Mohammed is a Ph.D. candidate at the Francis Crick Institute and Imperial College London in the United Kingdom. He earned his master’s degree from the Stony Brook University in the United States. His research solved a fundamental question in biology: How is the nucleation of actin—the most abundant cellular protein—triggered and regulated at the molecular and structural level?
In his first-author paper, Mohammed and colleagues came up with a unique approach to solve this question, which had puzzled the field for over two decades. Mohammed’s research revealed the first high-resolution structure of an activated actin nucleator, Arp2/3 complex, while nucleating the first monomers of an actin filament. Regulation of this process is critical for many cellular functions such as cell motility, maintenance of cell shape, and regulation of transcription. Its dysregulation is associated with pathologies such as cancer metastasis, neurodegeneration, and bacterial and viral infections.
Mohammed’s current research uses state-of-the-art time-resolved cryo-EM to understand the dynamics of cellular processes—at the highest possible spatiotemporal resolution—while they progress in time; a long-overdue endeavor in the field. Mohammed aims to understand the regulation of cullin–RING ligases, enzymes that label cellular proteins for cellular trafficking or destruction.