Evidence map›Paper›PMID 27498819›Full record

ArticleScientific reports2016

Miniaturizing VEGF: Peptides mimicking the discontinuous VEGF receptor-binding site modulate the angiogenic response.

Lucia De Rosa, Federica Finetti, Donatella Diana, Rossella Di Stasi, Sara Auriemma, Alessandra Romanelli, Roberto Fattorusso, Marina Ziche, Lucia Morbidelli, Luca Domenico D'Andrea

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.4field-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

8 citing papers in PubMed, 22 citations in OpenAlex.

  1. AI-assisted design of a VEGFR2 agonistic peptide that promotes angiogenesis and wound repair.Protein science : a publication of the Protein Society · 2026
    Article
  2. Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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

10 authors at 3 institutions in 1 country.

Lucia De RosaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Federica FinettiDipartimento di Scienze della Vita, Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
Donatella DianaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Rossella Di StasiIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Sara AuriemmaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Alessandra RomanelliDipartimento di Farmacia, Università di Napoli "Federico II", via Mezzocannone 16, 80134, Napoli, Italy.
Roberto FattorussoDipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, via A. Vivaldi 43, 81100, Caserta, Italy.
Marina ZicheDipartimento di Scienze della Vita, Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
Lucia MorbidelliDipartimento di Scienze della Vita, Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
Luca Domenico D'AndreaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
Institute of Biostructure and Bioimaging · ITUniversity of Siena · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The angiogenic properties of VEGF are mediated through the binding of VEGF to its receptor VEGFR2. The VEGF/VEGFR interface is constituted by a discontinuous binding region distributed on both VEGF monomers. We attempted to reproduce this discontinuous binding site by covalently linking into a single molecular entity two VEGF segments involved in receptor recognition. We designed and synthesized by chemical ligation a set of peptides differing in length and flexibility of the molecular linker joining the two VEGF segments. The biological activity of the peptides was characterized in vitro and in vivo showing a VEGF-like activity. The most biologically active mini-VEGF was further analyzed by NMR to determine the atomic details of its interaction with the receptor.

Indexed as

AnimalsBinding SitesCell MovementCell ProliferationCircular DichroismCrystallography, X-RayHumansHuman Umbilical Vein Endothelial CellsMagnetic Resonance SpectroscopyMiceMice, Inbred C57BLNeovascularization, PathologicPeptidesPhosphorylationProtein BindingProtein Structure, SecondaryKDR protein, humanKdr protein, mousePeptidesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2

Identifiers

PMID27498819
PMCPMC4976335
OpenAlexW2528609914

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.