Stefan G. Kathman
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View article: <scp>NONO</scp> Maintains <scp>SREBP</scp> ‐Regulated Cholesterol Biosynthesis via <scp>RNA</scp> Binding in Neuroblastoma
<span>NONO</span> Maintains <span>SREBP</span> ‐Regulated Cholesterol Biosynthesis via <span>RNA</span> Binding in Neuroblastoma Open
High‐risk neuroblastoma is associated with upregulation of cholesterol biosynthesis through increased expression of sterol regulatory element—binding protein (SREBP). NONO, a multifunctional nuclear RNA binding protein, is an established o…
View article: Remodeling oncogenic transcriptomes by small molecules targeting NONO
Remodeling oncogenic transcriptomes by small molecules targeting NONO Open
View article: A masked zinger to block GPX4
A masked zinger to block GPX4 Open
View article: Blockade of the Lysophosphatidylserine Lipase ABHD12 Potentiates Ferroptosis in Cancer Cells
Blockade of the Lysophosphatidylserine Lipase ABHD12 Potentiates Ferroptosis in Cancer Cells Open
Ferroptosis is a type of cell death caused by the pathogenic accumulation of lipid hydroperoxides. Pharmacological mechanisms to induce ferroptosis may provide a way to kill cancer cells that are resistant to other forms of cell death like…
View article: Covalent-Fragment Screening of BRD4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites
Covalent-Fragment Screening of BRD4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites Open
BRD4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding s…
View article: Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites
Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites Open
Brd4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding s…
View article: Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites
Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites Open
Brd4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding s…
View article: Discovery of covalent enzyme inhibitors using virtual docking of covalent fragments
Discovery of covalent enzyme inhibitors using virtual docking of covalent fragments Open
View article: Front Cover: Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from <i>Chlamydia trachomatis</i> (ChemMedChem 19/2018)
Front Cover: Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from <i>Chlamydia trachomatis</i> (ChemMedChem 19/2018) Open
The Front Cover shows a covalent inhibitor (orange) simultaneously addressing the active sites of the Chlamydia trachomatis deubiquitylase 1 (Cdu1, green) and the adenovirus protease (adenain, red). The covalent bond is highlighted in yell…
View article: Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from <i>Chlamydia trachomatis</i>
Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from <i>Chlamydia trachomatis</i> Open
Based on the similarity between the active sites of the deubiquitylating and deneddylating enzyme ChlaDub1 (Cdu1) and the evolutionarily related protease adenain, a target‐hopping screening approach on a focused set of adenain inhibitors w…
View article: Covalent tethering of fragments for covalent probe discovery
Covalent tethering of fragments for covalent probe discovery Open
Design rules for covalent fragment libraries are outlined.
View article: Inhibitors of the Ubiquitin Ligase Nedd4-1 Discovered by Covalent Fragment Screening
Inhibitors of the Ubiquitin Ligase Nedd4-1 Discovered by Covalent Fragment Screening Open
View article: A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism
A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism Open
E3 ligases are genetically implicated in many human diseases, yet E3 enzyme mechanisms are not fully understood, and there is a strong need for pharmacological probes of E3s. We report the discovery that the HECT E3 Nedd4-1 is a processive…