Evidence map›Paper›PMID 28019699›Full record

ArticleProteins2017

Conformational stability of the epidermal growth factor (EGF) receptor as influenced by glycosylation, dimerization and EGF hormone binding.

Eric S Taylor, Laercio Pol-Fachin, Roberto D Lins, Steven K Lower

Abstract read
In one paragraph

Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  8. Elevated UDP-glucuronic acid levels mend drug resistance and stress responses via a protease and a transporter inProceedings of the National Academy of Sciences of the United States of America · 2025
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  17. I-branched carbohydrates as emerging effectors of malignant progression.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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 3 institutions in 2 countries.

Eric S TaylorDepartment of Geology, Kent State University, North Canton, Ohio, 44720.
Laercio Pol-FachinAggeu Magalhães Research Center, Oswaldo Cruz Foundation, Recife, Pernambuco, 50740-465, Brazil.ORCID 0000-0002-4621-3031
Roberto D LinsAggeu Magalhães Research Center, Oswaldo Cruz Foundation, Recife, Pernambuco, 50740-465, Brazil.
Steven K LowerSchool of Environment and Natural Resources, Ohio State University, 275 Mendenhall Laboratory, Columbus, Ohio, 43210.
Universidade Federal de Pernambuco · BRKent State University · USOhio Department of Natural Resources · US

Funding

Molecular binding reaction that initiates Staphylococcus aureus infections of carR01HL119648 · NHLBI · OHIO STATE UNIVERSITY · PI LOWER, STEVEN K · 2014 to 2018
$3.0M
NHLBI NIH HHS R01 HL119648
6 · The paper itself

Abstract

The epidermal growth factor receptor (EGFR) is an important transmembrane glycoprotein kinase involved the initiation or perpetuation of signal transduction cascades within cells. These processes occur after EGFR binds to a ligand [epidermal growth factor (EGF)], thus inducing its dimerization and tyrosine autophosphorylation. Previous publications have highlighted the importance of glycosylation and dimerization for promoting proper function of the receptor and conformation in membranes; however, the effects of these associations on the protein conformational stability have not yet been described. Molecular dynamics simulations were performed to characterize the conformational preferences of the monomeric and dimeric forms of the EGFR extracellular domain upon binding to EGF in the presence and absence of N-glycan moieties. Structural stability analyses revealed that EGF provides the most conformational stability to EGFR, followed by glycosylation and dimerization, respectively. The findings also support that EGF-EGFR binding takes place through a large-scale induced-fitting mechanism. Proteins 2017; 85:561-570. © 2016 Wiley Periodicals, Inc.

Indexed as

Molecular Dynamics SimulationAcetylglucosamineAsparagineBinding SitesEpidermal Growth FactorErbB ReceptorsGlycosylationHumansProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein StabilityProtein Structure, SecondaryThermodynamicsAcetylglucosamineAsparagineEGFR protein, humanEpidermal Growth FactorErbB ReceptorsEGF bindingErbBglycoproteinmolecular dynamics

Identifiers

PMID28019699
PMCPMC5835389
OpenAlexW2566322373

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.