Evidence map›Paper›PMID 20168077›Full record

ReviewCell adhesion & migration

Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics.

Edwin Li, Kalina Hristova

Abstract readReview
In one paragraph

Review in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
–field-weighted citation impact
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

58 citing papers in PubMed.

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  11. Corneal Vascularization Associated With a Novel PDGFRB Variant.Investigative ophthalmology & visual science · 2023
    Article
  12. Computational analysis of regulatory regions in human protein kinases.Protein science : a publication of the Protein Society · 2023
    Article
  13. Future treatment of Diabetes - Tyrosine Kinase inhibitors.Journal of diabetes and metabolic disorders · 2023
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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

2 authors.

Edwin LiDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD, USA.
Kalina Hristova

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane (TM) domains of receptor tyrosine kinases (RTKs) play an active role in signaling. They contribute to the stability of full-length receptor dimers and to maintaining a signaling-competent dimeric receptor conformation. In an exciting new development, two structures of RTK TM domains have been solved, a break-through achievement in the field. Here we review these structures, and we discuss recent studies of RTK TM domain dimerization energetics, possible synergies between domains, and the effects of pathogenic RTK TM mutations on structure and dimerization.

Indexed as

AnimalsCell MembraneDimerizationHumansProtein Structure, TertiaryReceptor Protein-Tyrosine KinasesSignal TransductionReceptor Protein-Tyrosine Kinases

Identifiers

PMID20168077
PMCPMC2900622

What OpenQuestion holds

Textmetadata
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.