Aaron Ciechanover Research Articles

The Nobel Prize in Chemistry 2004

The Nobel Prize in Chemistry for 2004 is shared by Aaron Ciechanover, Avram Hershko and Irwin Rose, who made fundamental discoveries concerning how cells regulate the breakdown of cellular proteins with extreme specificity. The three biochemists discovered ubiquitin-mediated proteolysis, a process where an enzyme system tags unwanted proteins with many molecules of a small protein called ubiquitin and then sends then to the proteasome where they are broken down.

Websites of note

Websites of note

The Ubiquitin-Proteasome Pathway and Plant Development

The importance of the ubiquitin-proteasome pathway to cellular regulation in eukaryotes has become increasingly apparent during the last several years. This fact was formally acknowledged recently by the awarding of the 2004 Nobel Prize in Chemistry to Aaron Ciechanover, Avram Hershko, and Irwin

Varshavsky's Contributions

We are writing to express our enthusiasm that the discovery of the ubiquitin conjugation system has been acknowledged with the award of the Nobel Prize in Chemistry to three outstanding biochemists: Avram Hershko and Aaron Ciechanover of the Technion Institute in Israel, and Irwin Rose of the University of California at Irvine (“Gold medal from cellular trash,” G. Vogel, News Focus, 15 Oct., p. 400). Unraveling the chemistry that underlies the attachment of ubiquitin to proteins that are destined to be degraded was a magnificent achievement and is fully deserving of this recognition.

The 'kiss of death' prize

Aaron Ciechanover, Avram Hershko and Irwin Rose have been awarded the Nobel Prize in Chemistry 2004 for ...helping to understand how the human body gives the 'kiss of death' to rogue proteins to defend itself from diseases like cancer (Reuters, 6 October 2004).

Ubiquitin-mediated degradation of cellular proteins in health and disease

HepatologyVolume 35, Issue 1 p. 3-6 Science FrontierFree Access Ubiquitin-mediated degradation of cellular proteins in health and disease Aaron Ciechanover M.D., Ph.D., Corresponding Author Aaron Ciechanover M.D., Ph.D. c_tzachy@netvision.net.il mdaaron@tx.technion.ac.il Department of Biochemistry, The Bruce Rappaport Faculty of Medicine and the Rappaport Family Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa, IsraelDepartment of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology, Efron Street, Bat Galim, Haifa 31096, Israel. fax: (972) 4-851-3922.===Search for more papers by this authorAlan L. Schwartz, Alan L. Schwartz Departments of Pediatrics and Molecular Biology and Pharmacology, St. Louis Children' Hospital and Washington University School of Medicine, St. Louis, MOSearch for more papers by this author Aaron Ciechanover M.D., Ph.D., Corresponding Author Aaron Ciechanover M.D., Ph.D. c_tzachy@netvision.net.il mdaaron@tx.technion.ac.il Department of Biochemistry, The Bruce Rappaport Faculty of Medicine and the Rappaport Family Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa, IsraelDepartment of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology, Efron Street, Bat Galim, Haifa 31096, Israel. fax: (972) 4-851-3922.===Search for more papers by this authorAlan L. Schwartz, Alan L. Schwartz Departments of Pediatrics and Molecular Biology and Pharmacology, St. Louis Children' Hospital and Washington University School of Medicine, St. Louis, MOSearch for more papers by this author First published: 30 December 2003 https://doi.org/10.1053/jhep.2002.30316Citations: 55AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume35, Issue1January 2002Pages 3-6 ReferencesRelatedInformation

Regulation of the G1 to S transition by the ubiquitin pathway

This year the most prestigious prize in medical sciences, the Lasker Award, has been presented to the three scientists who discovered the ubiquitin pathway: Aaron Ciechanover, Avram Hershko, and Alexander Varshavsky [Nature Med. 6 (2000) 1073–1081]. During a time when the scientific community was focused on understanding how proteins were synthesized, they intently pursued the novel idea that cells were programmed to selectively destroy proteins. Their work led to the identification of an elaborate system of protein degradation targeting a myriad of cellular substrates. A small protein called ubiquitin is at the center of this process. Although the ubiquitin pathway was first described in the early 1980s, it has only more recently advanced to the forefront of basic research as a significant regulatory network within the cell. The field continues to grow as new ubiquitination enzymes and novel functions of this system are identified. Scientists are focused on elucidating the mechanisms by which cells deploy the ubiquitin pathway to control levels of selected proteins, such as cell cycle regulatory proteins, transcription factors and signaling molecules. Accelerated or decelerated rates of degradation of particular substrates participate in the genesis of many human diseases. Thus, understanding the mechanisms that confer specificity to the ubiquitin system will allow the development of novel therapeutic approaches to target aberrations in this pathway underlying tumorigenesis and other human pathologies.

The meteoric rise of regulated intracellular proteolysis.

It is often the case in biology that research into breaking things down lags behind research into synthesizing them, and this is certainly true for intracellular proteolysis. Now that we recognize that intracellular proteolysis, triggered by attaching multiple copies of a small protein called ubiquitin to target proteins, is fundamental to life, it is hard to believe that 20 years ago this field was little more than a backwater of biochemistry studied by a handful of laboratories. Among the few were Avram Hershko, Aaron Ciechanover and Alexander Varshavsky, who were recently awarded the Albert Lasker award for basic medical research for discovering the importance of protein degradation in cellular physiology. This Timeline traces how they and their collaborators triggered the rapid movement of ubiquitin-mediated proteolysis to centre stage.