Irwin Rose
Irwin Rose (1926–2015) was an American biochemist who shared the 2004 Nobel Prize in Chemistry for discovering ubiquitin-mediated protein degradation.
Aaron Ciechanover: An Israeli biochemist who shared the 2004 Nobel Prize in Chemistry for discovering ubiquitin-mediated protein degradation. Ciechanover collaborated with Rose and Avram Hershko to establish the ubiquitin pathway.
Ubiquitin-activating enzyme: An enzyme, also called E1, that uses ATP to activate ubiquitin for transfer in the ubiquitination cascade. Rose’s experiments helped reveal the ATP-dependent step that activates ubiquitin.
Proteostasis: The cellular processes that maintain a functional balance of protein synthesis, folding, localization, and degradation. Ubiquitin-mediated degradation is one major arm of the protein quality-control system.
Protein degradation: The cellular breakdown of proteins into smaller peptides or amino acids. Rose’s work explained a selective, ATP-dependent route within this broader process.
Avram Hershko: An Israeli biochemist who shared the 2004 Nobel Prize in Chemistry for discovering ubiquitin-mediated protein degradation. Hershko’s collaboration with Rose and Ciechanover produced the central discoveries recognized by the Nobel Prize.
Ubiquitin-conjugating enzyme: An enzyme, also called E2, that carries activated ubiquitin and transfers it to a target protein. E2 enzymes participate in the cascade Rose and colleagues characterized.
Cell cycle: The ordered series of events through which a cell grows, replicates its DNA, and divides. Selective protein destruction helps control the timing and direction of cell-cycle transitions.
Radioimmunoassay: A laboratory method that measures substances using antibodies and radioactive tracers. Hershko and colleagues used this technique to track a protein factor later identified as ubiquitin.
University of Pennsylvania: A private research university in Philadelphia, Pennsylvania, founded in 1740. Rose conducted much of his foundational research on protein degradation at Penn.
Ubiquitin ligase: An enzyme, also called E3, that helps attach ubiquitin to selected target proteins. Target selection by E3 enzymes explains how ubiquitin-mediated degradation can be selective.