Irwin Rose, c. 2000
Irwin Allan Rose
July 16, 1926
Brooklyn, New York, U.S.
|Died||June 2, 2015 88) (aged|
Deerfield, Massachusetts, U.S.
|Alma mater||University of Chicago (BS, PhD) NYU (postdoc)|
|Known for||Ubiquitin-mediated protein degradation|
|Spouse(s)||Zelda Budenstein[ citation needed ]|
|Children||4[ citation needed ]|
|Awards||Nobel Prize in Chemistry (2004)|
Irwin Allan Rose (July 16, 1926 – June 2, 2015) was an American biologist. Along with Aaron Ciechanover and Avram Hershko, he was awarded the 2004 Nobel Prize in Chemistry for the discovery of ubiquitin-mediated protein degradation.
Biology is the natural science that studies life and living organisms, including their physical structure, chemical processes, molecular interactions, physiological mechanisms, development and evolution. Despite the complexity of the science, there are certain unifying concepts that consolidate it into a single, coherent field. Biology recognizes the cell as the basic unit of life, genes as the basic unit of heredity, and evolution as the engine that propels the creation and extinction of species. Living organisms are open systems that survive by transforming energy and decreasing their local entropy to maintain a stable and vital condition defined as homeostasis.
Aaron Ciechanover is an Israeli biologist, who won the Nobel prize in Chemistry for characterizing the method that cells use to degrade and recycle proteins using ubiquitin.
Avram Hershko is a Hungarian-born Israeli biochemist and Nobel laureate in Chemistry.
Rose was born in Brooklyn, New York, into a secular Jewish family, the son of Ella (Greenwald) and Harry Royze, who owned a flooring store.Rose attended Washington State University for one year prior to serving in the Navy during World War II. Upon returning from the war he received his Bachelor of Science degree in 1948 and his PhD in biochemistry in 1952, both from the University of Chicago. He did his post-doctoral studies at NYU.
Washington State University is a public research university in Pullman, Washington. Founded in 1890, WSU is one of the oldest land-grant universities in the American West and features programs in a broad range of academic disciplines. With an undergraduate enrollment of 24,470 and a total enrollment of 29,686, it is the second largest institution of higher education in Washington state behind the University of Washington. The WSU Pullman campus is perched upon a hill, characterized by open spaces, views, deep green conifers, and a restrained red brick and basalt material palette--materials originally found on site. The university is nestled within the spectacular rolling topography of the Palouse in rural eastern Washington and remains intimately connected to the town, the region, and the landscape in which it sits.
A Bachelor of Science is an undergraduate academic degree awarded for completed courses that generally last three to five years, or a person holding such a degree.
The University of Chicago is a private research university in Chicago, Illinois. Founded in 1890, the school is located on a 217-acre campus in Chicago's Hyde Park neighborhood, near Lake Michigan. The University of Chicago holds top-ten positions in various national and international rankings.
Rose served on the faculty of Yale School of Medicine's department of biochemistry from 1954 to 1963. He then joined the Fox Chase Cancer Center in 1963 and stayed there until he retired in 1995.He joined University of Pennsylvania during the 1970s and served as a Professor of Physical Biochemistry. He was a distinguished professor-in-residence in the Department of Physiology and Biophysics at the University of California, Irvine School of Medicine at the time his Nobel Prize was announced in 2004.
The Yale School of Medicine is the graduate medical school at Yale University in New Haven, Connecticut. It was founded in 1810 as The Medical Institution of Yale College, and formally opened in 1813.
Fox Chase Cancer Center is a National Cancer Institute-designated Comprehensive Cancer Center research facility and hospital located in the Fox Chase section of Philadelphia, Pennsylvania, United States. The main facilities of the center are located on property adjoining Burholme Park. The center is part of the Temple University Health System (TUHS) and specializes in the treatment and prevention of cancer.
The University of Pennsylvania is a private Ivy League research university in Philadelphia, Pennsylvania. It is one of the nine colonial colleges founded prior to the Declaration of Independence and the first institution of higher learning in the United States to refer to itself as a university. Benjamin Franklin, Penn's founder and first president, advocated an educational program that trained leaders in commerce, government, and public service, similar to a modern liberal arts curriculum.
Irwin (Ernie) trained several postdoctoral research fellows while at the Fox Chase Cancer Center in Philadelphia. These included Art Haas,the first to see Ubiquitin chains, Keith Wilkinson, the one to first identify APF-1 as Ubiquitin, and Cecile Pickart, a world class enzymologist in many parts of the Ub system.
Rose was awarded the Nobel prize in 2004.
Rose was married to Zelda Budenstein and had four children.He died on June 2, 2015 at Deerfield, Massachusetts. His wife died in 2016.
Deerfield is a town in Franklin County, Massachusetts, United States. Settled near the Connecticut River in the 17th century during the colonial era, the population was 5,125 as of the 2010 census. Deerfield is part of the Springfield, Massachusetts Metropolitan Statistical Area in western Massachusetts, lying 30 miles (48 km) north of the city of Springfield.
Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases.
Ubiquitin is a small regulatory protein found in most tissues of eukaryotic organisms, i.e. it occurs ubiquitously. It was discovered in 1975 by Gideon Goldstein and further characterized throughout the 1970s and 1980s. Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A.
Paul Delos Boyer was an American biochemist, analytical chemist, and a professor of chemistry at University of California Los Angeles (UCLA). He shared the 1997 Nobel Prize in Chemistry for research on the "enzymatic mechanism underlying the biosynthesis of adenosine triphosphate (ATP)" with John E. Walker, making Boyer the first Utah-born Nobel laureate; the remainder of the Prize in that year was awarded to Danish chemist Jens Christian Skou for his discovery of the Na+/K+-ATPase.
A ubiquitin ligase is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. The ubiquitin is attached to a lysine on the target protein by an isopeptide bond. E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the proteasome. However, many other types of linkages are possible and alter a protein's activity, interactions, or localization. Ubiquitination by E3 ligases regulates diverse areas such as cell trafficking, DNA repair, and signaling and is of profound importance in cell biology. E3 ligases are also key players in cell cycle control, mediating the degradation of cyclins, as well as cyclin dependent kinase inhibitor proteins. The human genome encodes over 600 putative E3 ligases, allowing for tremendous diversity in substrates.
Mouse double minute 2 homolog (MDM2) also known as E3 ubiquitin-protein ligase Mdm2 is a protein that in humans is encoded by the MDM2 gene. Mdm2 is an important negative regulator of the p53 tumor suppressor. Mdm2 protein functions both as an E3 ubiquitin ligase that recognizes the N-terminal trans-activation domain (TAD) of the p53 tumor suppressor and as an inhibitor of p53 transcriptional activation.
S-phase kinase-associated protein 2 is an enzyme that in humans is encoded by the SKP2 gene.
Transitional endoplasmic reticulum ATPase also known as valosin-containing protein (VCP) or p97 in mammals and CDC48 in S. Cerevisiae, is an enzyme that in humans is encoded by the VCP gene. The TER ATPase is an ATPase enzyme present in all eukaryotes and archaebacteria. Its main function is to segregate protein molecules from large cellular structures such as protein assemblies, organelle membranes and chromatin, and thus facilitate the degradation of released polypeptides by the multi-subunit protease proteasome.
F-box/WD repeat-containing protein 1A (FBXW1A) also known as βTrCP1 or Fbxw1 or hsSlimb or pIkappaBalpha-E3 receptor subunit is a protein that in humans is encoded by the BTRC gene.
STUB1 is a human gene that codes for the protein CHIP.
F-box/WD repeat-containing protein 7 is a protein that in humans is encoded by the FBXW7 gene.
Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.
Ubiquitin-conjugating enzyme E2 D3 is a protein that in humans is encoded by the UBE2D3 gene.
Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene.
Autophagy related 7 is a protein in humans encoded by ATG7 gene. Related to GSA7; APG7L; APG7-LIKE.
Prokaryotic ubiquitin-like protein (Pup) is a functional analog of ubiquitin found in the prokaryote Mycobacterium tuberculosis. Modification with Pup is called pupylation. Pup serves the same function as ubiquitin, although the enzymology of ubiquitylation and pupylation is different. In contrast to the three-step reaction of ubiquitylation, pupylation requires two steps, therefore only two enzymes are involved in pupylation. Similar to ubiquitin, Pup attaches to specific lysine residues of substrate proteins by forming isopeptide bonds. It is then recognized by Mycobacterium proteasomal ATPase (Mpa) by a binding-induced folding mechanism that forms a unique alpha-helix. Mpa then delivers the Pup-substrate to the 20S proteasome by coupling of ATP hydrolysis for proteasomal degradation.
Yoshinori Ohsumi is a Japanese cell biologist specializing in autophagy, the process that cells use to destroy and recycle cellular components. Ohsumi is a professor at Tokyo Institute of Technology's Institute of Innovative Research. He received the Kyoto Prize for Basic Sciences in 2012, the 2016 Nobel Prize in Physiology or Medicine, and the 2017 Breakthrough Prize in Life Sciences for his discoveries of mechanisms for autophagy.
Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in a cell, usually with a regulatory function. The UBL protein family derives its name from the first member of the class to be discovered, ubiquitin (Ub), best known for its role in regulating protein degradation through covalent modification of other proteins. Following the discovery of ubiquitin, many additional evolutionarily related members of the group were described, involving parallel regulatory processes and similar chemistry. UBLs are involved in a widely varying array of cellular functions including autophagy, protein trafficking, inflammation and immune responses, transcription, DNA repair, RNA splicing, and cellular differentiation.
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