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Després, Philippe C.; Dubé, Alexandre K.; Picard, Marie-Ève; Grenier, Jordan; Shi, Rong et al. (2024). Compensatory mutations potentiate constructive neutral evolution by gene duplication. Science 385(6710) , 770-775. 10.1126/science.ado5719. |
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Ali, Mohamed G.; Wahba, Haytham M.; Igelmann, Sebastian; Cyr, Normand; Ferbeyre, Gerardo et al. (2024). Structural and functional characterization of the role of acetylation on the interactions of the human Atg8-family proteins with the autophagy receptor TP53INP2/DOR. Autophagy . 10.1080/15548627.2024.2353443. |
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Bon, Christopher G.; Grigg, Jason C.; Lee, Jaeyong; Robb, Craig S.; Caveney, Nathanael A. et al. (2024). Structural and kinetic analysis of the monofunctional Staphylococcus aureus PBP1. Journal of Structural Biology 216(2) , 108086. 10.1016/j.jsb.2024.108086. |
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Smith, Christopher R.; Chen, Dan; Christensen, James G.; Coulombe, René; Féthière, James et al. (2023). Discovery of Five SOS2 Fragment Hits with Binding Modes Determined by SOS2 X-Ray Cocrystallography. Journal of Medicinal Chemistry 67(1) , 774-781. 10.1021/acs.jmedchem.3c02140. |
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Pérez-Vargas, Jimena; Worrall, Liam J.; Olmstead, Andrea D.; Ton, Anh-Tien; Lee, Jaeyong et al. (2023). A novel class of broad-spectrum active-site-directed 3C-like protease inhibitors with nanomolar antiviral activity against highly immune-evasive SARS-CoV-2 Omicron subvariants. Emerging Microbes and Infections 12(2) . 10.1080/22221751.2023.2246594. |
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McLeod, Matthew J.; Tran, Norman; McCluskey, Gregory D.; Gillis, Tom D.; Bearne, Stephen L. et al. (2023). A metal‐dependent conformational change provides a structural basis for the inhibition of CTP synthase by gemcitabine‐5′‐triphosphate. Protein Science 32(6) . 10.1002/pro.4648. |
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Chen, Sizhu Amelia; Arutyunova, Elena; Lu, Jimmy; Khan, Muhammad Bashir; Rut, Wioletta et al. (2023). SARS-CoV-2 Mpro Protease Variants of Concern Display Altered Viral Substrate and Cell Host Target Galectin-8 Processing but Retain Sensitivity toward Antivirals. ACS Central Science 9(4) , 696-708. 10.1021/acscentsci.3c00054. |
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Callahan, Alex J.; Gandhesiri, Satish; Travaline, Tara L.; Lozano Salazar, Lia; Hanna, Stephanie et al. (2023). Single-Shot Flow Synthesis of D-Proteins for Mirror-Image Phage Display. Environmental Science & Technology . 10.26434/chemrxiv-2023-x86xp. |
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Mabanglo, Mark F.; Wong, Keith S.; Barghash, Marim M.; Leung, Elisa; Chuang, Stephanie H.W. et al. (2022). Potent ClpP agonists with anticancer properties bind with improved structural complementarity and alter the mitochondrial N-terminome. Structure . 10.1016/j.str.2022.12.002. |
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Lee, Jaeyong; Kenward, Calem; Worrall, Liam J.; Vuckovic, Marija; Gentile, Francesco et al. (2022). X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation. Nature Communications 13(1) . 10.1038/s41467-022-32854-4. |
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Nguyen, Peter; Eshaque, Rony; Garland, Barbara Anne; Dang, Anthony; Suits, Michael D. L. et al. (2022). Degradation of chondroitin sulfate A by a PUL-like operon in Tannerella forsythia. PLoS ONE 17(9) , e0272904. 10.1371/journal.pone.0272904. |
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Forrester, Taylor J. B.; Ovchinnikova, Olga G.; Li, Zhixiong; Kitova, Elena N.; Nothof, Jeremy T. et al. (2022). The retaining β-Kdo glycosyltransferase WbbB uses a double-displacement mechanism with an intermediate adduct rearrangement step. Nature Communications 13(1) . 10.1038/s41467-022-33988-1. |
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Lorente Cobo, Neil; Sibinelli-Sousa, Stephanie; Biboy, Jacob; Vollmer, Waldemar; Bayer-Santos, Ethel et al. (2022). Molecular characterization of the type VI secretion system effector Tlde1a reveals a structurally altered LD-transpeptidase fold. Journal of Biological Chemistry 298(11) , 102556. 10.1016/j.jbc.2022.102556. |
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Kuttiyatveetil, Jijin R.A.; Soufari, Heddy; Dasovich, Morgan; Uribe, Isabel R.; Mirhasan, Manija et al. (2022). Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a distinctive mode of engaging poly(ADP-ribose). Cell Reports 41(4) , 111529. 10.1016/j.celrep.2022.111529. |
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