Author

C.-T. Zee

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:cryo-EM· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1

Frequent Co-Authors

C. Glynn· 3 shared J. A. Rodriguez· 3 shared M. Gallagher-Jones· 3 shared M. R. Sawaya· 3 shared D. Cascio· 2 shared M. D. Flores· 2 shared T. Gonen· 2 shared A. Saucedo· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiochemistry

C. Glynn

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Author profile →

5 papers

Recent·Most cited

Structure of a reversible amyloid fibril formed by the CPEB3 prion-like domain reveals a core sequence involved in translational regulation

M. D. Flores, M. R. Sawaya, D. R. Boyer, S. Zink, S. Tovmasyan, A. Saucedo, C.-T. Zee, J. Cardenas, L. Fioriti, J. A. Rodriguez

This study identifies an amyloidogenic segment in CPEB3's prion domain that is critical for its function in translational regulation and long-term memory.

bioRxiv · Dec 7, 2022 · PreprintBiochemistry

Fragment-based ab initio phasing of peptidic nanocrystals by MicroED

L. Richards, M. D. Flores, C. Millan, C.-T. Zee, C. Glynn, M. R. Sawaya, M. Gallagher-Jones, R. Borges, I. Uson, J. A. Rodriguez

This paper introduces a fragment-based method for de novo structure determination of peptidic nanocrystals using MicroED, enabling the solution of previously intractable structures.

bioRxiv · Sep 13, 2021Biochemistry

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

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

Analysis of global and site-specific radiation damage in cryo-EM

J. Hattne, D. Shi, C. Glynn, C.-T. Zee, M. Gallagher-Jones, M. Martynowycz, J. Rodriguez, T. Gonen

The paper analyzes radiation damage in cryo-EM using MicroED, finding similar damage dynamics to X-ray crystallography, including metal ion perturbation and disulfide bond breaking.

bioRxiv · Feb 1, 2018Biochemistry