Evidence map›Paper›PMID 35051416›Full record

ReviewThe Journal of biological chemistry2022

High-affinity TrkA and p75 neurotrophin receptor complexes: A twisted affair.

Jacinta N Conroy, Elizabeth J Coulson

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Nerve growth factor receptor (NGFR): A key player in glioblastoma progression.Biochimica et biophysica acta. Reviews on cancer · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. A lifespan staging model of basal forebrain cholinergic vulnerability.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Novel deep intronic variants inFrontiers in genetics · 2026
    Article
  18. Review
  19. Review
  20. Review
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.

Jacinta N ConroySchool of Biomedical Sciences, The University of Queensland, Brisbane, Queensland, Australia.
Elizabeth J CoulsonSchool of Biomedical Sciences, The University of Queensland, Brisbane, Queensland, Australia; Queensland Brain Institute, The University of Queensland, Brisbane, Queensland, Australia; Clem Jones Centre for Ageing and Disease Research, The University of Queensland, Brisbane, Queensland, Australia. Electronic address: e.coulson@uq.edu.au.
The University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotrophin signaling is essential for normal nervous system development and adult function. Neurotrophins are secreted proteins that signal via interacting with two neurotrophin receptor types: the multifaceted p75 neurotrophin receptor and the tropomyosin receptor kinase receptors. In vivo, neurons compete for the limited quantities of neurotrophins, a process that underpins neural plasticity, axonal targeting, and ultimately survival of the neuron. Thirty years ago, it was discovered that p75 neurotrophin receptor and tropomyosin receptor kinase A form a complex and mediate high-affinity ligand binding and survival signaling; however, despite decades of functional and structural research, the mechanism of modulation that yields this high-affinity complex remains unclear. Understanding the structure and mechanism of high-affinity receptor generation will allow development of pharmaceuticals to modulate this function for treatment of the many nervous system disorders in which altered neurotrophin expression or signaling plays a causative or contributory role. Here we re-examine the key older literature and integrate it with more recent studies on the topic of how these two receptors interact. We also identify key outstanding questions and propose a model of inside-out allosteric modulation to assist in resolving the elusive high-affinity mechanism and complex.

Indexed as

Receptor, Nerve Growth FactorReceptor, trkATropomyosinAnimalsHumansNerve Growth FactorsReceptor Protein-Tyrosine KinasesReceptors, Nerve Growth FactorNerve Growth FactorsReceptor, Nerve Growth FactorReceptor Protein-Tyrosine KinasesReceptors, Nerve Growth FactorReceptor, trkATropomyosinhigh-affinity bindingintracellular domainnerve growth factorneurotrophinp75 neurotrophin receptorreceptor structure-functionreceptor tyrosine kinasetransmembrane domainTrkATrk receptor

Identifiers

PMID35051416
PMCPMC8889134
OpenAlexW4206079600

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.