Avram Hershko Explained
Avram Hershko (Hebrew: אברהם הרשקו|Avraham Hershko, Hungarian: Herskó Ferenc Ábrahám;[1] born December 31, 1937) is a Hungarian-Israeli biochemist who received the Nobel Prize in Chemistry in 2004.
Biography
He was born Herskó Ferenc in Karcag, Hungary, into a Jewish family,[2] the son of Shoshana/Margit 'Manci' (née Wulc) and Moshe Hershko, both teachers.[3] During the Second World War, his father was forced into labor service in the Hungarian army and then taken as a prisoner by the Soviet Army. For years, Avram's family didn't known anything about what had happened to his father. Avram, his mother and older brother Chaim/Laszlo 'Laci' were put in a ghetto in Szolnok. During the final days of the ghetto, most Jews were sent to be murdered in Auschwitz, but Avram and his family managed to board trains that took them to a concentration camp in Austria, where they were forced into labor until the end of the war. Avram and his mother and brother survived the war and returned to their home. His father returned as well, 4 years after they had last seen him.[4]
Hershko and his family emigrated to Israel in 1950 and settled in Jerusalem. He received his MD in 1965 and his PhD in 1969 from the Hebrew University of Jerusalem-Hadassah Medical Center. He was a postdoctoral scholar at the University of California, San Francisco. He is currently a Distinguished Professor at the Rappaport Faculty of Medicine at the Technion in Haifa and a Distinguished Adjunct Professor at the New York University Grossman School of Medicine.
Along with Aaron Ciechanover and Irwin Rose, he was awarded the 2004 Nobel Prize in Chemistry for the discovery of ubiquitin-mediated protein degradation. The ubiquitin-proteasome system has a critical role in maintaining the homeostasis of cells and is believed to be involved in the development and progression of diseases such as cancer, muscular and neurological diseases, and immune and inflammatory responses.
His contributions to science directly helped cure one of his long-time friends of cancer.[5]
Honours and awards
Publications
- Hershko . A. . Ciechanover . A. . Heller . H. . Haas . A. L. . Rose . I. A. . Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. . Proceedings of the National Academy of Sciences . 77 . 4 . April 1, 1980 . 0027-8424 . 10.1073/pnas.77.4.1783 . 1783–1786. 6990414 . 348591 . 1980PNAS...77.1783H . free .
- Hershko . A . Heller . H . Elias . S . Ciechanover . A . Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. . The Journal of Biological Chemistry . 258 . 13 . July 10, 1983 . 0021-9258 . 6305978 . 8206–14. 10.1016/S0021-9258(20)82050-X . free .
- Hershko . A. . Leshinsky . E. . Ganoth . D. . Heller . H. . ATP-dependent degradation of ubiquitin-protein conjugates. . Proceedings of the National Academy of Sciences . 81 . 6 . March 1, 1984 . 0027-8424 . 10.1073/pnas.81.6.1619 . 1619–1623. 6324208 . 344969 . 1984PNAS...81.1619H . free .
- Hershko . A . Heller . H . Eytan . E . Reiss . Y . The protein substrate binding site of the ubiquitin-protein ligase system. . Journal of Biological Chemistry . Elsevier BV . 261 . 26 . 1986 . 0021-9258 . 10.1016/s0021-9258(18)67192-3 . 11992–11999. 3017957 . free .
- Ganoth . D . Leshinsky . E . Eytan . E . Hershko . A . A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation. . The Journal of Biological Chemistry . 263 . 25 . September 5, 1988 . 0021-9258 . 2842333 . 12412–9. 10.1016/S0021-9258(18)37771-8 . free .
- Sudakin . V . Ganoth . D . Dahan . A . Heller . H . Hershko . J . Luca . F C . Ruderman . J V . Hershko . A . The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. . Molecular Biology of the Cell . American Society for Cell Biology (ASCB) . 6 . 2 . 1995 . 1059-1524 . 7787245 . 275828 . 10.1091/mbc.6.2.185 . 185–197.
Involvement with biotechnology
Hershko serves on the Scientific Advisory Board of Oramed Pharmaceuticals.[10]
See also
External links
Notes and References
- Web site: Hungary's Nobel Prize Winners. www.mta.hu. September 22, 2021. dead. https://web.archive.org/web/20151006113721/http://mta.hu/articles/hungarys_nobel_prize_winners__25577. October 6, 2015.
- Web site: JINFO . Jewish Nobel Prize Winners in Chemistry . March 30, 2023 . www.jinfo.org.
- including the Nobel Lecture The Ubiquitin System for Protein Degradation and some of its Roles in the Control of the Cell Division Cycle
- Web site: אברהם הרשקו.
- Web site: Nobel Prize winner's discovery helps save longtime physician friend . https://archive.today/20120913041804/http://www.phillyburbs.com/news/local/burlington_county_times_news/nobel-prize-winner-s-discovery-helps-save-longtime-physician-friend/article_9ad53d9b-22f5-5fec-8956-92a7aae6a009.html . dead . September 13, 2012 . September 13, 2011 . Sally . Friedman . . phillyBurbs.com . May 15, 2012 .
- Web site: Israel Prize Official Site – Recipients in 1994 . dead . https://web.archive.org/web/20081227153428/http://cms.education.gov.il/EducationCMS/Units/PrasIsrael/TashnagTashsab/TASNAG_TASNAT_Rikuz.htm?DictionaryKey=Tashnad . December 27, 2008 . hebrew .
- Web site: Wolf Prize Recipients in Medicine . https://web.archive.org/web/20090226015735/http://www.wolffund.org.il/cat.asp?id=24&cat_title=MEDICINE . February 26, 2009.
- Web site: Two Israeli Scientists Have Won The Nobel Prize In Chemistry . isracast.com . Iddo Genuth . July 29, 2005 . https://web.archive.org/web/20051219160839/http://www.isracast.com/tech_news/101004_tech.htm . December 19, 2005.
- Web site: APS Member History. June 8, 2021. search.amphilsoc.org.
- Web site: Nobel Laureate, Oramed SAB member Prof. Avram Hershko and Oramed CSO Dr. Miriam Kidron to be Featured on Biotalknology Webinar "Oral Delivery of Therapeutic Proteins – Oramed Story" on November 18, 2020 . Oramed Pharmaceuticals . November 18, 2020 . July 15, 2023.