ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum

By T. Serwold, F. Gonzalez, Jennifer Kim, Richard Jacob, N. Shastri. Nature, 2002

711 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e307d6fea5f423662aaff96c0f28ecb329d3043c

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In Immunology

1. Pedro A. Reche
2. Hong Zhang
3. Ellis L. Reinherz
4. John-Paul Glutting
5. K. Rock
6. Fang Zhou

In Molecular Biology

1. Pedro A. Reche
2. Hong Zhang
3. Ellis L. Reinherz
4. John-Paul Glutting
5. K. Rock
6. P. Wearsch
7. Manoj Bhasin
8. Gajendra P. Raghava

Citations in the corpus

• MHC-guided processing: binding of large antigen fragments (2003, background): “; the ER aminopeptidase that concludes the processing has recently been identifie”
• Pathways of Antigen Processing (2013, background): “One other ER luminal component that is critically important for the proper generation of MHC-I-peptide complexes is an aminopeptidase, in the mouse called ER Aminopeptidase associated with Antigen Processing (ERAAP) and in humans called ER Aminopeptidase-1 (ERAP1) (Figure 3) (38, 39).”
• Cancer Immune Evasion Through Loss of MHC Class I Antigen Presentation (2021, background): “Much of the trimming of long peptides occurs in the endoplasmic reticulum by an aminopeptidase called ERAP1 (ERAAP) (55, 56) and in humans also a second related peptidase called ERAP2 (57).”
• Molecular Mechanisms of IFN-γ to Up-Regulate MHC Class I Antigen Processing and Presentation (2009, background): “ERAP-1 trims peptides with 9–16 amino acids in length and forms an 8–9 amino acid long peptide, which can no longer be cut by ERAP-1 [143, 144].”
• Towards a systems understanding of MHC class I and MHC class II antigen presentation (2011, background): “One ER aminopeptidase — termed ER aminopeptidase associated with antigen processing (ERAAP) — has been identified in mice, and two have been found in humans and termed ER aminopeptidase 1 (ERAP1) and ERAP2 (Ref”
• Enhancement to the RANKPEP resource for the prediction of peptide binding to MHC molecules using profiles (2004, background): “Nevertheless, a few peptides ranging between eight and 15 residues in length are translocated to the endoplasmic reticulum (ER) by the TAP transporter, where they can either be destroyed by an additional amino-peptidase or be rescued by binding to MHCI molecules (Pamer and Cresswell 1998; Rammensee ”