David Ron

David Ron

David Ron in 2014, portrait via the Royal Society
Fields
Institutions
Alma mater Technion – Israel Institute of Technology
Notable awards
Website
ron.cimr.cam.ac.uk

David Ron MD FRS FMedSci is a Professor of Cellular Pathophysiology and Clinical Biochemistry, Cambridge Institute for Medical Research and the Institute of Metabolic Science, University of Cambridge where he is also a Wellcome Trust Principal Research Fellow.[3][4][5]

Education and career

Ron was educated at the Technion in Israel where he received his medical tranining. He went for medical internship and residency training at Mount Sinai Medical Center, in New York City and in 1989 completed subspecialty training in Endocrinology at Massachusetts General Hospital in Boston.[6]

Research

Ron's research investigates malfolded proteins, cellular degeneration and human disease.[7][8][9][10][11]

Awards and honours

Ron was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

“ David Ron has pioneered our understanding of how cells cope with the stress induced by protein misfolding in the endoplasmic reticulum. This stress is increasingly recognised to contribute to many diseases including endocrine disorders and neurodegeneration. Among many achievements, he has deciphered the molecular mechanism by which cells match protein synthesis rates to protein folding in the secretory pathway. His greatest conceptual contribution has been to reveal the precariousness of the protein folding environment in the ER and to highlight how it is challenged by subtle failure of homeostasis - concepts with both fundamental implications to biology and therapeutic application.[1] ”

Ron was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2013. His nomination reads

“ David Ron is Professor of Cellular Pathophysiology and Clinical Biochemistry at the University of Cambridge. Protein misfolding in the endoplasmic reticulum (ER stress) is implicated in processes from neurodegeneration to endocrine disorders. David Ron has been at the forefront of this confluence of Cell Biology and Pathophysiology. He identified the transcription factor CHOP and discovered its role in deregulating adipose tissue development in liposarcoma. He identified the ER stress transducer PERK, establishing the molecular mechanism by which unfolded protein stress regulates protein synthesis and identified the long-sought mammalian counterpart of the yeast master regulator of gene expression in the UPR, IRE. An endocrinologist by training, he is deeply committed to disease-oriented research and laboratory practice.[2] ”

References

  1. 1 2 "Professor David Ron FMedSci FRS". London: The Royal Society. Archived from the original on 2014-10-07.
  2. 1 2 "Professor David Ron FRS FMedSci". London: The Academy of Medical Sciences. Archived from the original on 2014-10-07.
  3. ↑ List of publications from Microsoft Academic Search
  4. ↑ David Ron's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
  5. ↑ ABCD Lecture: An interview with Professor David Ron on YouTube
  6. ↑ "Biosketch: David Ron, M.D.". NYU Langone Medical Center. Archived from the original on 2014-10-07.
  7. ↑ Ron, D.; Walter, P. (2007). "Signal integration in the endoplasmic reticulum unfolded protein response". Nature Reviews Molecular Cell Biology 8 (7): 519. doi:10.1038/nrm2199. PMID 17565364.
  8. ↑ Ron, D.; Harding, H. P.; Zhang, Y. (1999). "Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase". Nature 397 (6716): 271–4. doi:10.1038/16729. PMID 9930704.
  9. ↑ Harding, H. P.; Novoa, I.; Zhang, Y.; Zeng, H.; Wek, R.; Schapira, M.; Ron, D. (2000). "Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells". Molecular Cell 6 (5): 1099. doi:10.1016/S1097-2765(00)00108-8. PMID 11106749.
  10. ↑ Urano, F.; Wang, X; Bertolotti, A; Zhang, Y; Chung, P; Harding, H. P.; Ron, D (2000). "Coupling of Stress in the ER to Activation of JNK Protein Kinases by Transmembrane Protein Kinase IRE1". Science 287 (5453): 664–6. doi:10.1126/science.287.5453.664. PMID 10650002.
  11. ↑ Harding, H. P.; Zhang, Y.; Zeng, H.; Novoa, I.; Lu, P. D.; Calfon, M.; Sadri, N.; Yun, C.; Popko, B.; Paules, R.; Stojdl, D. F.; Bell, J. C.; Hettmann, T.; Leiden, J. M.; Ron, D. (2003). "An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress". Molecular Cell 11 (3): 619. doi:10.1016/S1097-2765(03)00105-9. PMID 12667446.


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