Evidence map›Paper›PMID 22896701›Full record

ArticleThe Journal of biological chemistry2012

A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR).

Haydyn D T Mertens, Magnus Kjaergaard, Simon Mysling, Henrik Gårdsvoll, Thomas J D Jørgensen, Dmitri I Svergun, Michael Ploug

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Trial
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  6. Article
  7. Review
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  9. Review
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  12. Article
  13. Review
  14. suPAR, a Circulating Kidney Disease Factor.Frontiers in medicine · 2021
    Review
  15. Article
  16. Evolution and Medical Significance of LU Domain-Containing Proteins.International journal of molecular sciences · 2019
    Review
  17. Article
  18. Article
  19. Review
  20. Journal of applied crystallography · 2017
    Article
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 2 countries.

Haydyn D T MertensFinsen Laboratory, Rigshospitalet and Biotech Research and Innovation Centre (BRIC), Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.
Magnus Kjaergaard
Simon Mysling
Henrik Gårdsvoll
Thomas J D Jørgensen
Dmitri I Svergun
Michael Ploug
Rigshospitalet · DKUniversity of Southern Denmark · DKEuropean Molecular Biology Laboratory · DEUniversity of Copenhagen · DK

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
NCRR NIH HHS P41 RR001081
6 · The paper itself

Abstract

The urokinase-type plasminogen activator receptor (uPAR) provides a rendezvous between proteolytic degradation of the extracellular matrix and integrin-mediated adhesion to vitronectin. These processes are, however, tightly linked because the high affinity binding of urokinase regulates the binding of uPAR to matrix-embedded vitronectin. Although crystal structures exist to define the corresponding static bi- and trimolecular receptor complexes, it is evident that the dynamic property of uPAR plays a decisive role in its function. In the present study, we combine small angle x-ray scattering, hydrogen-deuterium exchange, and surface plasmon resonance to develop a structural model describing the allosteric regulation of uPAR. We show that the flexibility of its N-terminal domain provides the key for understanding this allosteric mechanism. Importantly, our model has direct implications for understanding uPAR-assisted cell adhesion and migration as well as for translational research, including targeted intervention therapy and non-invasive tumor imaging in vivo.

Indexed as

Extracellular MatrixProteolysisReceptors, Urokinase Plasminogen ActivatorVitronectinAllosteric RegulationAnimalsCell AdhesionCell LineCell MovementDeuterium Exchange MeasurementDrosophila melanogasterHumansNeoplasm InvasivenessNeoplasmsProtein BindingProtein Structure, TertiaryReceptors, Urokinase Plasminogen ActivatorVitronectin

Identifiers

PMID22896701
PMCPMC3464537
OpenAlexW2057938042

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.