Author

D. Cascio

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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Approach:experimental assay· 5 Assay:cryo-EM· 3 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

M. R. Sawaya· 4 shared C.-T. Zee· 2 shared R. Abskharon· 2 shared B. A. Nguyen· 1 shared C. G. Santiago· 1 shared C. Glynn· 1 shared C. Phillips· 1 shared C. Tai· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersBiochemistry

M. R. Sawaya

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Author profile →

5 papers

Recent·Most cited

Rigidified Scaffolds for 3-Angstrom Resolution Cryo-EM of Small Therapeutic Protein Targets

R. Castells-Graells, K. Meador, M. A. Arbing, M. R. Sawaya, M. Gee, D. Cascio, E. S. Gleave, J. E. Debreczeni, J. Breed, C. Phillips, T. O. Yeates

This paper demonstrates that rigidified scaffolds enable 3-angstrom resolution cryo-EM for small therapeutic proteins like KRAS, overcoming size limitations in structural characterization.

bioRxiv · Sep 18, 2022Biochemistry

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

R. Abskharon, M. R. Sawaya, D. R. Boyer, Q. Cao, B. A. Nguyen, D. Cascio, D. S. Eisenberg

The paper presents a cryo-EM structure of RNA-bound tau fibrils, revealing a small C-terminal core that may nucleate fibril formation and is essential for fibril integrity.

bioRxiv · Jan 28, 2022Biophysics

Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2

E. Tayeb-Fligelman, X. Cheng, C. Tai, J. T. Bowler, S. Griner, M. R. Sawaya, P. M. Seidler, Y. X. Jiang, J. Lu, G. M. Rosenberg, L. Salwinski, R. Abskharon, C.-T. Zee, K. Hou, Y. Li, , D. Eisenberg

The paper identifies amyloid-forming segments in SARS-CoV-2 Nucleoprotein and designs peptide inhibitors based on their atomic structures to target Covid-19.

bioRxiv · Mar 5, 2021 · PreprintBiochemistry

Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria

M. D. Kattke, J. E. Gosschalk, O. E. Martinez, G. Kumar, R. T. Gale, D. Cascio, M. R. Sawaya, M. Phillips, E. Brown, R. T. Clubb

This paper determines the structure of TagA, a glycosyltransferase involved in wall teichoic acid biosynthesis, and reveals its mechanism of catalysis and regulation by membrane interactions.

bioRxiv · Dec 28, 2018Biochemistry

Homochiral and racemic MicroED structures of a peptide from the ice nucleation protein InaZ

C.-T. Zee, C. Glynn, M. Gallagher-Jones, J. Miao, C. G. Santiago, D. Cascio, T. Gonen, M. Sawaya, J. A. Rodriguez

The paper determines homochiral and racemic structures of a peptide from InaZ using MicroED, revealing amyloid-like protofibrils with distinct chiral arrangements.

bioRxiv · Nov 19, 2018Biochemistry