Jerome M.Fox

  • Associate Professor
  • CHEMICAL AND BIOLOGICAL ENGINEERING
  • BIOMEDICAL ENGINEERING PROGRAM
Address

Office: JSCBB D126
Mailbox: 596 UCB

Education

PhD, University of California, Berkeley (2012)
BS, Johns Hopkins University (2007)

Awards

  • National Institutes of Health Maximizing Investigators' Research Award (MIRA), 2021
  • Outstanding Undergraduate Teaching Faculty Award, Department of Chemical and Biological Engineering, CU 糖心Vlog破解版, 2020
  • Army Early Career Award for Scientists and Engineers (ECASE) Award, 2018
  • Army Research Office Young Investigator Award, 2018
  • National Science Foundation CAREER Award, 2018

Selected Publications

  • Sarkar A, Kim EY, Jang T, Hongdusit A, Kim H, Choi JM, and Fox JM (2021). Microbially guided discovery and biosynthesis of biologically active natural products. ACS Synthetic Biology, 10 (6), 1505-1519.
  • Ruppe A, Mains K, and Fox JM (2020). A Kinetic Rationale for Functional Redundancy in Fatty Acid Biosynthesis. Proceedings of the National Academy of Sciences, 117 (38), 23557-23564
  • Hongdusit A, Zwart P, Sankaran B, and Fox JM (2020). Minimally Disruptive Optical Control of Protein Tyrosine Phosphatase 1B. Nature Communications,听11 (788), 1-11.

  • Ruppe A and Fox JM (2018). Analysis of Interdependent Kinetic Controls of Fatty Acid Synthases. ACS Catalysis, 8, 11722-11734.

  • Hjortness MK, Riccardi L, Zwart PH, Sankaran B, De Vivo M, and Fox JM (2018). Evolutionarily Conserved Allosteric Communication in Protein Tyrosine Phosphatases. Biochemistry, 57 (45),

  • Hjortness MK, Riccardi L, Hongdusit A, Ruppe A, Zhao M, Kim EY, Zwart P, Sankaran B, Arthanari H, Sousa MC, De Vivo M, and Fox JM (2018). Abietane-Type Diterpenoids Inhibit Protein Tyrosine Phosphatases by Stabilizing an Inactive Enzyme Conformation. Biochemistry, 57 (40), 5886-5896.

  • Fox JM, Zhao M, Fink MJ, Kang K, and Whitesides GM (2018). The Molecular Origin of Enthalpy/Entropy Compensation in Biomolecular Recognition. Annual Review of Biophysics, 47.

  • Fox JM, Kang K, Sastry M, Sherman W, Sankaran B, Zwart PH, and Whitesides GM (2017). Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase. Angewandte Chemie International Edition, 56, 1-6.
  • Semenov SN, Kraft LJ, Ainla A, Zhao M, Baghbanzadeh M, Campbell VE, Kang K, Fox JM, and Whitesides GM (2016). Autocatalytic, bistable, oscillatory networks of biologically relevant organic reactions. Nature, 537 (7622), 656-660.
  • Fox JM, Kang K, Lockett MR, Baghbanzadeh M, Sherman W, H茅roux A, Sastry M, Whitesides GM (2015). Interactions between Hofmeister Anions and the Binding Pocket of a Protein. Journal of the American Chemical Society, 137 (11), 3859-3866.
  • Fox JM and Whitesides GM (2015). Warning Signals for Eruptive Events in Spreading Fires. Proceedings of the National Academy of Sciences, 112 (8), 2378-2383.
  • Nemiroski A, Gonidec M, Fox JM, Jean-Remy P, Turnage E, and Whitesides GM (2014). Engineering Shadows to Fabricate Optical Metasurfaces. ACS Nano, 8 (11), 11061-11070.
  • Fox JM, Jess P, Jambusaria RB, Moo GM, Liphardt J, Clark DS, Blanch HW (2013). A Single-Molecule Analysis Reveals Morphological Targets for Cellulase Synergy. Nature Chemical Biology, 9 (6), 356-61.

Research Interests

The biological cell is, perhaps, the most impressive dissipative system found in nature. Operating far from equilibrium, the cell utilizes gradients in free energy to drive networks of chemical reactions that are staggeringly complex, yet tightly regulated in space and time. A detailed understanding of cellular function (and dysfunction) requires an understanding of the mechanisms by which individual reactions interact and organize themselves to sustain the higher-order biochemical processes (e.g. metabolism, cell division) that constitute cellular 鈥渓ife.鈥 My group studies these mechanisms of interaction and organization (temporal and spatial) and uses them to interrogate, control, and rewire biochemical networks of relevance to human health, energy, and the environment.

My research program has three broad goals: (i) to develop physical and biochemical methods to study and control the activities of enzymes of metabolic relevance, (ii) to employ those methods to answer fundamental questions of cellular metabolism, human disease, and molecular recognition, and (iii) to apply those methods, and correspondingly evolved theories, to develop novel enzyme inhibitors and protein therapeutics, and to engineer biosynthetic pathways for the production of fuels and chemicals. My group employs concepts and techniques from physical chemistry, biochemistry, synthetic biology, optics, nanotechnology, and applied mathematics.