Author

T. Nyalile

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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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Approach:genetic perturbation / CRISPR· 1 Assay:proteomics· 1 Assay:structural biology· 1 Organism:virus· 1

Frequent Co-Authors

J. Luban· 3 shared A. Dauphin· 2 shared K. Shen· 2 shared L. Yurkovetskiy· 2 shared A. Barve· 1 shared A. Baum· 1 shared A. Rafique· 1 shared A. T. Joynt· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersMicrobiology

J. Luban

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Addressing the dNTP bottleneck restricting prime editing activity

K. Ponnienselvan, P. Liu, T. Nyalile, S. Oikemus, A. T. Joynt, K. Kelly, D. Guo, Z. Chen, J. M. Lee, C. A. Schiffer, C. P. Emerson, N. D. Lawson, J. K. Watts, E. J. Sontheimer, J. Luban, S. A. Wolfe

This study identifies mutations to improve prime editing efficiency in low-dNTP environments by enhancing MMLV-reverse transcriptase and reducing SAMHD1 activity.

bioRxiv · Oct 21, 2023Biochemistry

S:D614G and S:H655Y are gateway mutations that act epistatically to promote SARS-CoV-2 variant fitness

L. Yurkovetskiy, S. Egri, C. Kurhade, M. A. Diaz-Salinas, J. A. Jaimes, T. Nyalile, X. Xie, M. C. Choudhary, A. Dauphin, J. Z. Li, J. B. Munro, P.-Y. Shi, K. Shen, J. Luban

This study shows that S:D614G and S:H655Y mutations enhance SARS-CoV-2 infectivity by stabilizing the Spike protein in an open RBD conformation, acting epistatically with the polybasic S1/S2 cleavage site.

bioRxiv · Mar 30, 2023 · PreprintMicrobiology

Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant

L. Yurkovetskiy, X. Wang, K. E. Pascal, C. Tompkins-Tinch, T. Nyalile, Y. Wang, A. Baum, W. E. Diehl, A. Dauphin, C. Carbone, K. Veinotte, S. B. Egri, S. F. Schaffner, J. E. Lemieux, J. Munro, , J. Luban

This study shows the D614G SARS-CoV-2 spike protein variant is more infectious but has reduced ACE2 affinity and altered trimer conformation, affecting viral entry and antibody neutralization.

bioRxiv · Jul 4, 2020Microbiology