Evidence map›Paper›PMID 26787460›Full record

ArticleFEBS letters2016

Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.

Sarah Garrido-Urbani, Pankaj Garg, Rania Ghossoub, Roland Arnold, Frédérique Lembo, Gustav N Sundell, Philip M Kim, Marc Lopez, Pascale Zimmermann, Sachdev S Sidhu and 1 more

Abstract readValidation Study
In one paragraph

Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Screening Intrinsically Disordered Regions for Short Linear Binding Motifs.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  11. Article
  12. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
    Review
  13. Article
  14. Review
  15. 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

11 authors.

Sarah Garrido-UrbaniInserm U1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille University, Centre National de la Recherche Scientifique UMR7258, Marseille, France.
Pankaj GargTerrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
Rania GhossoubInserm U1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille University, Centre National de la Recherche Scientifique UMR7258, Marseille, France.
Roland ArnoldTerrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
Frédérique LemboInserm U1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille University, Centre National de la Recherche Scientifique UMR7258, Marseille, France.
Gustav N SundellDepartment of Chemistry - BMC, Uppsala University, Sweden.
Philip M KimTerrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
Marc LopezInserm U1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille University, Centre National de la Recherche Scientifique UMR7258, Marseille, France.
Pascale ZimmermannInserm U1068, Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes, Aix-Marseille University, Centre National de la Recherche Scientifique UMR7258, Marseille, France.
Sachdev S SidhuTerrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
Ylva IvarssonDepartment of Chemistry - BMC, Uppsala University, Sweden.

Funding

Canadian Institutes of Health Research MOP-93684
6 · The paper itself

Abstract

Syntenin has crucial roles in cell adhesion, cell migration and synaptic transmission. Its closely linked postsynaptic density-95, discs large 1, zonula occludens-1 (PDZ) domains typically interact with C-terminal ligands. We profile syntenin PDZ1-2 through proteomic peptide phage display (ProP-PD) using a library that displays C-terminal regions of the human proteome. The protein recognizes a broad range of peptides, with a preference for hydrophobic motifs and has a tendency to recognize cryptic internal ligands. We validate the interaction with nectin-1 through orthogonal assays. The study demonstrates the power of ProP-PD as a complementary approach to uncover interactions of potential biological relevance.

Indexed as

Models, MolecularAmino Acid MotifsAnimalsBinding SitesCell Adhesion MoleculesChlorocebus aethiopsComputational BiologyCOS CellsHumansHydrophobic and Hydrophilic InteractionsImmobilized ProteinsKineticsLigandsMCF-7 CellsNectinsPDZ DomainsCell Adhesion MoleculesImmobilized ProteinsLigandsNECTIN1 protein, humanNectinsPeptide FragmentsPeptide LibraryRecombinant ProteinsSDCBP protein, humanSynteninsPDZ domainpeptide interactionphage displayprotein-protein interactionshort linear motif

Identifiers

PMID26787460
PMCPMC4819696

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.