2026-06-15T11:35:13Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/106552025-05-26T13:27:45Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Samino, Yolanda author Lorente, Elena author Jimenez, Mercedes author Garcia, Ruth author Val, Margarita del author Lopez, Daniel author Infantes, Susana author 2010-04-01 In the classical MHC class I Ag presentation pathway, antigenic peptides derived from viral proteins by multiple proteolytic cleavages are transported to the endoplasmic reticulum lumen and are then exposed to ami-nopeptidase activity. In the current study, a long MHC class I natural ligand recognized by cytotoxic T lymphocytes was used to study the kinetics of degradation by aminopeptidase. The in vitro data indicate that this N-extended peptide is efficiently trimmed to a 9-mer, unless its binding to the MHC molecules protects the full-length peptide. J Immunol . 2010 Apr 1;184(7):3351-5. 10.4049/jimmunol.0901560 1550-6606 0022-1767 Journal of immunology (Baltimore, Md. : 1950) 20200278 http://hdl.handle.net/20.500.12105/10655 H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processing