This paper describes the isolation as well as the biochemical and molecular characterization of ERAP1 and demonstrates its functional importance for the trimming of N-terminally elongated epitopes.

First two reports of the discovery of the ER aminopeptidase that trims antigenic peptides.

The demonstration that N-terminal trimming occurs in the endoplasmic reticulum and is carried out by an aminopeptidase.

This paper shows that efficient epitope trimming does not require the presence of MHC class I proteins.

First paper to provide evidence that TPPII shows endoproteolytic activity and suggest that TPPII acts downstream of the proteasome.

The discovery of proteolytic intermediates in the antigen-processing pathway. Peptides have variable N-terminal extensions that need further trimming in the endoplasmic reticulum.

This study shows that presence of MHC class I molecules is essential for detecting the presence of antigenic peptides in cell extracts. The discovery posed an enigma for the mechanisms of peptide generation, which were thought to occur solely in the cytoplasm. The authors predicted the presence of peptide-trimming enzymes in the endoplasmic reticulum.