Evidence map›Paper›PMID 28751379›Full record

ArticleThe Journal of biological chemistry2017

The interleukin-like epithelial-mesenchymal transition inducer ILEI exhibits a non-interleukin-like fold and is active as a domain-swapped dimer.

Anna M Jansson, Agnes Csiszar, Joachim Maier, Ann-Christin Nyström, Elisabeth Ax, Patrik Johansson, Lovisa Holmberg Schiavone

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 20 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 5 countries.

Anna M JanssonFrom the Reagents and Assay Development Division, Discovery Sciences Department.
Agnes Csiszarthe Institute of Cancer Research, Department of Medicine I, Medical University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria.
Joachim MaierFrom the Reagents and Assay Development Division, Discovery Sciences Department.
Ann-Christin NyströmTranslational Sciences Division, Cardiovascular and Metabolic Diseases Department, and.
Elisabeth AxFrom the Reagents and Assay Development Division, Discovery Sciences Department.
Patrik JohanssonStructure and Biophysics Division, Discovery Sciences Department, AstraZeneca, Pepparedsleden 1, 431 83 Mölndal, Sweden and patrik.johansson@astrazeneca.com.ORCID 0000-0002-7850-1169
Lovisa Holmberg SchiavoneFrom the Reagents and Assay Development Division, Discovery Sciences Department, lovisa.holmberg.schiavone@astrazeneca.com.
Discovery Centre · CAAstraZeneca (Australia) · AUAstraZeneca (Germany) · DEMedical University of Vienna · AT

Funding

Austrian Science Fund FWF P 25834
6 · The paper itself

Abstract

Production and secretion of pro-metastatic proteins is a feature of many tumor cells. The FAM3C interleukin-like epithelial-to-mesenchymal-transition (EMT) inducer (ILEI) has been shown to be strongly up-regulated in several cancers and to be essential for tumor formation and metastasis in epithelial cells, correlating with a significant decrease in overall survival in colon and breast cancer patients. ILEI has been seen to interact with the γ-secretase presenilin 1 subunit (PS1). However, not much is known about the mechanism-of-action or the detailed ILEI structure. We present here the crystal structures of FAM3C ILEI and show that it exists as monomers but also as covalent dimers. The observed ILEI β-β-α fold confirmed previous indications that the FAM3C proteins do not form classical four-helix-bundle structures as was initially predicted. This provides the first experimental evidence that the interleukin-like EMT inducers are not evolutionarily related to the interleukins. However, more surprisingly, the ILEI dimer structure was found to feature a

Indexed as

Models, MolecularAmino Acid SubstitutionAnimalsCell Line, TransformedCell MovementCrystallography, X-RayCysteineCystineCytokinesDimerizationHumansInterleukinsMiceNeoplasm ProteinsPeptide FragmentsPoint MutationCysteineCystineCytokinesFAM3C protein, humanFam3c protein, mouseInterleukinsNeoplasm ProteinsPeptide FragmentsRecombinant Fusion Proteinscancercrystallographyepithelial-mesenchymal transition (EMT)presenilintransforming growth factor β (TGF-β)γ-secretase

Identifiers

PMID28751379
PMCPMC5602407
OpenAlexW2739872581

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.