Biography:Stanley B. Prusiner

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Short description: American neurologist and biochemist
Stanley Prusiner
Prusiner 1.JPG
Prusiner in 2007
Born
Stanley Ben Prusiner

(1942-05-28) May 28, 1942 (age 82)
Des Moines, Iowa, United States
NationalityAmerican
Alma materUniversity of Pennsylvania (BA, MD)
Known for
Spouse(s)Sandy Turk Prusiner[1]
Childrentwo[1]
Awards
  • Potamkin Prize (1991)
  • Metlife Foundation Award for Medical Research in Alzheimer's Disease (1991)[2]
  • Dickson Prize (1993)
  • Richard Lounsbery Award (1993)
  • Lasker Award (1994)
  • Keio Medical Science Prize (1996)
  • Nobel Prize in Physiology or Medicine (1997)
  • ForMemRS (1997)[3]
  • Sir Hans Krebs Medal (1999)
Scientific career
Fields
Institutions
Websiteind.ucsf.edu/ind/aboutus/faculty/prusiners

Stanley Ben Prusiner (born May 28, 1942[1]) is an American neurologist and biochemist. He is the director of the Institute for Neurodegenerative Diseases at University of California, San Francisco (UCSF).[4] Prusiner discovered prions, a class of infectious self-reproducing pathogens primarily or solely composed of protein, considered by many as a heretical idea when first proposed. 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 (David E. Garfin,[5] D. P. Stites, W. J. Hadlow, C. M. Eklund) beginning in the early 1970s.[6][7]

Early life, career and research

He was born in Des Moines, Iowa, into a Jewish[8] family to 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 Arts degree in chemistry from the University of Pennsylvania and later received his M.D. from the University of Pennsylvania School of Medicine.[1] 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.[citation needed]

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.[citation needed]

Since 1999, Prusiner has been director of the Institute for Neurodegenerative Diseases research laboratory at UCSF, working on prion disease, Alzheimer's disease and tauopathies.[9]

Prion: A heretical idea

In his 1998 PNAS review article on Prions, Prusiner wrote: "The idea that scrapie prions were composed of an amyloidogenic protein was truly heretical when it was introduced." Encephalopathy was a myterious disease that attacks the brain, and leaves the brains of its victims full of holes. Scientists did not know what pathogen or disease-causing organism that produced such pattern. Prusiner and his co-workers suggested "One scientific theory, viewed as heretical in that it seems to challenge the role of nucleic acids as the exclusive carriers of genetic information." This theory suggested that this pathogen might be a "deadly variety of a normal protein that has the ability to amplify itself in the brain. The hypothetical protein is called a prion (pronounced PREE-on)."[10][11][12]

Awards and honors

Stanley 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.[1] 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.[13]

Prusiner was elected to the National Academy of Science in 1992 and to its governing council in 2007.[14] He is also an elected member of the American Academy of Arts and Sciences (1993),[15] a Foreign Member of the Royal Society (ForMemRS) in 1997,[3][16] and the American Philosophical Society (1998),[17] the Serbian Academy of Sciences and Arts (2003), and the Institute of Medicine.


  • Potamkin Prize for Alzheimer's Disease Research from the American Academy of Neurology (1991)
  • The Richard Lounsbery Award for Extraordinary Scientific Research in Biology and Medicine from the National Academy of Sciences (1993)
  • Dickson Prize (1993)
  • The Gairdner Foundation International Award (1993)
  • The Albert Lasker Award for Basic Medical Research (1994)
  • The Paul Ehrlich and Ludwig Darmstaedter Prize from the Federal Republic of Germany (1995)
  • The Wolf Prize in Medicine from the Wolf Foundation/State of Israel (1996)
  • Grand Prix Charles-Leopold Mayer (1996)
  • The Keio International Award for Medical Science (1996)
  • Golden Plate Award of the American Academy of Achievement (1996)[18]
  • The Louisa Gross Horwitz Prize from Columbia University (1997)
  • The Nobel Prize in Physiology or Medicine (1997)[1]
  • The Benjamin Franklin Medal from the Franklin Institute (1998)[19]
  • Honorary Doctorate from CEU Cardinal Herrera University (2005)
  • The National Medal of Science (2010)[20]


See also

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Miss nobel-id as parameter
  2. ↑ "MetLife Foundation Awards for Medical Research in Alzheimer's Disease". http://mlfawards.afar.org/docs/2016Edition_MetLifeFoundationAwards_PastWinners.pdf. 
  3. ↑ 3.0 3.1 "Fellows of the Royal Society". London: Royal Society. https://royalsociety.org/about-us/fellowship/fellows/. 
  4. ↑ Stanley Prusiner on ResearchGate
  5. ↑ AES 2013: Annual Meeting of the AES Electrophoresis Society
  6. ↑ Prusiner S. B. (1982). "Novel proteinaceous infectious particles cause scrapie". Science 216 (4542): 136–144. doi:10.1126/science.6801762. PMID 6801762. Bibcode: 1982Sci...216..136P. 
  7. ↑ Prusiner S. B. (1991). "Molecular biology of prion diseases". Science 252 (5012): 1515–1522. doi:10.1126/science.1675487. PMID 1675487. Bibcode: 1991Sci...252.1515P. 
  8. ↑ "Jewish Nobel Prize Winners in Medicine". https://www.jinfo.org/Nobels_Medicine.html. 
  9. ↑ "UCSF - Prusiner Laboratory - Stanley B. Prusiner, M.D.". 28 August 2008. http://prusinerlab.ucsf.edu/people/director.php. 
  10. ↑ Stanley Prusiner (1998-11-10). "Prions". https://www.pnas.org/doi/full/10.1073/pnas.95.23.13363. 
  11. ↑ Sandra Blakeslee (October 8, 1991). "Heretical Theory On Brain Diseases Gains New Ground". https://www.nytimes.com/1991/10/08/science/heretical-theory-on-brain-diseases-gains-new-ground.html. 
  12. ↑ "Stanley B. Prusiner, M.D.". Boston University, Amyloidosis Center. https://www.bu.edu/amyloid/events/prusiner-bio/. 
  13. ↑ "What really causes mad cow disease?". Wired. January 31, 2007. http://blog.wired.com/wiredscience/2007/01/what_really_cau.html. Retrieved 2007-01-02. 
  14. ↑ "Stanley B. Prusiner". http://www.nasonline.org/member-directory/members/61615.html. 
  15. ↑ "Stanley Ben Prusiner" (in en). https://www.amacad.org/person/stanley-ben-prusiner. 
  16. ↑ "Fellowship of the Royal Society 1660-2015". Royal Society. https://docs.google.com/spreadsheets/d/1RVVZY00MZNrK2YCTTzVrbTFH2t3RxoAZah128gQR-NM/pubhtml. 
  17. ↑ "APS Member History". https://search.amphilsoc.org/memhist/search?creator=Stanley+B.+Prusiner&title=&subject=&subdiv=&mem=&year=&year-max=&dead=&keyword=&smode=advanced. 
  18. ↑ "Golden Plate Awardees of the American Academy of Achievement". American Academy of Achievement. https://achievement.org/our-history/golden-plate-awards/#science-exploration. 
  19. ↑ "Franklin Laureate Database - Benjamin Franklin Medal 1998 Laureates". Franklin Institute. http://www.fi.edu/winners/show_results.faw?gs=&ln=&fn=&keyword=&subject=&award=BF+&sy=1997&ey=1999&name=Submit. 
  20. ↑ "White House Announces National Medal of Science Laureates - NSF - National Science Foundation". https://www.nsf.gov/news/news_summ.jsp?cntn_id=117875. 

External links

  • Miss nobel-id as parameter



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