Justine C. Rutter

Jul 28, 2024 | nature.com | Moritz Hunkeler |Mingxing Teng |Justine C. Rutter |Anna M Schmoker |Rebecca Metivier |Woong Sub Byun | +9 more

AbstractMolecular glues are proximity-inducing small molecules that have emerged as an attractive therapeutic approach. However, developing molecular glues remains challenging, requiring innovative mechanistic strategies to stabilize neoprotein interfaces and expedite discovery. Here we unveil a trans-labeling covalent molecular glue mechanism, termed ‘template-assisted covalent modification’.

May 30, 2024 | nature.com | Andrew Waters |Justine C. Rutter |Shannon McCall |Mariaelena Pierobon |J. Joshua Smith |Channing J. Der

AbstractAcquired resistance remains a major challenge for therapies targeting oncogene activated pathways. KRAS is the most frequently mutated oncogene in human cancers, yet strategies targeting its downstream signaling kinases have failed to produce durable treatment responses.

Jan 2, 2024 | jci.org | Hojong Yoon |Justine C. Rutter |Yen-Der Li |Benjamin Ebert

Pharmacological manipulation of the ubiquitin-proteasome systemThe majority of induced protein degradation engages the ubiquitin-proteasome system. This pathway leverages a posttranslational modification – the covalent attachment of ubiquitin to a substrate protein through the coordinated, sequential activity of three classes of enzymes (22). First, an E1 ubiquitin-activating enzyme utilizes ATP to adenylate ubiquitin and establish a thioester bond between ubiquitin and the E1 enzyme.