Evidence map›Paper›PMID 25223306›Full record

ArticleJournal of the American Society for Mass Spectrometry2014

The influence of adnectin binding on the extracellular domain of epidermal growth factor receptor.

Roxana E Iacob, Guodong Chen, Joomi Ahn, Stephane Houel, Hui Wei, Jingjie Mo, Li Tao, Daniel Cohen, Dianlin Xie, Zheng Lin and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. 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

14 authors at 3 institutions in 1 country.

Roxana E IacobDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, 02115, USA.
Guodong Chen
Joomi Ahn
Stephane Houel
Hui Wei
Jingjie Mo
Li Tao
Daniel Cohen
Dianlin Xie
Zheng Lin
Paul E Morin
Michael L Doyle
Adrienne A Tymiak
John R Engen
Bristol-Myers Squibb (United States) · USNortheastern University · USWaters (United States) · US

Funding

Protein conformational change upon membrane associationR01GM086507 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2009 to 2012
$1.6M
Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS GM086507NIGMS NIH HHS GM 101135NIGMS NIH HHS R01 GM086507NIGMS NIH HHS R01 GM101135
6 · The paper itself

Abstract

The precise and unambiguous elucidation and characterization of interactions between a high affinity recognition entity and its cognate protein provides important insights for the design and development of drugs with optimized properties and efficacy. In oncology, one important target protein has been shown to be the epidermal growth factor receptor (EGFR) through the development of therapeutic anticancer antibodies that are selective inhibitors of EGFR activity. More recently, smaller protein derived from the 10th type III domain of human fibronectin termed an adnectin has also been shown to inhibit EGFR in clinical studies. The mechanism of EGFR inhibition by either an adnectin or an antibody results from specific binding of the high affinity protein to the extracellular portion of EGFR (exEGFR) in a manner that prevents phosphorylation of the intracellular kinase domain of the receptor and thereby blocks intracellular signaling. Here, the structural changes induced upon binding were studied by probing the solution conformations of full length exEGFR alone and bound to a cognate adnectin through hydrogen/deuterium exchange mass spectrometry (HDX MS). The effects of binding in solution were identified and compared with the structure of a bound complex determined by X-ray crystallography.ᅟ

Indexed as

Binding SitesCrystallography, X-RayDeuterium Exchange MeasurementErbB ReceptorsFibronectinsHumansModels, MolecularProtein BindingProtein Structure, TertiaryErbB ReceptorsFibronectins

Identifiers

PMID25223306
PMCPMC4224629
OpenAlexW1981842336

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.