Evidence map›Paper›PMID 26062445›Full record

ArticleOncotarget2015

Discovery of new small molecules inhibiting 67 kDa laminin receptor interaction with laminin and cancer cell invasion.

Ada Pesapane, Carmen Di Giovanni, Francesca Wanda Rossi, Daniela Alfano, Luigi Formisano, Pia Ragno, Carmine Selleri, Nunzia Montuori, Antonio Lavecchia

Open access · diamondAbstract readComparative Study
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

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  11. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
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  13. Article
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  16. 37/67-laminin receptor facilitates neural crest cell migration during enteric nervous system development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  17. Article
  18. Review
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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

9 authors at 4 institutions in 1 country.

Ada PesapaneDepartment of Translational Medical Sciences, University of Naples Federico II, Naples, Italy.
Carmen Di GiovanniDepartment of Pharmacy, Drug Discovery Laboratory, University of Naples Federico II, Naples, Italy.
Francesca Wanda RossiDepartment of Translational Medical Sciences, University of Naples Federico II, Naples, Italy.
Daniela AlfanoInstitute of Genetics and Biophysics Adriano Buzzati-Traverso, Consiglio Nazionale delle Ricerche (CNR), Naples, Italy.
Luigi FormisanoDepartment of Science and Technology, University of Sannio, Benevento, Italy.
Pia RagnoDepartment of Chemistry, University of Salerno, Salerno, Italy.
Carmine SelleriDepartment of Medicine and Surgery, University of Salerno, Salerno, Italy.
Nunzia MontuoriDepartment of Translational Medical Sciences, University of Naples Federico II, Naples, Italy.
Antonio LavecchiaDepartment of Pharmacy, Drug Discovery Laboratory, University of Naples Federico II, Naples, Italy.
University of Naples Federico II · ITUniversity of Salerno · ITInstitute of Genetics and Biophysics · ITUniversity of Sannio · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 67 kDa laminin receptor (67LR) is a non-integrin receptor for laminin (LM) that derives from a 37 kDa precursor (37LRP). 67LR expression is increased in neoplastic cells and correlates with an enhanced invasive and metastatic potential. We used structure-based virtual screening (SB-VS) to search for 67LR inhibitory small molecules, by focusing on a 37LRP sequence, the peptide G, able to specifically bind LM. Forty-six compounds were identified and tested on HEK-293 cells transfected with 37LRP/67LR (LR-293 cells). One compound, NSC47924, selectively inhibited LR-293 cell adhesion to LM with IC50 and Ki values of 19.35 and 2.45 μmol/L. NSC47924 engaged residues W176 and L173 of peptide G, critical for specific LM binding. Indeed, NSC47924 inhibited in vitro binding of recombinant 37LRP to both LM and its YIGSR fragment. NSC47924 also impaired LR-293 cell migration to LM and cell invasion. A subsequent hierarchical similarity search with NSC47924 led to the identification of additional four compounds inhibiting LR-293 cell binding to LM: NSC47923, NSC48478, NSC48861, and NSC48869, with IC50 values of 1.99, 1.76, 3.4, and 4.0 μmol/L, respectively, and able to block in vitro cancer cell invasion. These compounds are promising scaffolds for future drug design and discovery efforts in cancer progression.

Indexed as

Aniline CompoundsAntineoplastic AgentsCell AdhesionCell MovementComputer-Aided DesignComputer SimulationDose-Response Relationship, DrugDrug DiscoveryHEK293 CellsHumansLamininModels, MolecularNaphtholsNeoplasm InvasivenessNeoplasmsProtein Binding1-((4-methoxyanilino)methyl)-2-naphtholAniline CompoundsAntineoplastic AgentsLamininNaphtholsReceptors, LamininRibosomal ProteinsRPSA protein, humancell adhesionlamininlaminin receptorsmall molecules

Identifiers

PMID26062445
PMCPMC4627239
OpenAlexW1886463992

What OpenQuestion holds

Textmetadata
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.