Evidence map›Paper›PMID 31801826›Full record

ArticleThe Journal of biological chemistry2020

Structural basis of the transmembrane domain dimerization and rotation in the activation mechanism of the TRKA receptor by nerve growth factor.

María L Franco, Kirill D Nadezhdin, Sergey A Goncharuk, Konstantin S Mineev, Alexander S Arseniev, Marçal Vilar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-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

19 citing papers in PubMed, 40 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

6 authors at 2 institutions in 2 countries.

María L FrancoMolecular Basis of Neurodegeneration Unit, Institute of Biomedicine of València, Consejo Superior de Investigaciones Científicas, 46010 València, Spain.
Kirill D NadezhdinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskiy Pereulok 9, Dolgoprudny, Moscow Region 141700, Russian Federation.
Sergey A GoncharukShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskiy Pereulok 9, Dolgoprudny, Moscow Region 141700, Russian Federation.
Konstantin S MineevShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskiy Pereulok 9, Dolgoprudny, Moscow Region 141700, Russian Federation.
Alexander S ArsenievShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskiy Pereulok 9, Dolgoprudny, Moscow Region 141700, Russian Federation. Electronic address: aars@nmr.ru.
Marçal VilarMolecular Basis of Neurodegeneration Unit, Institute of Biomedicine of València, Consejo Superior de Investigaciones Científicas, 46010 València, Spain. Electronic address: mvilar@ibv.csic.es.
Moscow Institute of Physics and Technology · RUConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tropomyosin-receptor kinases (TRKs) are essential for the development of the nervous system. The molecular mechanism of TRKA activation by its ligand nerve growth factor (NGF) is still unsolved. Recent results indicate that at endogenous levels most of TRKA is in a monomer-dimer equilibrium and that the binding of NGF induces an increase of the dimeric and oligomeric forms of this receptor. An unsolved issue is the role of the TRKA transmembrane domain (TMD) in the dimerization of TRKA and the structural details of the TMD in the active dimer receptor. Here, we found that the TRKA-TMD can form dimers, identified the structural determinants of the dimer interface in the active receptor, and validated this interface through site-directed mutagenesis together with functional and cell differentiation studies. Using

Indexed as

Molecular Dynamics SimulationProtein MultimerizationAmino Acid SubstitutionAnimalsBinding SitesCell DifferentiationHeLa CellsHumansNerve Growth FactorPC12 CellsProtein BindingRatsReceptor, trkANerve Growth FactorReceptor, trkAbrain derived neurotrophic factor (BDNF)nerve growth factor (NGF)neurotrophinnuclear magnetic resonance (NMR)p75 neurotrophin receptorreceptor tyrosine kinasetransmembrane domaintropomyosin receptor kinase A (TRKA)tropomyosin receptor kinase B (TRKB)

Identifiers

PMID31801826
PMCPMC6952603
OpenAlexW2993129623

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.