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 The ubiquitin system for protein degradation and some of its roles in the control  of the cell division cycle Hershko ACell Death Differ  2005[Sep]; 12 (9): 1191-7Owing to the intensive research activity on protein synthesis, little attention  was paid in the 1950s and 1960s to protein degradation. However, work by my group  and others between 1970 and 1990 led to the identification of the  ubiquitin-dependent degradation system. We found that this system contains three  types of enzymes: E1 ubiquitin--activating enzyme, E2 ubiquitin--carrier enzyme  and E3 ubiquitin--protein ligase. The sequential action of these enzymes leads to  conjugation of ubiquitin to proteins and then in most cases to their degradation.  This review briefly tells the story of how this pathway was discovered describing  the main findings that during the years allowed us to draw the complex picture we  have now.|Anaphase-Promoting Complex-Cyclosome[MESH]|Animals[MESH]|Biochemistry/*history[MESH]|Carrier Proteins/chemistry[MESH]|Cell Division[MESH]|History, 20th Century[MESH]|Humans[MESH]|Models, Biological[MESH]|Muramidase/chemistry[MESH]|Proteasome Endopeptidase Complex/chemistry[MESH]|Proteins/metabolism[MESH]|Time Factors[MESH]|Ubiquitin-Activating Enzymes/metabolism[MESH]|Ubiquitin-Protein Ligase Complexes/metabolism[MESH]|Ubiquitin-Protein Ligases/chemistry[MESH]|Ubiquitin/*chemistry/metabolism[MESH]
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