Evidence map›Paper›PMID 33277361›Full record

ArticleThe Journal of biological chemistry

PIP

Katherine M Stefanski, Charles M Russell, Justin M Westerfield, Rajan Lamichhane, Francisco N Barrera

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Activation dynamics of a water-soluble human mu-opioid receptor.The Journal of biological chemistry · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Regulation of receptor tyrosine kinase hetero-interactions.Current opinion in structural biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Cholesterol inhibits assembly and activation of the EphA2 receptor.bioRxiv : the preprint server for biology · 2024
    Article
  17. Review
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Katherine M StefanskiGraduate School of Genome Science and Technology, University of Tennessee, Knoxville, USA.
Charles M RussellDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, USA.
Justin M WesterfieldDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, USA.
Rajan LamichhaneDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, USA. Electronic address: rajan@utk.edu.
Francisco N BarreraDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, USA. Electronic address: fbarrera@utk.edu.
University of Tennessee at Knoxville · US

Funding

Transmembrane Peptides for Targeting Acidosis - Equipment SupplementR01GM120642 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI BARRERA, FRANCISCO NICOLAS · 2016 to 2020
$1.7M
6 · The paper itself

Abstract

The impact of the EphA2 receptor on cancer malignancy hinges on the two different ways it can be activated. EphA2 induces antioncogenic signaling after ligand binding, but ligand-independent activation of EphA2 is pro-oncogenic. It is believed that the transmembrane (TM) domain of EphA2 adopts two alternate conformations in the ligand-dependent and the ligand-independent states. However, it is poorly understood how the difference in TM helical crossing angles found in the two conformations impacts the activity and regulation of EphA2. We devised a method that uses hydrophobic matching to stabilize two conformations of a peptide comprising the EphA2 TM domain and a portion of the intracellular juxtamembrane (JM) segment. The two conformations exhibit different TM crossing angles, resembling the ligand-dependent and ligand-independent states. We developed a single-molecule technique using styrene maleic acid lipid particles to measure dimerization in membranes. We observed that the signaling lipid PIP

Indexed as

Protein MultimerizationBinding SitesCell MembraneHumansPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein ConformationProtein DomainsReceptor, EphA2Signal TransductionPhosphatidylinositol 4,5-DiphosphateReceptor, EphA2AKTjuxtamembranereceptor tyrosine kinasesingle-moleculeSMALPtransmembrane

Identifiers

PMID33277361
PMCPMC7900517
OpenAlexW3109714469

What Socratic 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 Socratic graph.