Advances in covalent drug discovery
L Boike, NJ Henning, DK Nomura - Nature Reviews Drug Discovery, 2022 - nature.com
Covalent drugs have been used to treat diseases for more than a century, but tools that
facilitate the rational design of covalent drugs have emerged more recently. The purposeful …
facilitate the rational design of covalent drugs have emerged more recently. The purposeful …
Emerging and Re-emerging Warheads for Targeted Covalent Inhibitors: An Update
L Hillebrand, XJ Liang, RAM Serafim… - Journal of Medicinal …, 2024 - ACS Publications
Covalent inhibitors and other types of covalent modalities have seen a revival in the past two
decades, with a variety of new targeted covalent drugs having been approved in recent …
decades, with a variety of new targeted covalent drugs having been approved in recent …
An activity-based oxaziridine platform for identifying and developing covalent ligands for functional allosteric methionine sites: redox-dependent inhibition of cyclin …
A Gonzalez-Valero, AG Reeves… - Journal of the …, 2022 - ACS Publications
Activity-based protein profiling (ABPP) is a versatile strategy for identifying and
characterizing functional protein sites and compounds for therapeutic development …
characterizing functional protein sites and compounds for therapeutic development …
Discovery of potent and selective inhibitors against protein-derived electrophilic cofactors
Electrophilic cofactors are widely distributed in nature and play important roles in many
physiological and disease processes, yet they have remained blind spots in traditional …
physiological and disease processes, yet they have remained blind spots in traditional …
Developing an Affinity-Based Chemical Proteomics Method to In Situ Capture Amorphous Aggregated Proteome and Profile Its Heterogeneity in Stressed Cells
Stress induced amorphous proteome aggregation is a hallmark for diseased cells, with the
proteomic composition intimately associated with disease pathogenicity. Due to its …
proteomic composition intimately associated with disease pathogenicity. Due to its …
[HTML][HTML] CySP3-96 enables scalable, streamlined, and low-cost sample preparation for cysteine chemoproteomic applications
F Shikwana, BS Heydari, S Ofori, C Truong… - Molecular & Cellular …, 2024 - Elsevier
Cysteine chemoproteomic screening platforms are widely utilized for chemical probe and
drug discovery campaigns. Chemoproteomic compound screens, which use a mass …
drug discovery campaigns. Chemoproteomic compound screens, which use a mass …
Protein oxidation of fucose environments (POFE) reveals fucose–protein interactions
Cell membrane glycoproteins are generally highly fucosylated and sialylated, and post-
translational modifications play important roles in the proteins' functions of signaling, binding …
translational modifications play important roles in the proteins' functions of signaling, binding …
Automation to Enable High-Throughput Chemical Proteomics
Chemical proteomics utilizes small-molecule probes to covalently engage with their
interacting proteins. Since chemical probes are tagged to the active or binding sites of …
interacting proteins. Since chemical probes are tagged to the active or binding sites of …
Flipping the switch: innovations in inducible probes for protein profiling
SM McKenna, EM Fay, JF McGouran - ACS Chemical Biology, 2021 - ACS Publications
Over the past two decades, activity-based probes have enabled a range of discoveries,
including the characterization of new enzymes and drug targets. However, their suitability in …
including the characterization of new enzymes and drug targets. However, their suitability in …
Protein phosphatase PP2Cα S-glutathionylation regulates cell migration
DSK Kukulage, KTG Samarasinghe, NNJM Don… - Journal of Biological …, 2024 - jbc.org
Redox signaling is a fundamental mechanism that controls all major biological processes
partly via protein cysteine oxidations, including S-glutathionylation. Despite over 2000 …
partly via protein cysteine oxidations, including S-glutathionylation. Despite over 2000 …