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Chemistry Nobel Laureate Irwin Rose Dies

Biochemist shared 2004 prize for work on regulated protein degradation

by Jyllian Kemsley
June 4, 2015 | A version of this story appeared in Volume 93, Issue 23

Credit: Paul R. Kennedy
Photograph of Irwin Rose.
Credit: Paul R. Kennedy

Biochemist Irwin (Ernie) Rose, who shared the 2004 Nobel Prize in Chemistry for research on regulated protein degradation, died on June 2 at age 88.

Rose spent much of his career as a research scientist at the Fox Chase Cancer Center in Philadelphia. There, he collaborated with fellow Nobel Prize winners Aaron Ciechanover and Avram Hershko of Technion—Israel Institute of Technology.

Starting in the 1970s, the trio identified the small regulatory polypeptide, now known as ubiquitin, that cells attach to other proteins to label them for degradation by a protease. The researchers went on to discover more proteins that activate ubiquitin and add it to targets.

At the time of this research, attaching ubiquitin to a protein represented a new kind of posttranslational modification. “With his deep knowledge and ability to think far out of the box, Ernie was able to take us out of the swamp where we were drowning” to discover the mechanism of ubiquitin tagging, Ciechanover says.

Rose “also contributed enormously to our understanding of enzyme function in general, creating novel methodologies and new ways of thinking about reaction mechanisms,” says Judith P. Klinman, a chemistry professor at the University of California, Berkeley. Klinman worked with Rose as a postdoctoral researcher and later as a colleague at Fox Chase.

Adds Klinman, “He was a formidable example of how to pursue basic research with curiosity, integrity, and a fierce determination to uncover the ‘truth’ behind the question at hand.”


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