한빛사 논문
Shashikanth M. Sriram1, Bo Yeon Kim2 & Yong Tae Kwon1,3,*
1.Center for Pharmacogenetics and Department of Pharmaceutical Sciences, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
2.World Class Institute (WCI), Chemical Biology Research Center, Korea Research Institute of Bioscience & Biotechnology, Ochang 363-883, Republic of Korea.
3.World Class University (WCU) Program, Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology and College of Medicine, Seoul National University, Seoul 110-799, Republic of Korea.
* Correspondence to: Yong Tae Kwon
Abstract
The N-end rule defines the protein-destabilizing activity of a given amino-terminal residue and its post-translational modification. Since its discovery 25 years ago, the pathway involved in the N-end rule has been thought to target only a limited set of specific substrates of the ubiquitin-proteasome system. Recent studies have provided insights into the components, substrates, functions and structural basis of substrate recognition. The N-end rule pathway is now emerging as a major cellular proteolytic system, in which the majority of proteins are born with or acquire specific N-terminal degradation determinants through protein-specific or global post-translational modifications.
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