Evidence map›Paper›PMID 29339412›Full record

ArticleMolecular & cellular proteomics : MCP2018

The Sequence-specific Peptide-binding Activity of the Protein Sulfide Isomerase AGR2 Directs Its Stable Binding to the Oncogenic Receptor EpCAM.

M Aiman Mohtar, Lenka Hernychova, J Robert O'Neill, Melanie L Lawrence, Euan Murray, Borek Vojtesek, Ted R Hupp

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
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

13 citing papers in PubMed, 22 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

M Aiman MohtarFrom the ‡University of Edinburgh, Institute of Genetics and Molecular Medicine, Edinburgh, Scotland, United Kingdom, EH4 2XR.
Lenka Hernychova¶Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, 656 53 Brno, Czech Republic.
J Robert O'NeillFrom the ‡University of Edinburgh, Institute of Genetics and Molecular Medicine, Edinburgh, Scotland, United Kingdom, EH4 2XR.
Melanie L LawrenceFrom the ‡University of Edinburgh, Institute of Genetics and Molecular Medicine, Edinburgh, Scotland, United Kingdom, EH4 2XR.
Euan MurrayFrom the ‡University of Edinburgh, Institute of Genetics and Molecular Medicine, Edinburgh, Scotland, United Kingdom, EH4 2XR.
Borek Vojtesek¶Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, 656 53 Brno, Czech Republic.
Ted R HuppFrom the ‡University of Edinburgh, Institute of Genetics and Molecular Medicine, Edinburgh, Scotland, United Kingdom, EH4 2XR; ted.hupp@ed.ac.uk.
University of Edinburgh · GBMasaryk Memorial Cancer Institute · CZMRC Institute of Genetics and Molecular Medicine · GBNational University of Malaysia · MY

Funding

Biotechnology and Biological Sciences Research Council BB/C511599/1Wellcome TrustWellcome Trust 094417/Z/10/Z
6 · The paper itself

Abstract

AGR2 is an oncogenic endoplasmic reticulum (ER)-resident protein disulfide isomerase. AGR2 protein has a relatively unique property for a chaperone in that it can bind sequence-specifically to a specific peptide motif (TTIYY). A synthetic TTIYY-containing peptide column was used to affinity-purify AGR2 from crude lysates highlighting peptide selectivity in complex mixtures. Hydrogen-deuterium exchange mass spectrometry localized the dominant region in AGR2 that interacts with the TTIYY peptide to within a structural loop from amino acids 131-135 (VDPSL). A peptide binding site consensus of Tx[IL][YF][YF] was developed for AGR2 by measuring its activity against a mutant peptide library. Screening the human proteome for proteins harboring this motif revealed an enrichment in transmembrane proteins and we focused on validating EpCAM as a potential AGR2-interacting protein. AGR2 and EpCAM proteins formed a dose-dependent protein-protein interaction

Indexed as

Epithelial Cell Adhesion MoleculeHumansMCF-7 CellsMucoproteinsOncogene ProteinsPeptidesProtein BindingProteinsProto-Oncogene Proteins c-mdm2Recombinant ProteinsAGR2 protein, humanEPCAM protein, humanEpithelial Cell Adhesion MoleculeMDM2 protein, humanMucoproteinsOncogene ProteinsPeptidesProteinsProto-Oncogene Proteins c-mdm2Recombinant Proteins

Identifiers

PMID29339412
PMCPMC5880107
OpenAlexW2784233439

What OpenQuestion holds

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LicenceCC BY
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.