Evidence map›Paper›PMID 31889156›Full record

ArticleScientific reports2019

Enhanced oligomerization of full-length RAGE by synergy of the interaction of its domains.

Alexander Moysa, Dietmar Hammerschmid, Roman H Szczepanowski, Frank Sobott, Michal Dadlez

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  10. RAGE Inhibitors for Targeted Therapy of Cancer: A Comprehensive Review.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. RAGE Signaling in Melanoma Tumors.International journal of molecular sciences · 2020
    Review
  15. An in Silico Approach Reveals the Potential Function of Cyanidin-3-o-glucoside of Red Rice in Inhibiting the Advanced Glycation End Products (AGES)-Receptor (RAGE) Signaling Pathway.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2020
    Article
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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

5 authors at 4 institutions in 3 countries.

Alexander MoysaInstitute of Biochemistry and Biophysics, PAN, Pawinskiego 5a, 02-109, Warsaw, Poland. a.alexandrmoysa@gmail.com.ORCID http://orcid.org/0000-0003-3618-9813
Dietmar HammerschmidBiomolecular & Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, 2020, Antwerp, Belgium.
Roman H SzczepanowskiInternational Institute of Molecular and Cell Biology, Trojdena 4, 02-109, Warsaw, Poland.
Frank SobottBiomolecular & Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, 2020, Antwerp, Belgium.
Michal DadlezInstitute of Biochemistry and Biophysics, PAN, Pawinskiego 5a, 02-109, Warsaw, Poland.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLInternational Institute of Molecular and Cell Biology · PLUniversity of Antwerp · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pattern recognition receptor RAGE (receptor for advanced glycation end-products) transmits proinflammatory signals in several inflammation-related pathological states, including vascular diseases, cancer, neurodegeneration and diabetes. Its oligomerization is believed to be important in signal transduction, but RAGE oligomeric structures and stoichiometries remain unclear. Different oligomerization modes have been proposed in studies involving different truncated versions of the extracellular parts of RAGE. Here, we provide basic characterization of the oligomerization patterns of full-length RAGE (including the transmembrane (TM) and cytosolic regions) and compare the results with oligomerization modes of its four truncated fragments. For this purpose, we used native mass spectrometry, analytical ultracentrifugation, and size-exclusion chromatography coupled with multi-angle light scattering. Our results confirm known oligomerization tendencies of separate domains and highlight the enhanced oligomerization properties of full-length RAGE. Mutational analyses within the GxxxG motif of the TM region show sensitivity of oligomeric distributions to the TM sequence. Using hydrogen-deuterium exchange, we mapped regions involved in TM-dependent RAGE oligomerization. Our data provide experimental evidence for the major role of the C2 and TM domains in oligomerization, underscoring synergy among different oligomerization contact regions along the RAGE sequence. These results also explain the variability of obtained oligomerization modes in RAGE fragments.

Indexed as

Protein Interaction Domains and MotifsProtein MultimerizationMass SpectrometryMembrane ProteinsModels, MolecularMutationProtein BindingProtein ConformationProtein FoldingReceptor for Advanced Glycation End ProductsStructure-Activity RelationshipMembrane ProteinsReceptor for Advanced Glycation End Products

Identifiers

PMID31889156
PMCPMC6937306
OpenAlexW2997076598

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

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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.