Matthew R. Batchelor

This study identifies the molecular mechanism by which hnRNPK activates Aurora-A kinase through specific residue interactions in the Y-pocket.

The paper identifies the DNA binding domain of TFIIIC5 as a key interaction site for N-myc and elucidates the molecular mechanism of their interaction using structural and biophysical methods.

This study presents structural models of the Aurora-A/Bora and Aurora-A/Bora/PLK1 complexes, revealing how Bora bridges Aurora-A activation and PLK1 substrate recognition.

This study generates genomic sequences for Galapagos iguanas to explore their evolutionary history and identify genes associated with marine adaptation, pigmentation, and DNA damage responses.

This study uses NMR to analyze the structure, dynamics, and interactions of N-myc's transactivation domain, revealing phosphorylation sites and binding interactions.