Evidence map›Paper›PMID 33333800›Full record

ReviewBiomolecules2020

Structural Basis for Vascular Endothelial Growth Factor Receptor Activation and Implications for Disease Therapy.

Faheem Shaik, Gary A Cuthbert, Shervanthi Homer-Vanniasinkam, Stephen P Muench, Sreenivasan Ponnambalam, Michael A Harrison

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 96 citations in OpenAlex.

  1. A Phase II Trial of Rivoceranib, an Oral Vascular Endothelial Growth Factor Receptor 2 Inhibitor, for Recurrent or Metastatic Adenoid Cystic Carcinoma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
    Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. VEGF and the VEGFMolecular neurobiology · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. A Complementarity-Based Approach to De Novo Binder Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. BioImpacts : BI · 2025
    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

6 authors at 1 institution in 1 country.

Faheem ShaikSchool of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK.
Gary A CuthbertFaculty of Medicine and Health, University of Leeds, Leeds LS2 9JT, UK.
Shervanthi Homer-VanniasinkamFaculty of Medicine and Health, University of Leeds, Leeds LS2 9JT, UK.
Stephen P MuenchSchool of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0001-6869-4414
Sreenivasan PonnambalamSchool of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0002-4452-7619
Michael A HarrisonFaculty of Medicine and Health, University of Leeds, Leeds LS2 9JT, UK.
University of Leeds · GB

Funding

British Heart Foundation FS/16/24/32133British Heart Foundation PG/16/86/32474
6 · The paper itself

Abstract

Vascular endothelial growth factors (VEGFs) bind to membrane receptors on a wide variety of cells to regulate diverse biological responses. The VEGF-A family member promotes vasculogenesis and angiogenesis, processes which are essential for vascular development and physiology. As angiogenesis can be subverted in many disease states, including tumour development and progression, there is much interest in understanding the mechanistic basis for how VEGF-A regulates cell and tissue function. VEGF-A binds with high affinity to two VEGF receptor tyrosine kinases (VEGFR1, VEGFR2) and with lower affinity to co-receptors called neuropilin-1 and neuropilin-2 (NRP1, NRP2). Here, we use a structural viewpoint to summarise our current knowledge of VEGF-VEGFR activation and signal transduction. As targeting VEGF-VEGFR activation holds much therapeutic promise, we examine the structural basis for anti-angiogenic therapy using small-molecule compounds such as tyrosine kinase inhibitors that block VEGFR activation and downstream signalling. This review provides a rational basis towards reconciling VEGF and VEGFR structure and function in developing new therapeutics for a diverse range of ailments.

Indexed as

DiseaseAnimalsHumansLigandsProtein DomainsProtein Kinase InhibitorsReceptors, Vascular Endothelial Growth FactorSignal TransductionVascular Endothelial Growth Factor ALigandsProtein Kinase InhibitorsReceptors, Vascular Endothelial Growth FactorVascular Endothelial Growth Factor Aafliberceptangiogenesisbevacizumabcancerreceptor tyrosine kinasesignal transductionsunitinibVEGFR

Identifiers

PMID33333800
PMCPMC7765180
OpenAlexW3110732212

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.