Evidence map›Paper›PMID 31711797›Full record

ReviewCytokine & growth factor reviews2019

The transition model of RTK activation: A quantitative framework for understanding RTK signaling and RTK modulator activity.

Michael D Paul, Kalina Hristova

Open access · greenAbstract readReview
In one paragraph

Review in Cytokine & growth factor reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

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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 at 1 institution in 1 country.

Michael D PaulDepartment of Materials Science and Engineering, Institute for NanoBioTechnology, and Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD, 21218, United States.
Kalina HristovaDepartment of Materials Science and Engineering, Institute for NanoBioTechnology, and Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD, 21218, United States. Electronic address: kh@jhu.edu.
Johns Hopkins University · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

Here, we discuss the transition model of receptor tyrosine kinase (RTK) activation, which is derived from biophysical investigations of RTK interactions and signaling. The model postulates that (1) RTKs can interact laterally to form dimers even in the absence of ligand, (2) different unliganded RTK dimers have different stabilities, (3) ligand binding stabilizes the RTK dimers, and (4) ligand binding causes structural changes in the RTK dimer. The model is grounded in the principles of physical chemistry and provides a framework to understand RTK activity and to make predictions in quantitative terms. It can guide basic research aimed at uncovering the mechanism of RTK activation and, in the long run, can empower the search for modulators of RTK function.

Indexed as

Signal TransductionCell MembraneHumansLigandsMutationProtein BindingProtein MultimerizationReceptor Protein-Tyrosine KinasesThermodynamicsLigandsReceptor Protein-Tyrosine KinasesGrowth factorInteractionsReceptor tyrosine kinaseSignaling

Identifiers

PMID31711797
PMCPMC6898792
OpenAlexW2988583904

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.