Sponsor: Merck Research Laboratories
Citation: For her seminal contributions to peptide structure and function, peptide models for protein folding and function, and roles of peptide and protein aggregation in disease.
Current position: Distinguished Professor of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts, Amherst
Education: A.B., chemistry, Mount Holyoke College; Ph.D., biophysics, Harvard University
Gierasch on what she hopes to accomplish in the next decade: “The environment in a cell is extremely complex and challenging for the process of protein folding, leading to a need for a network of species that protect protein states that are susceptible to aggregation—the protein homeostasis network. We are working with colleagues and collaborators to understand the underlying mechanisms of protein homeostasis from the level of the molecular chaperone machines that act on protein clients to the coordinated action of the network in all of its complexity. We would love to witness and contribute to new discoveries related to these questions, both because of the fascinating basic science involved and because failures in these systems are implicated in a wide array of diseases, including neurodegenerative diseases.”
What her colleagues say:“Lila demonstrates the highest levels of scientific creativity in her research. During the past 40 years, she has made seminal contributions to our understanding of peptide structure and function, the mechanisms by which sorting peptides direct intracellular protein trafficking, the roles of molecular chaperones in protein folding, the interplay among secondary structural elements in determining the tertiary structure of proteins, and understanding the role of peptide and protein aggregation in disease.”—Joel Schneider, National Cancer Institute
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