Evidence map›Paper›PMID 41479007›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Expression, Purification, and Functional Analysis Methods of Antigen-Processing Aminopeptidases ERAP1, ERAP2, and IRAP.

Anastasia Mpakali

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Anastasia MpakaliLaboratory of Biochemistry, Department of Chemistry, National and Kapodistrian University of Athens, Athens, Greece. ampakali@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum aminopeptidases 1 and 2 (ERAP1, ERAP2), along with Insulin-Regulated Aminopeptidase (IRAP), play key roles in antigen processing by trimming precursor peptides for major histocompatibility complex (MHC) class I presentation, thereby contributing to adaptive immune regulation. Dysregulation of these enzymes has been implicated in various diseases, including autoimmune disorders and cancer. This chapter provides a comprehensive, step-by-step methodological guide for the expression, purification, and functional characterization of recombinant ERAP1, ERAP2, and IRAP. Detailed protocols include baculovirus-mediated expression in insect cells, affinity chromatography for protein purification, and a suite of functional assays to study enzymatic activity, substrate specificity, and inhibitor screening. Fluorogenic, colorimetric, and HPLC-based assays are described, offering versatile tools for kinetic analysis and inhibitor evaluation. These protocols are designed to yield high-purity, functionally active enzymes suitable for biochemical, structural, mechanistic, and drug discovery studies.

Indexed as

AminopeptidasesAntigen PresentationCystinyl AminopeptidaseMinor Histocompatibility AntigensAnimalsBaculoviridaeChromatography, AffinityGene ExpressionHumansRecombinant ProteinsSf9 CellsSubstrate SpecificityAminopeptidasesCystinyl AminopeptidaseERAP1 protein, humanERAP2 protein, humanleucyl-cystinyl aminopeptidaseMinor Histocompatibility AntigensRecombinant ProteinsAffinity chromatographyAminopeptidase enzymatic assaysAntigen processingBaculovirus-mediated expressionEndoplasmic reticulum aminopeptidases (ERAP1, ERAP2)Enzyme kineticsInhibitor screeningInsulin-regulated aminopeptidase (IRAP)Recombinant protein expression

Identifiers

PMID41479007

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.