Evidence map›Paper›PMID 10595525›Full record

ArticleProtein science : a publication of the Protein Society1999

The interaction of neurotrophins with the p75NTR common neurotrophin receptor: a comprehensive molecular modeling study.

I L Shamovsky, G M Ross, R J Riopelle, D F Weaver

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Role of NGF and its receptors in wound healing (Review).Experimental and therapeutic medicine · 2021
    Review
  4. Neurobiology of zinc and its role in neurogenesis.European journal of nutrition · 2021
    Review
  5. Observational
  6. Circulating biomarkers in extremely preterm infants associated with ultrasound indicators of brain damage.European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society · 2018
    Observational
  7. Observational
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

I L ShamovskyDepartment of Medicine, Queen's University, Kingston, Ontario, Canada.
G M Ross
R J Riopelle
D F Weaver
Queen's University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotrophins are a family of proteins with pleiotropic effects mediated by two distinct receptor types, namely the Trk family, and the common neurotrophin receptor p75NTR. Binding of four mammalian neurotrophins, nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4/5 (NT-4/5), to p75NTR is studied by molecular modeling based on X-ray structures of the neurotrophins and the extracellular domain of p55TNFR, a homologue of p75NTR. The model of neurotrophin/receptor interactions suggests that the receptor binding domains of neurotrophins (loops I and IV) are geometrically and electrostatically complementary to a putative binding site of p75NTR, formed by the second and part of the third cysteine-rich domains. Geometric match of neurotrophin/receptor binding domains in the complexes, as characterized by shape complementarity statistic Sc, is comparable to known protein/protein complexes. All charged residues within the loops I and IV of the neurotrophins, previously determined as being critical for p75NTR binding, directly participate in receptor binding in the framework of the model. Principal residues of the binding site of p75NTR include Asp47, Lys56, Asp75, Asp76, Asp88, and Glu89. The additional involvement of Arg80 and Glu53 is specific for NGF and BDNF, respectively, and Glu73 participates in binding with NT-3 and NT-4/5. Neurotrophins are likely to induce similar, but not identical, conformational changes within the p75NTR binding site.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBrain-Derived Neurotrophic FactorMammalsModels, MolecularMolecular Sequence DataNerve Growth FactorsNeuroprotective AgentsNeurotrophin 3Protein ConformationProtein Structure, SecondaryReceptors, Nerve Growth FactorBrain-Derived Neurotrophic FactorNerve Growth FactorsNeuroprotective AgentsNeurotrophin 3neurotrophin 4neurotrophin 5Receptors, Nerve Growth Factor

Identifiers

PMID10595525
PMCPMC2144181
OpenAlexW2124769381

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.