Evidence map›Paper›PMID 24478383›Full record

ReviewCold Spring Harbor perspectives in biology2014

Tie2 and Eph receptor tyrosine kinase activation and signaling.

William A Barton, Annamarie C Dalton, Tom C M Seegar, Juha P Himanen, Dimitar B Nikolov

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Mechanistic insights into the role of FOXO in diabetic retinopathy.American journal of translational research · 2022
    Review
  6. Review
  7. Article
  8. SVEP1 as a Genetic Modifier of TEK-Related Primary Congenital Glaucoma.Investigative ophthalmology & visual science · 2020
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Antiangiogenic Effect of Alkaloids.Oxidative medicine and cellular longevity · 2019
    Review
  14. Article
  15. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. Review
  19. Eph receptor signaling and ephrins.Cold Spring Harbor perspectives in biology · 2013
    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

5 authors at 2 institutions in 1 country.

William A BartonDepartment of Biochemistry and Molecular Biology, School of Medicine, Virginia Commonwealth University, Richmond, Virginia 23298.
Annamarie C Dalton
Tom C M Seegar
Juha P Himanen
Dimitar B Nikolov
Virginia Commonwealth University · USMemorial Sloan Kettering Cancer Center · US

Funding

STRUCTURAL STUDY OF EPH RECEPTORS AND EPHRINSR01NS038486 · NINDS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIKOLOV, DIMITAR B · 1999 to 2018
$5.9M
Structure Study of Angiopoietins and the Tie2 ReceptorR01HL077249 · NHLBI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIKOLOV, DIMITAR B · 2004 to 2008
$1.7M
Biochemical and Biophysical Analysis of Angiopoietin SignalingR01CA127501 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI BARTON, WILLIAM A. · 2008 to 2012
$1.4M
Structural and biophysical characterization of Tie receptor/integrin interactionsF31CA165673 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI DALTON, ANNAMARIE C · 2012 to 2014
$92k
NCI NIH HHS 1R01CA127501NCI NIH HHS F31 CA165673NCI NIH HHS R01 CA127501NHLBI NIH HHS 1R01HL077249NHLBI NIH HHS R01 HL077249NINDS NIH HHS R01 NS038486NINDS NIH HHS R01NS038486
6 · The paper itself

Abstract

The Eph and Tie cell surface receptors mediate a variety of signaling events during development and in the adult organism. As other receptor tyrosine kinases, they are activated on binding of extracellular ligands and their catalytic activity is tightly regulated on multiple levels. The Eph and Tie receptors display some unique characteristics, including the requirement of ligand-induced receptor clustering for efficient signaling. Interestingly, both Ephs and Ties can mediate different, even opposite, biological effects depending on the specific ligand eliciting the response and on the cellular context. Here we discuss the structural features of these receptors, their interactions with various ligands, as well as functional implications for downstream signaling initiation. The Eph/ephrin structures are already well reviewed and we only provide a brief overview on the initial binding events. We go into more detail discussing the Tie-angiopoietin structures and recognition.

Indexed as

Signal TransductionAngiopoietinsBinding SitesEnzyme ActivationLigandsModels, MolecularProtein Structure, TertiaryReceptors, Eph FamilyReceptor, TIE-2AngiopoietinsLigandsReceptors, Eph FamilyReceptor, TIE-2

Identifiers

PMID24478383
PMCPMC3949358
OpenAlexW2113432476

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.