Evidence map›Paper›PMID 29630862›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Interactions between NRP1 and VEGFR2 molecules in the plasma membrane.

Christopher King, Daniel Wirth, Samuel Workman, Kalina Hristova

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

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  12. Revisiting a controversy: The effect of EGF on EGFR dimer stability.Biochimica et biophysica acta. Biomembranes · 2020
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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

4 authors at 1 institution in 1 country.

Christopher KingProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States.
Daniel WirthDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore, MD 21218, United States.
Samuel WorkmanDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore, MD 21218, United States.
Kalina HristovaDepartment of Materials Science and Engineering and Institute for NanoBioTechnology, Johns Hopkins University, Baltimore, MD 21218, United States; Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States. Electronic address: kh@jhu.edu.
Johns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

Here we use a quantitative FRET approach, specifically developed to probe membrane protein interactions, to study the homo-association of neuropilin 1 (NRP1) in the plasma membrane, as well as its hetero-interactions with vascular endothelial growth factor receptor 2 (VEGFR2). Experiments are performed both in the absence and presence of the soluble ligand vascular endothelial growth factor A (VEGFA), which binds to both VEGFR2 and NRP1. We demonstrate the presence of homo-interactions between NRP1 molecules, as well as hetero-interactions between NRP1 and VEGFR2 molecules, in the plasma membrane. Our results underscore the complex nature of the interactions between self-associating receptors, co-receptors, and their ligands in the plasma membrane. They also highlight the need for new methodologies that capture this complexity, and the need for precise physiological measurements of local receptor surface densities in the membrane of cells. This article is part of a Special Issue entitled: Emergence of Complex Behavior in Biomembranes edited by Marjorie Longo.

Indexed as

Cell MembraneEndothelium, VascularFluorescence Resonance Energy TransferHEK293 CellsHumansLigandsNeuropilin-1Signal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2KDR protein, humanLigandsNeuropilin-1NRP1 protein, humanVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2VEGFA protein, humanInteractionsMembrane proteinPlasma membraneReceptor

Identifiers

PMID29630862
PMCPMC6177318
OpenAlexW2795935511

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.