Stanley B. Prusiner

Stanley Prusiner

Prusiner in 2007
Born Stanley Benjamin Prusiner
(1942-05-28) May 28, 1942
Des Moines, Iowa, United States
Residence San Francisco, United States
Nationality American
Fields
Institutions
Alma mater University of Pennsylvania (BS, MD)
Known for
Notable awards
Spouse Sandy Turk Prusiner[2]
Children two[2]
Website
ind.ucsf.edu/ind/aboutus/faculty/prusiners

Stanley Benjamin Prusiner M.D (born May 28, 1942[3]) is an American neurologist and biochemist. Currently the director of the Institute for Neurodegenerative Diseases at University of California, San Francisco (UCSF). Prusiner discovered prions, a class of infectious self-reproducing pathogens primarily or solely composed of protein. He received the Albert Lasker Award for Basic Medical Research in 1994 and the Nobel Prize in Physiology or Medicine in 1997 for prion research developed by him and his team of experts (D. E. Garfin, D. P. Stites, W. J. Hadlow, C. W. Eklund) beginning in the early 1970s.[4][5]

Early life, career and research

Prusiner was born in Des Moines, Iowa, the son of Miriam (Spigel) and Lawrence Prusiner, an architect. He spent his childhood in Des Moines and Cincinnati, Ohio, where he attended Walnut Hills High School, where he was known as the little Genius for his groundbreaking work on a repellent for Boxelder bugs. Prusiner received a Bachelor of Science degree in chemistry from the University of Pennsylvania and later received his M.D. from the University of Pennsylvania School of Medicine.[3] Prusiner then completed an internship in medicine at the University of California, San Francisco. Later Prusiner moved to the National Institutes of Health, where he studied glutaminases in E. coli in the laboratory of Earl Stadtman.

After three years at NIH, Prusiner returned to UCSF to complete a residency in neurology. Upon completion of the residency in 1974, Prusiner joined the faculty of the UCSF neurology department. Since that time, Prusiner has held various faculty and visiting faculty positions at both UCSF and UC Berkeley.

Prusiner currently heads the Institute for Neurodegenerative Diseases research laboratory at UCSF, working on prion disease, Alzheimer's disease and tauopathies.[6]

Awards and honors

Prusiner won the Nobel Prize in Physiology or Medicine in 1997 for his work in proposing an explanation for the cause of bovine spongiform encephalopathy ("mad cow disease") and its human equivalent, Creutzfeldt–Jakob disease.[3] In this work, he coined the term prion, which comes from the words "proteinaceous" and "infectious," in 1982 to refer to a previously undescribed form of infection due to protein misfolding.[7]

Prusiner was elected to the National Academy of Science in 1992 and to its governing council in 2007. He is also an elected member of the American Academy of Arts and Sciences (1993), a Foreign Member of the Royal Society (ForMemRS) in 1997,[1][8] and the American Philosophical Society (1998), the Serbian Academy of Sciences and Arts (2003), and the Institute of Medicine.

References

  1. 1 2 "Fellows of the Royal Society". London: Royal Society. Archived from the original on 2015-03-16.
  2. 1 2 http://www.nobelprize.org/nobel_prizes/medicine/laureates/1997/prusiner-autobio.html
  3. 1 2 3 "Stanley B. Prusiner - Autobiography". NobelPrize.org. Retrieved 2007-01-02.
  4. Prusiner S. B. (1982). "Novel proteinaceous infectious particles cause scrapie". Science. 216 (4542): 136–144. Bibcode:1982Sci...216..136P. doi:10.1126/science.6801762. PMID 6801762.
  5. Prusiner S. B. (1991). "Molecular biology of prion diseases". Science. 252 (5012): 1515–1522. Bibcode:1991Sci...252.1515P. doi:10.1126/science.1675487. PMID 1675487.
  6. UCSF Prusiner Lab site
  7. "What really causes mad cow disease?". Wired. January 31, 2007. Retrieved 2007-01-02.
  8. "Fellowship of the Royal Society 1660-2015". Royal Society. Archived from the original on 2015-07-15.
  9. Prusiner's Nobel Prize page
  10. "Franklin Laureate Database - Benjamin Franklin Medal 1998 Laureates". Franklin Institute. Retrieved 2013-02-14.
  11. http://www.nsf.gov/news/news_summ.jsp?cntn_id=117875
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