Evidence map›Paper›PMID 28586369›Full record

ArticlePloS one2017

Synthesis and biochemical characterization of EGF receptor in a water-soluble membrane model system.

Tiffany M Scharadin, Wei He, Yianni Yiannakou, Alexey A Tomilov, Matthew Saldana, Gino A Cortopassi, Kermit L Carraway, Matthew A Coleman, Paul T Henderson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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

9 authors at 3 institutions in 1 country.

Tiffany M ScharadinUniversity of California Davis School of Medicine, Department of Internal Medicine, Division of Hematology Oncology, Sacramento, California, United States of America.
Wei HeLawrence Livermore National Laboratory, Livermore, California, United States of America.
Yianni YiannakouUniversity of California Davis, Nutrition, Davis, California, United States of America.
Alexey A TomilovUniversity of California Davis, School of Veterinary Medicine, Molecular Biosciences, Davis, California, United States of America.
Matthew SaldanaUniversity of California Davis School of Medicine, Biochemistry and Molecular Medicine, Sacramento, California, United States of America.
Gino A CortopassiUniversity of California Davis, School of Veterinary Medicine, Molecular Biosciences, Davis, California, United States of America.
Kermit L CarrawayUniversity of California Davis School of Medicine, Biochemistry and Molecular Medicine, Sacramento, California, United States of America.
Matthew A ColemanLawrence Livermore National Laboratory, Livermore, California, United States of America.
Paul T HendersonUniversity of California Davis School of Medicine, Department of Internal Medicine, Division of Hematology Oncology, Sacramento, California, United States of America.ORCID http://orcid.org/0000-0003-4238-0446
University of California, Davis · USLawrence Livermore National Laboratory · USUC Davis Comprehensive Cancer Center

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
Training Program in Oncogenic Signals and Chromosome BiologyT32CA108459 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI HEYER, WOLF-DIETRICH · 2006 to 2020
$3.6M
NCI NIH HHS P30 CA093373NCI NIH HHS T32 CA108459
6 · The paper itself

Abstract

ErbB (Erythroblastic Leukemia Viral Oncogene Homolog) receptor tyrosine kinases are critical for tissue development and maintenance, and frequently become oncogenic when mutated or overexpressed. In vitro analysis of ErbB receptor kinases can be difficult because of their large size and poor water solubility. Here we report improved production and assembly of the correctly folded full-length EGF receptor (EGFR) into nanolipoprotein particles (NLPs). NLPs are ~10 nm in diameter discoidal cell membrane mimics composed of apolipoproteins surrounding a lipid bilayer. NLPs containing EGFR were synthesized via incubation of baculovirus-produced recombinant EGFR with apolipoprotein and phosphoplipids under conditions that favor self-assembly. The resulting EGFR-NLPs were the correct size, formed dimers and multimers, had intrinsic autophosphorylation activity, and retained the ability to interact with EGFR-targeted ligands and inhibitors consistent with previously-published in vitro binding affinities. We anticipate rapid adoption of EGFR-NLPs for structural studies of full-length receptors and drug screening, as well as for the in vitro characterization of ErbB heterodimers and disease-relevant mutants.

Indexed as

ApolipoproteinsErbB ReceptorsHumansLipid BilayersMembranes, ArtificialNanoparticlesSolubilityWaterApolipoproteinsErbB ReceptorsLipid BilayersMembranes, ArtificialWater

Identifiers

PMID28586369
PMCPMC5460842
OpenAlexW2621771062

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.