Evidence map›Paper›PMID 22044885›Full record

ReviewSeminars in cell & developmental biology2012

Targeting Eph receptors with peptides and small molecules: progress and challenges.

Roberta Noberini, Ilaria Lamberto, Elena B Pasquale

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Lipidation and PEGylation Strategies to Prolong theEuropean journal of medicinal chemistry · 2023
    Article
  9. Eph Receptors in Cancer.Biomedicines · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Interactions between Ligand-Bound EGFR and VEGFR2.Journal of molecular biology · 2021
    Article
  14. Eph Receptors and Ephrins in Retinal Diseases.International journal of molecular sciences · 2021
    Review
  15. Identification of tetracycline combinations as EphB1 tyrosine kinase inhibitors for treatment of neuropathic pain.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. The Pyrazolo[3,4-Molecules (Basel, Switzerland) · 2020
    Article
  18. Review
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Roberta NoberiniSanford-Burnham Medical Research Institute, 10901 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Ilaria Lamberto
Elena B Pasquale
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

Tissue CultureP01HD025938 · NICHD · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI YAMAGUCHI, YU · 1989 to 2011
$13.6M
Targeting Eph receptors in cancerP01CA138390 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2010 to 2014
$7.3M
The EphB4 Receptor as a Novel Breast Cancer TargetR01CA116099 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2006 to 2010
$1.9M
Optimization of EphA4 antagonists for CNS disordersR21NS067502 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI COSFORD, NICHOLAS DAVID, PASQUALE, ELENA B · 2009 to 2010
$523k
Cell-based screening for EphA2 receptor inhibitorsR21NS066479 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2009 to 2011
$239k
NCI NIH HHS P01 CA138390NCI NIH HHS R01 CA116099NICHD NIH HHS P01 HD025938NINDS NIH HHS R21 NS066479NINDS NIH HHS R21 NS067502
6 · The paper itself

Abstract

The Eph receptors are a large family of receptor tyrosine kinases. Their kinase activity and downstream signaling ability are stimulated by the binding of cell surface-associated ligands, the ephrins. The ensuing signals are bidirectional because the ephrins can also transduce signals (known as reverse signals) following their interaction with Eph receptors. The ephrin-binding pocket in the extracellular N-terminal domain of the Eph receptors and the ATP-binding pocket in the intracellular kinase domain represent potential binding sites for peptides and small molecules. Indeed, a number of peptides and chemical compounds that target Eph receptors and inhibit ephrin binding or kinase activity have been identified. These molecules show promise as probes to study Eph receptor/ephrin biology, as lead compounds for drug development, and as targeting agents to deliver drugs or imaging agents to tumors. Current challenges are to find (1) small molecules that inhibit Eph receptor-ephrin interactions with high binding affinity and good lead-like properties and (2) selective kinase inhibitors that preferentially target the Eph receptor family or subsets of Eph receptors. Strategies that could also be explored include targeting additional Eph receptor interfaces and the ephrin ligands.

Indexed as

AnimalsHumansLithocholic AcidMolecular Targeted TherapyNeoplasmsPeptidesProtein Kinase InhibitorsReceptors, Eph FamilySalicylatesLithocholic AcidPeptidesProtein Kinase InhibitorsReceptors, Eph FamilySalicylates

Identifiers

PMID22044885
PMCPMC3319464
OpenAlexW2050974395

What OpenQuestion holds

Textmetadata
LicenceTDM
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.