Author

S. Rawson

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· 6 Pharmacology & Toxicology· 2 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Assay:cryo-EM· 6 Organism:human· 6 Research Focus:host-pathogen & immune response· 4 Research Focus:protein folding & dynamics· 3 Research Focus:protein structure prediction· 3 Approach:biophysical modeling· 2 Organism:virus· 2

Frequent Co-Authors

R. M. Walsh· 3 shared A. C. Kruse· 2 shared B. Chen· 2 shared H. Peng· 2 shared J. Zhang· 2 shared S. M. Sterling· 2 shared S. Rits-Volloch· 2 shared T. Xiao· 2 shared

Activity by Year

2019-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

R. M. Walsh

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10 papers

Recent·Most cited

Visualizing chaperone-mediated multistep assembly of the human 20S proteasome

F. Adolf, J. Du, E. A. Goodall, R. M. Walsh, S. rawson, S. von Gronaua, J. W. Harper, J. Hanna, B. A. Schulman

The paper uses cryo-EM to visualize the assembly of the human 20S proteasome, revealing how chaperones and propeptides guide subunit incorporation and proteasome activation.

bioRxiv · Jan 27, 2024Biochemistry

Molecular Mechanism of PP2A/B55α Phosphatase Inhibition by IER5

R. Cao, D. T. Jones, L. Pan, S. Wang, S. K. R. Padi, S. Rawson, J. C. Aster, S. C. Blacklow

This study determines the structure of PP2A/B55 inhibited by IER5-N50 and shows its role in suppressing pTau dephosphorylation and KRT1 expression.

bioRxiv · Aug 29, 2023Biochemistry

Antibodies Expand the Scope of Angiotensin Receptor Pharmacology

M. A. Skiba, S. M. Sterling, S. Rawson, M. S. A. Gilman, H. Xu, G. R. Nemeth, J. D. Hurley, P. Shen, D. P. Staus, J. Kim, C. McMahon, M. K. Lehtinen, L. M. Wingler, A. C. Kruse

This study develops nanobody antagonists against the AT1R receptor, showing they can selectively bind and modulate the receptor with tunable ligand selectivity.

bioRxiv · Aug 23, 2023Pharmacology & Toxicology

Cryo-EM structure of the RADAR supramolecular anti-phage defense complex

B. Duncan-Lowey, N. Tal, A. G. Johnson, S. Rawson, M. L. Mayer, S. Doron, A. Millman, S. Melamed, T. Fedorenko, A. Kacen, G. Amitai, R. Sorek, P. J. Kranzusch

The paper determines the cryo-EM structure of the RADAR complex, showing RdrB targets mononucleotides and catalyzes ATP-to-ITP conversion to limit phage replication.

Cell · Mar 1, 2023Peer-reviewedBiochemistry

Cryo-EM structure of a RAS/RAF recruitment complex

M. J. Eck, H. Jeon, E. Park, S. Rawson, A. Schmoker, B.-W. Kim, S. Oh, K. Song

The paper presents cryo-EM structures of a KRAS/BRAF/MEK1/14-3-3 complex, showing KRAS binding to BRAF's Ras-binding domain without activating it, suggesting stabilization of a pre-activation intermediate as a therapeutic target.

bioRxiv · Jul 14, 2022Biochemistry

The relaxin receptor RXFP1 signals through a mechanism of autoinhibition

S. C. Erlandson, S. Rawson, J. Osei-Owusu, K. P. Brock, X. Liu, J. A. Paulo, J. Mintseris, S. P. Gygi, D. S. Marks, X. Cong, A. C. Kruse

This study determines the cryo-EM structure of active-state RXFP1 bound to relaxin-2 and Gs protein, revealing an autoinhibition mechanism.

bioRxiv · Jan 22, 2022 · PreprintPharmacology & Toxicology

Full-length NLRP3 forms oligomeric cages to mediate NLRP3 sensing and activation

L. Andreeva, L. David, S. Rawson, C. Shen, T. Pasricha, P. Pelegrin, H. Wu

This study identifies full-length NLRP3 as a membrane-localized oligomeric cage that senses stimuli and activates the inflammasome, distinct from other monomeric inflammasome sensors.

bioRxiv · Sep 12, 2021Immunology

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

Y. Cai, J. Zhang, T. Xiao, C. L. Lavine, S. Rawson, H. Peng, H. Zhu, K. Anand, P. Tong, A. Gautam, S. Lu, S. Sterling, R. M. Walsh, S. Rits-Volloch, J. Lu, , B. Chen

This study reports cryo-EM structures of SARS-CoV-2 variants B.1.1.7 and B.1.351, revealing mutations that enhance infectivity and immune evasion.

bioRxiv · Apr 13, 2021Biochemistry

Distinct conformational states of SARS-CoV-2 spike protein

Y. Cai, J. Zhang, T. Xiao, H. Peng, S. M. Sterling, R. M. Walsh, S. Rawson, S. Rits-Volloch, B. Chen

The paper reports two cryo-EM structures of the SARS-CoV-2 spike protein, showing prefusion and postfusion conformations, and discusses their implications for viral entry and immune evasion.

bioRxiv · May 16, 2020Biochemistry

Dynamic oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

M. Madej, J. White, Z. Nowakowska, S. Rawson, C. Scavenius, J. Enghild, G. Bereta, K. Pothula, U. Kleinekathoefer, A. Basle, N. Ranson, J. Potempa, B. van den Berg

This study identifies RagAB as the oligopeptide transporter in P. gingivalis, revealing its structure and mechanism for nutrient uptake from the extracellular environment.

bioRxiv · Sep 4, 2019Microbiology