Rate My Professor Isabelle Rouiller

The Rouiller laboratory employs cryo-EM techniques, including single particle analysis and tomography, to determine structures of molecular nanomachines in action along biological pathways, with implications for disease mechanisms and therapeutic development. Key research areas include the AAA ATPase p97 and its functions in cellular homeostasis, cancer, and neurodegenerative conditions such as Inclusion Body Myopathy with early-onset Paget disease and Frontotemporal Dementia (IBMFD) and Amyotrophic Lateral Sclerosis (ALS); membrane transporters like the Anthrax lethal toxin prepore complex, ABC transporter MalFGK2, RND transporters involved in mycolic acid export from Mycobacterium tuberculosis, and the mechanosensitive ion channel TACAN; and viral glycoproteins such as Influenza Hemagglutinin for host-pathogen interactions and vaccine design. Notable publications encompass "A major conformational change in p97 AAA ATPase upon ATP binding" (Journal of Biological Chemistry, 2006), "Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry" (Journal of General Physiology, 2016), "Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK2" (Journal of Biological Chemistry, 2017), "The peptidisc, a simple method for stabilizing membrane proteins in detergent-free solution" (eLife, 2018), and "Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy" (PLoS ONE, 2017). Her contributions advance structural insights into protein complexes critical for mitochondrial and neuronal health.