Author

S. Griner

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:virus· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1

Frequent Co-Authors

E. Tayeb-Fligelman· 2 shared F. Guo· 2 shared J. T. Bowler· 2 shared L. Salwinski· 2 shared P. M. Seidler· 2 shared R. Abskharon· 2 shared X. Cheng· 2 shared Y. X. Jiang· 2 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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2 shared papersBiochemistry

E. Tayeb-Fligelman

Mutual co-authors in cluster

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2 papers

Recent·Most cited

The SARS-CoV-2 nucleocapsid protein preferentially binds long and structured RNAs

C. E. Tai, E. Tayeb-Fligelman, S. Griner, L. Salwinski, J. T. Bowler, R. Abskharon, X. Cheng, P. M. Seidler, Y. X. Jiang, D. S. Eisenberg, F. Guo

This study investigates how SARS-CoV-2 nucleocapsid protein binds RNA, finding it preferentially interacts with structured and long RNAs, and proposes a mechanism linking packaging to RNA recognition.

bioRxiv · Dec 25, 2021 · PreprintBiochemistry

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