Evidence map›Paper›PMID 30984741›Full record

ArticleFrontiers in chemistry2019

Rational Design of Antiangiogenic Helical Oligopeptides Targeting the Vascular Endothelial Growth Factor Receptors.

Simone Zanella, Gianfranco Bocchinfuso, Marta De Zotti, Daniela Arosio, Franca Marino, Stefano Raniolo, Luca Pignataro, Giovanni Sacco, Antonio Palleschi, Alvaro S Siano and 5 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023
    Review
  4. Article
  5. Review
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

15 authors at 7 institutions in 2 countries.

Simone ZanellaDepartment of Chemistry, University of Milan, Milan, Italy.
Gianfranco BocchinfusoDepartment of Chemical Science and Technologies, University of Rome Tor Vergata, Rome, Italy.
Marta De ZottiPadova Unit, Department of Chemistry, Institute of Biomolecular Chemistry, CNR, University of Padova, Padova, Italy.
Daniela ArosioNational Research Council, Institute of Molecular Science and Technologies, Milan, Italy.
Franca MarinoCenter for Research in Medical Pharmacology, University of Insubria, Varese, Italy.
Stefano RanioloDepartment of Chemical Science and Technologies, University of Rome Tor Vergata, Rome, Italy.
Luca PignataroDepartment of Chemistry, University of Milan, Milan, Italy.
Giovanni SaccoDepartment of Chemistry, University of Milan, Milan, Italy.
Antonio PalleschiDepartment of Chemical Science and Technologies, University of Rome Tor Vergata, Rome, Italy.
Alvaro S SianoDepartamento de Química Organica, Facultad de Bioquímica y Ciencias Biologicas, Universidad Nacional del Litoral, Santa Fe, Argentina.
Umberto PiarulliCenter for Research in Medical Pharmacology, University of Insubria, Varese, Italy.
Laura BelvisiDepartment of Chemistry, University of Milan, Milan, Italy.
Fernando FormaggioPadova Unit, Department of Chemistry, Institute of Biomolecular Chemistry, CNR, University of Padova, Padova, Italy.
Cesare GennariDepartment of Chemistry, University of Milan, Milan, Italy.
Lorenzo StellaDepartment of Chemical Science and Technologies, University of Rome Tor Vergata, Rome, Italy.
University of Rome Tor Vergata · ITUniversity of Milan · ITInstitute of Molecular Science and Technologies · ITUniversity of Insubria · ITUniversity of Padua · ITNational Research Council · ITNational University of the Littoral · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor angiogenesis, essential for cancer development, is regulated mainly by vascular endothelial growth factors (VEGFs) and their receptors (VEGFRs), which are overexpressed in cancer cells. Therefore, the VEGF/VEGFR interaction represents a promising pharmaceutical target to fight cancer progression. The VEGF surface interacting with VEGFRs comprises a short α-helix. In this work, helical oligopeptides mimicking the VEGF-C helix were rationally designed based on structural analyses and computational studies. The helical conformation was stabilized by optimizing intramolecular interactions and by introducing helix-inducing C

Indexed as

angiogenesisCα,α-disubstituted amino acidshelical folded peptidesprotein-protein interactionsVEGF-C

Identifiers

PMID30984741
PMCPMC6449863
OpenAlexW2933205775

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.