Erap1 Antibody

1. data provide the first evidence that ERAP1 associated with exosomes plays important roles in inflammatory processes via activation of macrophages. PMID: 29567213
2. we have shown that the loss of ERAAP leads to shifts in the nature and lengths of peptides presented by MHC I molecules on the cell surface PMID: 27371725
3. results suggest that several aminopeptidases play important roles in the maximum synthesis of NO in activated macrophages in a substrate peptide-dependent manner and ERAP1 is one of the aminopeptidases involved in the NO synthesis PMID: 25577645
4. This study clarifies ERAP1's role in shaping immunodominance through creation and destruction of peptides in vivo and demonstrates the functional significance of ERAP1 in modulating T-cell killing based upon this role. PMID: 25087231
5. These results suggest that secretion of ERAP1 is mediated by toll-like receptors via induction of intermediate cytokines PMID: 24688025
6. ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis. PMID: 24504800
7. Absence of Tpn or ERAAP independently altered the peptide repertoire by causing loss as well as gain of new pMHC I. ERAAP defined the characteristic amino termini of canonical MHC I peptides. PMID: 23863903
8. MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo. PMID: 22522492
9. endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma PMID: 21531727
10. ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice PMID: 21252114
11. The characteristic peptide length, as well as composition, of class I histocompatibility peptide cargo is determined not only by the class-I peptide-binding groove, but also by ERAAP proteolysis in the endoplasmic reticulum. PMID: 20173027
12. identification of ERAAP, the aminopeptidase associated with antigen processing in the endoplasmic reticulum (ERAAP) PMID: 12368856
13. Data show that loss of endoplasmic reticulum aminopeptidase 1 (ERAP1) in the antigen-processing pathway results in a marked shift in the hierarchy of immunodominance in viral infections. PMID: 16754858
14. Although PILSAP may not function in the initial generation of Flk-1 positive mesodermal precursors, it does play a role in growth of vascular, hematopoietic, and muscular lineage population from those precursors. PMID: 16824192
15. PILSAP affects RhoA activation and that influences the proper function of endothelial cells PMID: 17385722
16. ERAAP, in concert with major histocompatibility complex class I molecules, regulates the quality of processed peptides presented on the cell surface. PMID: 18941218

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KEGG: mmu:80898

STRING: 10090.ENSMUSP00000133166

UniGene: Mm.83526