The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones Carla Marques * ,† , 1 , Weimin Guo * , 1 , Paulo Pereira † , Allen Taylor * , Cam Patterson ‡ , Paul C. Evans § and Fu Shang * ,2 * Human Nutrition Research Center on Aging, Tufts University, Boston, Massachusetts, USA; † Center of Ophthalmology, IBILI, Faculty of Medicine, University of Coimbra, Coimbra, Portugal; ‡ Carolina Cardiovascular Biology Center, University of North Carolina, Chapel Hill, Chapel Hill, North Carolina, USA; and § BHF Cardiovascular Medicine, Imperial College, London, UK 2 Correspondence: Jean Mayer USDA Human Nutrition Research Center on Aging, Tufts University, Boston, MA 02111, USA. E-mail: fu.shang@tufts.edu <h3>SPECIFIC AIMS</h3> Accumulation of damaged or abnormal proteins is associated with various age-related diseases, so prompt repair and/or removal of damaged proteins are essential for the survival of cells and the health of organisms. The ubiquitin-proteasome pathway (UPP) plays a role in selective degradation of damaged or abnormal proteins, whereas molecular chaperones such as heat shock proteins are involved in refolding of denatured proteins. The specific aims of this work were to elucidate the mechanism of recognition of damaged proteins
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