Author

Katherine T. Grasso

Boston College

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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Synthetic Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:E. coli· 1 Research Focus:protein design· 1 Assay:protein structure· 1

Frequent Co-Authors

Abhishek ChatterjeeiD· 2 shared Christen M. Hillenbrand· 2 shared Megan J. R. YeoiD· 2 shared Arianna O. OsgoodiD· 1 shared Chintan SoniiD· 1 shared Elise D. FicarettaiD· 1 shared James S. ItaliaiD· 1 shared Rachel L. HuangiD· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

9 top collaborators · 27 mutual co-author links

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2 shared papersSynthetic Biology

Abhishek ChatterjeeORCID

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2 papers

Recent·Most cited

A facile platform to engineer E. coli tyrosyl-tRNA synthetase adds new chemistries to the eukaryotic genetic code, including a phosphotyrosine mimic

Katherine T. Grasso, Soumya Jyoti Singha Roy, Megan J. R. Yeo, Chintan Soni, Arianna O. Osgood, Christen M. Hillenbrand, Abhishek Chatterjee

This paper describes an engineered E. coli tyrosyl-tRNA synthetase system that enables the incorporation of new noncanonical amino acids into eukaryotic cells.

bioRxiv · Nov 28, 2021 · PreprintSynthetic Biology

Structural robustness affects the engineerability of aminoacyl-tRNA synthetases for genetic code expansion

Katherine T. Grasso, Megan J. R. Yeo, Christen M. Hillenbrand, Elise D. Ficaretta, James S. Italia, Rachel L. Huang, Abhishek Chatterjee

The paper shows that structural robustness of tyrosyl-tRNA synthetases affects their ability to be engineered for genetic code expansion, with MjTyrRS being more robust than EcTyrRS.

Biochemistry · Feb 9, 2021Peer-reviewedSynthetic Biology