn

This study identifies CREB5 as a key driver of resistance to androgen receptor targeting therapies by reprogramming nuclear interactions and activating TGFβ and Wnt signaling pathways.

bioRxiv · Aug 18, 2021Cancer Biology

The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro)

A. Ebrahim, B. T. Riley, D. Kumaran, B. Andi, M. R. Fuchs, S. McSweeney, D. A. Keedy

This study reports high-resolution crystal structures of SARS-CoV-2 Mpro at various temperatures and humidity, revealing temperature-dependent conformational changes and structural features relevant to antiviral drug development.

bioRxiv · May 3, 2021Biophysics

Structural Basis for SARS-CoV-2 Envelope Protein in Recognition of Human Cell Junction Protein PALS1

J. Chai, Y. Cai, C. Pang, L. Wang, S. McSweeney, J. Shanklin, Q. Liu

The paper determines the structure of the SARS-CoV-2 E protein-PALS1 complex using cryo-EM, revealing a hydrophobic interaction that explains viral spread and suggesting therapeutic targets.

bioRxiv · Feb 22, 2021Biochemistry

Structural Basis for Ca2+-Dependent Activation of a Plant Metacaspase

P. Zhu, X.-H. Yu, C. Wang, Q. Zhang, W. Liu, S. McSweeney, J. Shanklin, E. Lam, Q. Liu

This study determines the crystal structure of AtMC4, revealing how Ca2+ activates plant metacaspase through linker domain cleavage and substrate access.

bioRxiv · Mar 9, 2020Biochemistry