Author

E. G. Kuiper

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

G. L. Conn· 3 shared D. Dey· 2 shared A. Krishnamohan· 1 shared C. B. Edgington· 1 shared C. J. Hancock· 1 shared C. M. Dunham· 1 shared H. A. Nguyen· 1 shared H. Kim· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

G. L. Conn

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

tRNA m1G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10

S. E. Strassler, I. E. Bowles, A. Krishnamohan, H. Kim, C. B. Edgington, E. G. Kuiper, C. J. Hancock, L. Comstock, J. E. Jackman, G. L. Conn

This study identifies that Trm10 substrate recognition depends on tRNA conformational changes induced by the enzyme, revealing a novel mechanism for tRNA modification.

bioRxiv · Feb 1, 2023Biochemistry

50S subunit recognition and modification by the Mycobacterium tuberculosis ribosomal RNA methyltransferase TlyA

Z. T. Laughlin, S. Nandi, D. Dey, N. Zelinskaya, M. A. Witek, P. Srinivas, H. A. Nguyen, E. G. Kuiper, L. R. Comstock, C. M. Dunham, G. L. Conn

This paper reports the structure of the Mycobacterium tuberculosis TlyA enzyme bound to the 50S ribosomal subunit, revealing mechanisms of rRNA substrate recognition and modification that contribute to antibiotic resistance.

bioRxiv · Nov 11, 2021Biochemistry

Substrate recognition by the Pseudomonas aeruginosa EF-Tu methyltransferase EftM

E. G. Kuiper, D. Dey, P. A. LaMore, J. P. Owings, S. M. Prezioso, J. B. Goldberg, G. L. Conn

This study defines the molecular mechanism of EF-Tu substrate recognition by the Pseudomonas aeruginosa methyltransferase EftM through computational modeling and experimental validation.

bioRxiv · Sep 23, 2019Biochemistry