Evidence map›Paper›PMID 11689428›Full record

ArticleThe EMBO journal2001

Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor.

C Hundt, J M Peyrin, S Haïk, S Gauczynski, C Leucht, R Rieger, M L Riley, J P Deslys, D Dormont, C I Lasmézas and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

105 citing papers in PubMed, 280 citations in OpenAlex.

  1. Article
  2. PrPInternational journal of molecular sciences · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. RhoA/ROCK Regulates Prion Pathogenesis by Controlling Connexin 43 Activity.International journal of molecular sciences · 2020
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017
    Review

45 more citing papers are in PubMed but not listed here.

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

11 authors at 1 institution in 2 countries.

C HundtLaboratorium für Molekulare Biologie-Genzentrum-Institut für Biochemie der LMU München, Feodor-Lynen Strasse 25, D-81377 Munich, Germany.
J M Peyrin
S Haïk
S Gauczynski
C Leucht
R Rieger
M L Riley
J P Deslys
D Dormont
C I Lasmézas
S Weiss
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell-binding and internalization studies on neuronal and non-neuronal cells have demonstrated that the 37-kDa/67-kDa laminin receptor (LRP/LR) acts as the receptor for the cellular prion protein (PrP). Here we identify direct and heparan sulfate proteoglycan (HSPG)-dependent interaction sites mediating the binding of the cellular PrP to its receptor, which we demonstrated in vitro on recombinant proteins. Mapping analyses in the yeast two-hybrid system and cell-binding assays identified PrPLRPbd1 [amino acids (aa) 144-179] as a direct and PrPLRPbd2 (aa 53-93) as an indirect HSPG-dependent laminin receptor precursor (LRP)-binding site on PrP. The yeast two-hybrid system localized the direct PrP-binding domain on LRP between aa 161 and 179. Expression of an LRP mutant lacking the direct PrP-binding domain in wild-type and mutant HSPG-deficient Chinese hamster ovary cells by the Semliki Forest virus system demonstrates a second HSPG-dependent PrP-binding site on LRP. Considering the absence of LRP homodimerization and the direct and indirect LRP-PrP interaction sites, we propose a comprehensive model for the LRP-PrP-HSPG complex.

Indexed as

Two-Hybrid System TechniquesAnimalsBinding SitesCell LineCHO CellsChromatography, GelCricetinaeGalactosidesGlutathione TransferaseHeparan Sulfate ProteoglycansHumansMiceOligopeptidesPeptide FragmentsPeptidesPrionsbeta-galactosideFLAG peptideGalactosidesGlutathione TransferaseHeparan Sulfate ProteoglycansOligopeptidesPeptide FragmentsPeptidesPrionsProtein PrecursorsReceptors, LamininRecombinant Fusion Proteins

Identifiers

PMID11689428
PMCPMC125289
OpenAlexW2132905193

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.