gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Endoplasmic reticulum aminopeptidase 2

ERAP2, LRAP, leukocyte-derived arginine aminopeptidase, endoplasmic reticulum aminopeptidase 2
Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 (MIM 606832) and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2; MIM 190470) (Tanioka et al., 2003 [PubMed 12799365]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Amelogenin, ERAP1, aminopeptidase, CAN, MHC
Papers on ERAP2
Truncated amelogenin and LRAP transgenes improve Amelx null mouse enamel.
Pugach et al., Cambridge, United States. In Matrix Biol, Dec 2015
We aimed to determine whether the 2 transgenes (Tg), LRAP and CTRNC together, can improve LRAPTg/Amelx-/- and CTRNCTg/Amelx-/- enamel thickness and prism organization, which were not rescued in Amelx-/- enamel.
The immunogenetics of Psoriasis: A comprehensive review.
Bowcock et al., New York City, United States. In J Autoimmun, Nov 2015
These genes span an array of functions that involve antigen presentation (HLA-Cw6, ERAP1, ERAP2, MICA), the IL-23 axis (IL12Bp40, IL23Ap19, IL23R, JAK2, TYK2), T-cell development and T-cells polarization (RUNX1, RUNX3, STAT3, TAGAP, IL4, IL13), innate immunity (CARD14, c-REL, TRAF3IP2, DDX58, IFIH1), and negative regulators of immune responses (TNIP1, TNFAIP3, NFKBIA, ZC3H12C, IL36RN, SOCS1).
Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (ER) Aminopeptidase 2.
Stratikos et al., Athens, Greece. In J Biol Chem, Nov 2015
To understand how these enzymes recognize substrates, we determined crystal structures of ER aminopeptidase 2 (ERAP2) in complex with a substrate analogue and a peptidic product to 2.5 and 2.7 Å, respectively, and compared them to the apo-form structure determined to 3.0 Å.
HLA class I is most tightly linked to levels of tapasin compared with other antigen-processing proteins in glioblastoma.
Paulsson et al., Lund, Sweden. In Br J Cancer, Oct 2015
Some APM components, for example, TAP1/TAP2 and LMP2/LMP7, showed variable but coordinated expression, whereas ERAP1/ERAP2 displayed an imbalanced expression pattern.
The peptidome of the Behçet's disease-associated HLA-B*51:01 includes two sub-peptidomes differentially shaped by ERAP1.
de Castro et al., Madrid, Spain. In Arthritis Rheumatol, Oct 2015
ERAP1 and ERAP2 from 721.221 cells were characterized by genomic sequencing and Western blotting.
Solid-state NMR studies of proteins immobilized on inorganic surfaces.
Shaw, Richland, United States. In Solid State Nucl Magn Reson, Sep 2015
Two calcium phosphate proteins, statherin (43 amino acids) and leucine rich amelogenin protein (LRAP; 59 amino acids), have been studied in depth and have different dynamic properties and 2D- and 3D-structural features.
Interaction of enamel matrix proteins with human periodontal ligament cells.
Donos et al., London, United Kingdom. In Clin Oral Investig, Aug 2015
OBJECTIVES: It has recently been shown that enamel matrix derivative (EMD) components (Fraction C, containing <6 kDa peptides (mainly a 5.3 kDa tyrosine-rich amelogenin peptide (TRAP)), and Fraction A, containing a mixture of >6 kDa peptides (including a leucine-rich amelogenin peptide (LRAP))) differentially regulate osteogenic differentiation of periodontal ligament (PDL) cells.
Revisiting MHC genes in spondyloarthritis.
Garchon et al., Boulogne-Billancourt, France. In Curr Rheumatol Rep, Jun 2015
Interestingly, some of those new genes, such as ERAP1, ERAP2, and NPEPPS, code for aminopeptidases that are involved in MHC class I presentation and were shown to interact with HLA-B27.
Endoplasmic reticulum aminopeptidase 2 is highly expressed in papillary thyroid microcarcinoma with cervical lymph node metastasis.
Bae et al., Seoul, South Korea. In J Cancer Res Ther, Apr 2015
RESULTS: We identified 12 differentially expressed gene, and most one is endoplasmic reticulum aminopeptidase 2 (ERAP2).
The immunopathogenesis of birdshot chorioretinopathy; a bird of many feathers.
Radstake et al., Utrecht, Netherlands. In Prog Retin Eye Res, 2015
The first genome-wide association study facilitated novel concepts into a disease mechanism beyond HLA-A29 that includes strong genetic predisposition for the ERAP2 gene that affects antigen processing for HLA class I. Furthermore, patients manifest with pro-inflammatory cytokine profiles and pathogenic T cell subsets that are associated with IL-17-linked inflammation.
A role for naturally occurring alleles of endoplasmic reticulum aminopeptidases in tumor immunity and cancer pre-disposition.
Fruci et al., Athens, Greece. In Front Oncol, 2013
Endoplasmic reticulum aminopeptidase 1 and 2 (ERAP1 and ERAP2) are key components on the pathway that generates antigenic epitopes for presentation to cytotoxic T-lymphocytes (CTLs).
A common single nucleotide polymorphism in endoplasmic reticulum aminopeptidase 2 induces a specificity switch that leads to altered antigen processing.
Stratikos et al., Athens, Greece. In J Immunol, 2012
The common ERAP2 single nucleotide polymorphism rs2549782 that codes for amino acid variation Asp392Lys leads to alterations in both the activity and the specificity of the enzyme.
OS049. Exome sequencing identifies likely functional variantsinfluencing preeclampsia and CVD risk.
Moses et al., San Antonio, United States. In Pregnancy Hypertens, 2012
Whilst our prior linkage- and association-based positional cloning studies in family- and population-based Australian cohorts, respectively, have discovered novel preeclampsia candidate genes (INHBB,ACVR2A,LCT,LRP1B,RND3,GCA,ERAP2,TNFSF13B), the full complement of causal genetic variation remains largely unknown.
OS046. Genome-wide association scans identify novel maternalsusceptibility loci for preeclampsia.
Moses et al., San Antonio, United States. In Pregnancy Hypertens, 2012
INTRODUCTION: We have successfully utilized a family-based study design to localize several positional candidate preeclampsia susceptibility genes to chromosomes 2q22(ACVR2A,LCT,LRP1B,RND3,GCA),5q (ERAP2) and 13q(TNFSF13B).
Crystallization and preliminary X-ray diffraction analysis of human endoplasmic reticulum aminopeptidase 2.
Parker et al., Australia. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
crystals of ERAP2 belonged to an orthorhombic space group and diffracted anisotropically to 3.3 A resolution in the best direction on an in-house X-ray source
The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing.
Mavridis et al., Athens, Greece. In Biochemistry, 2012
The molecular structure of glycosylated human ERAP2 has been determined to 3.08 A resolution by molecular replacement using ERAP1 as a search model and refined.
A common functional variant of endoplasmic reticulum aminopeptidase 2 (ERAP2) that reduces major histocompatibility complex class I expression is not associated with ankylosing spondylitis.
Wordsworth et al., In Rheumatology (oxford), 2011
assessed frequency of rs2248374 SNP in ERAP2 in ankylosing spondylitis (AS) cases and controls and found no association with AS
Fetal ERAP2 variation is associated with preeclampsia in African Americans in a case-control study.
Strauss et al., Richmond, United States. In Bmc Med Genet, 2010
strong evidence that ERAP2 plays a role in the development of preeclampsia
Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci.
Parkes et al., Kiel, Germany. In Nat Genet, 2010
A series of in silico analyses highlighted particular genes within these loci and, together with manual curation, implicated functionally interesting candidate genes including SMAD3, ERAP2, IL10, IL2RA, TYK2, FUT2, DNMT3A, DENND1B, BACH2 and TAGAP.
Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum.
van Endert et al., Paris, France. In Nat Immunol, 2005
We show here that one of these, ERAP1, was unable to remove several N-terminal amino acids that were trimmed efficiently by the second enzyme, ERAP2.
share on facebooktweetadd +1mail to friends