Jason Gestwicki, PhD

Executive Committee Member
Phone: +1 415 502-7121
Fax: +1 415 502-7053
675 Nelson Rising Lane, Rm 311
UCSF Box 0518
San Francisco, CA 94158
United States

What I do

My research group studies how molecular chaperones maintain protein homeostasis. This question is important because imbalances in protein homeostasis are linked to a number of incurable diseases, including neurodegenerative disorders. Molecular chaperones regulate all aspects of a protein’s lifecycle, including its expression, folding, trafficking and degradation. However, it isn’t yet clear how we might promote the activity of chaperones to cure diseases. Our approach to this question is to develop chemical probes that reveal how chaperones interact with disease-associated proteins.

Departmental research area

My research expertise

protein homeostasis, molecular chaperones, Alzheimer's disease, protein-protein interaction (PPI), high-throughput screening (HTS), Drug Discovery

Professional background


The Gestwicki Laboratory is interested in molecular chaperones, protein homeostasis and protein misfolding disorders. To approach the big questions in this area, we use a chemical biology strategy that includes the discovery and optimization of new chemical inhibitors. We use these chemical probes to acutely perturb chaperone functions, revealing how these systems normally protect from cancer and neurodegeneration. Many of our chemical probes target allosteric and protein-protein interaction sites on the molecular chaperones and we have a significant interest in discovering inhibitors of "difficult" targets. We hope to better understand the logic of protein folding and misfolding and use this information to design more effective therapies.

Research keywords

  • protein misfolding diseases
  • protein-protein interactions
  • medicinal chemistry
  • protein folding
  • high throughput screening
  • molecular chaperones
  • organic synthesis
  • allostery
  • Heat-Shock Proteins
  • Fluorometry
  • HSP90 Heat-Shock Proteins
  • molecular chaperones
  • tau Proteins
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • protein folding
  • Benzothiazoles
  • Protein Interaction Maps
  • HSP40 Heat-Shock Proteins
  • Apoptosis Regulatory Proteins
  • HSC70 Heat-Shock Proteins
  • Tauopathies
  • Proteostasis