Publications:
Das, S., Dunnett, L., Fisher, H., Venditti, V., & Prischi, F. (2026). Phosphorylation-dependent remodeling of the XIAP IRES by hnRNPA1.
Using BNMRF
1 Research Group
Das, S., Dunnett, L., Fisher, H., Venditti, V., & Prischi, F. (2026). Phosphorylation-dependent remodeling of the XIAP IRES by hnRNPA1.
Using BNMRF
3 Research Groups
Singh, A., Pettini, F., Gianibbi, B., Das, S., Barisani, D., Purslow, J. A., ... & Venditti, V. (2025). Structure-based discovery of a non-competitive FTO inhibitor bound to a cryptic site at the domain interface. Journal of Molecular Biology, 169575. https://doi.org/10.1016/j.jmb.2025.169575
Faal, B., Purslow, J. A., & Venditti, V. (2025). 1H, 15N, 13C backbone resonance assignment of human Alkbh7. Biomolecular NMR assignments, 19(1), 65-69. https://doi.org/10.1007/s12104-025-10219-4
O'Brien, E. A., Abbasi, M., Purslow, J. A., & VanVeller, B. (2025). The ‘ins’ and ‘outs’ of amidines in β-sheet folding and fibril disaggregation. Chemical Science, 16(36), 16970-16978. https://doi.org/10.1039/D5SC05902J
Siang, S., Patel, U., Chaves-Mejía, M., Purslow, J. A., Potoyan, D., & Roche, J. (2025). Fine-Tuning of ATF4 DNA Binding Activity by a Secondary Basic Motif Unique to the ATF-X Subfamily of bZip Transcription Factors. Biochemistry, 64(6), 1257-1265. https://doi.org/10.1021/acs.biochem.4c00640
Using BNMRF
3 Research Groups
Joseph, R. E., Wales, T. E., Jayne, S., Britton, R. G., Fulton, D. B., Engen, J. R., ... & Andreotti, A. H. (2024). Impact of the clinically approved BTK inhibitors on the conformation of full-length BTK and analysis of the development of BTK resistance mutations in chronic lymphocytic leukemia. Elife, 13, RP95488. https://doi.org/10.7554/elife.95488
Sedinkin, S. L., Roche, J., & Venditti, V. (2024). Elucidation of the Mechanisms of Inter-domain Coupling in the Monomeric State of Enzyme I by High-pressure NMR. Journal of molecular biology, 436(9), 168553. https://doi.org/10.1016/j.jmb.2024.168553
Levengood, J. D., Potoyan, D., Penumutchu, S., Kumar, A., Zhou, Q., Wang, Y., ... & Tolbert, B. S. (2024). Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Science Advances, 10(28), eadk6580. https://doi.org/10.1126/sciadv.adk6580
Burns, D., Khatiwada, B., Singh, A., Purslow, J. A., Potoyan, D. A., & Venditti, V. (2024). An α-ketoglutarate conformational switch controls iron accessibility, activation, and substrate selection of the human FTO protein. Proceedings of the National Academy of Sciences, 121(25), e2404457121. https://doi.org/10.1073/pnas.240445712
Using BNMRF
4 Research Groups
Daniel A Kramer, Heidy Y Narvaez-Ortiz, Urval Patel, Rebecca Shi, Kang Shen, Brad J Nolen, Julien Roche, & Baoyu Chen (2023). The intrinsically disordered cytoplasmic tail of a dendrite branching receptor uses two distinct mechanisms to regulate the actin cytoskeleton. eLife, 12:e88492. https://doi.org/10.7554/eLife.88492 (PDF)
An, Y., Chatterjee, P., Naik, P., Banerjee, S., Huang, W., Slowing, I. I., & Venditti, V. (2023). Hydrogen spillover and substrate-support hydrogen bonding mediate hydrogenation of phenol catalyzed by palladium on reducible metal oxides. Chemical science, 14(48), 14166–14175. https://doi.org/10.1039/d3sc02913a (PDF)
Sergey L. Sedinkin, Daniel Burns, Divyanshu Shukla, Davit A. Potoyan, & Vincenzo Venditti. (2023). Solution Structure Ensembles of the Open and Closed Forms of the ∼130 kDa Enzyme I via AlphaFold Modeling, Coarse Grained Simulations, and NMR. Journal of the American Chemical Society, 145 (24), 13347-13356. https:\\doi.org/10.1021/jacs.3c03425 (PDF)
Singh, A., Burns, D., Sedinkin, S. L., Van Veller, B., Potoyan, D. A., & Venditti, V. (2023). Protein Conformational Dynamics Underlie Selective Recognition of Thermophilic over Mesophilic Enzyme I by a Substrate Analogue. Biomolecules, 13(1), 160. https://doi.org/10.3390/biom13010160 (PDF)
Raji E. Joseph, Thomas E. Wales, Sandrine Jayne, Robert G. Britton, D. Bruce Fulton, John R. Engen, Martin J. S. Dyer, & Amy H. Andreotti. (2023). Impact of the clinically approved BTK inhibitors on the conformation of full-length BTK and analysis of the development of BTK resistance mutations in chronic lymphocytic leukemia. bioRxiv, 12.18.572223. https://doi.org/10.1101/2023.12.18.572223 (PDF)
Lowe, J., Joseph, R., Venditti, V., Fulton, D., & Andreotti, A. (2023). Employing Solution NMR to Study BTK Activation Through Sortase-Mediated Ligation and Paramagnetic Relaxation Enhancement. Journal of Biological Chemistry, 299(3), S593.
Zhao, L., Oyagbenro, R., Feng, Y., Xu, M., & Peters. RJ. (2023). Oryzalexin S biosynthesis: a cross-stitched disappearing pathway. aBIOTECH, 4, 1–7. https://doi.org/10.1007/s42994-022-00092-3 (PDF)