S. M. Hinshaw

The paper develops bivalent molecules that convert kinase inhibitors into activators of proapoptotic genes, achieving selective killing of DLBCL cells with low cytotoxicity.

The paper determines the crystal structure of a Cse4 peptide bound to the Okp1-Ame1 heterodimer in budding yeast, revealing key interactions essential for centromere recognition.

This study demonstrates the use of KLHDC2 as a substrate adaptor for targeted protein degradation using peptide-based bivalent compounds.

The paper identifies multi-site phosphorylation of Mif2/CENP-C as essential for inner kinetochore assembly and accurate chromosome segregation in yeast.

This study presents crystal structures of SARS-CoV-2 Mpro bound to viral substrate peptides, revealing how peptide sequences influence catalytic efficiency and providing insights for antiviral drug design.

This study identifies a mechanism for regulated kinetochore sumoylation by showing that Ulp2 recruitment to Ctf3/CENP-I controls sumoylation levels and chromosome segregation.

This study presents a high-resolution structure of the Ctf3 complex bound to Cnn1-Wip1, revealing their role in kinetochore stabilization and feedback regulation across yeast and vertebrates.

The paper reports a near-atomic model of the yeast Ctf3 complex using cryo-EM, providing insights into its recruitment and function.