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Your search keyword '"Owens, Dominic D. G."' showing total 9 results
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9 results on '"Owens, Dominic D. G."'

1. Recruitment of FBXO22 for targeted degradation of NSD2

Author

Nie, David Y., Tabor, John R., Li, Jianping, Kutera, Maria, St-Germain, Jonathan, Hanley, Ronan P., Wolf, Esther, Paulakonis, Ethan, Kenney, Tristan M. G., Duan, Shili, Shrestha, Suman, Owens, Dominic D. G., Maitland, Matthew E. R., Pon, Ailing, Szewczyk, Magdalena, Lamberto, Anthony Joseph, Menes, Michael, Li, Fengling, Penn, Linda Z., Barsyte-Lovejoy, Dalia, Brown, Nicholas G., Barsotti, Anthony M., Stamford, Andrew W., Collins, Jon L., Wilson, Derek J., Raught, Brian, Licht, Jonathan D., James, Lindsey I., and Arrowsmith, Cheryl H.

Published
2024
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2. A chemical probe to modulate human GID4 Pro/N-degron interactions

Author

Owens, Dominic D. G., Maitland, Matthew E. R., Khalili Yazdi, Aliakbar, Song, Xiaosheng, Reber, Viviane, Schwalm, Martin P., Machado, Raquel A. C., Bauer, Nicolas, Wang, Xu, Szewczyk, Magdalena M., Dong, Cheng, Dong, Aiping, Loppnau, Peter, Calabrese, Matthew F., Dowling, Matthew S., Lee, Jisun, Montgomery, Justin I., O’Connell, Thomas N., Subramanyam, Chakrapani, Wang, Feng, Adamson, Ella C., Schapira, Matthieu, Gstaiger, Matthias, Knapp, Stefan, Vedadi, Masoud, Min, Jinrong, Lajoie, Gilles A., Barsyte-Lovejoy, Dalia, Owen, Dafydd R., Schild-Poulter, Caroline, and Arrowsmith, Cheryl H.

Published
2024
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4. A chemical probe targeting the PWWP domain alters NSD2 nucleolar localization

Author

Dilworth, David, Hanley, Ronan P., Ferreira de Freitas, Renato, Allali-Hassani, Abdellah, Zhou, Mengqi, Mehta, Naimee, Marunde, Matthew R., Ackloo, Suzanne, Carvalho Machado, Raquel Arminda, Khalili Yazdi, Aliakbar, Owens, Dominic D. G., Vu, Victoria, Nie, David Y., Alqazzaz, Mona, Marcon, Edyta, Li, Fengling, Chau, Irene, Bolotokova, Albina, Qin, Su, Lei, Ming, Liu, Yanli, Szewczyk, Magdalena M., Dong, Aiping, Kazemzadeh, Sina, Abramyan, Tigran, Popova, Irina K., Hall, Nathan W., Meiners, Matthew J., Cheek, Marcus A., Gibson, Elisa, Kireev, Dmitri, Greenblatt, Jack F., Keogh, Michael-C., Min, Jinrong, Brown, Peter J., Vedadi, Masoud, Arrowsmith, Cheryl H., Barsyte-Lovejoy, Dalia, James, Lindsey I., and Schapira, Matthieu

Published
2022
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6. Discovery and Characterization of a Chemical Probe Targeting the Zinc-Finger Ubiquitin-Binding Domain of HDAC6

Author

Harding, Rachel J., primary, Franzoni, Ivan, additional, Mann, Mandeep K., additional, Szewczyk, Magdalena M., additional, Mirabi, Bijan, additional, Ferreira de Freitas, Renato, additional, Owens, Dominic D. G., additional, Ackloo, Suzanne, additional, Scheremetjew, Alexej, additional, Juarez-Ornelas, Kevin A., additional, Sanichar, Randy, additional, Baker, Rachel J., additional, Dank, Christian, additional, Brown, Peter J., additional, Barsyte-Lovejoy, Dalia, additional, Santhakumar, Vijayaratnam, additional, Schapira, Matthieu, additional, Lautens, Mark, additional, and Arrowsmith, Cheryl H., additional

Published
2023
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8. Recruitment of FBXO22 for Targeted Degradation of NSD2.

Author

Nie DY, Tabor JR, Li J, Kutera M, St-Germain J, Hanley RP, Wolf E, Paulakonis E, Kenney TMG, Duan S, Shrestha S, Owens DDG, Pon A, Szewczyk M, Lamberto AJ, Menes M, Li F, Barsyte-Lovejoy D, Brown NG, Barsotti AM, Stamford AW, Collins JL, Wilson DJ, Raught B, Licht JD, James LI, and Arrowsmith CH

Abstract

Targeted protein degradation (TPD) is an emerging therapeutic strategy that would benefit from new chemical entities with which to recruit a wider variety of ubiquitin E3 ligases to target proteins for proteasomal degradation. Here, we describe a TPD strategy involving the recruitment of FBXO22 to induce degradation of the histone methyltransferase and oncogene NSD2. UNC8732 facilitates FBXO22-mediated degradation of NSD2 in acute lymphoblastic leukemia cells harboring the NSD2 gain of function mutation p.E1099K, resulting in growth suppression, apoptosis, and reversal of drug resistance. The primary amine of UNC8732 is metabolized to an aldehyde species, which engages C326 of FBXO22 in a covalent and reversible manner to recruit the SCF FBXO22 Cullin complex. We further demonstrate that a previously reported alkyl amine-containing degrader targeting XIAP is similarly dependent on SCF FBXO22 . Overall, we present a highly potent NSD2 degrader for the exploration of NSD2 disease phenotypes and a novel FBXO22-dependent TPD strategy.

Published
2023
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9. Measuring Protein-Protein Interactions in Cells using Nanoluciferase Bioluminescence Resonance Energy Transfer (NanoBRET) Assay.

Author

Szewczyk MM, Owens DDG, and Barsyte-Lovejoy D

Subjects
Reproducibility of Results, Luminescent Proteins genetics, Luminescent Proteins metabolism, Energy Transfer, Biophysical Phenomena, Luminescent Measurements methods, Bioluminescence Resonance Energy Transfer Techniques methods
Abstract

Protein-protein interactions (PPIs) are increasingly recognized for their roles in functional cellular networks and their importance in disease-targeting contexts. Assessing PPI in the native cellular environment is challenging and requires specific and quantitative methods. Bioluminescence resonance energy transfer (BRET) is a biophysical process that can be used to quantify PPI. With Nanoluciferase bioluminescent protein as a donor and a fluorescent chloroalkane ligand covalently bound to HaloTag protein as an acceptor, NanoBRET provides a versatile and robust system to quantitatively measure PPI in living cells. BRET efficiency is proportional to the distance between the donor and acceptor, allowing for the measurement of PPI in real time. In this paper, we describe the use of NanoBRET to study specific interactions between proteins of interest in living cells that can be perturbed by using small-molecule antagonists and genetic mutations. Here, we provide a detailed protocol for expressing NanoLuc and HaloTag fusion proteins in cell culture and the necessary optimization of NanoBRET assay conditions. Our example results demonstrate the reliability and sensitivity of NanoBRET for measuring interactions between proteins, protein domains, and short peptides and quantitating the PPI antagonist compound activity in living cells., (© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

Published
2023
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