Evidence map›Paper›PMID 16798810›Full record

ArticleBiophysical journal2006

Molecular simulation of the binding of nerve growth factor peptide mimics to the receptor tyrosine kinase A.

Marco Berrera, Antonino Cattaneo, Paolo Carloni

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Peptides Derived from Growth Factors to Treat Alzheimer's Disease.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Marco BerreraScuola Internazionale Superiore di Studi Avanzati, Trieste, Italy.
Antonino Cattaneo
Paolo Carloni
Scuola Internazionale Superiore di Studi Avanzati · ITIstituto Nazionale per la Fisica della Materia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nerve growth factor (NGF) mimics play an important role for therapies that target the receptor tyrosine kinase A (trkA). The N-terminal fragment of the NGF (N-term@NGF) was previously demonstrated to be an important determinant for affinity and specificity in the binding to trkA. Here we use a variety of computational tools (contact surface analysis and free energy predictions) to identify residues playing a key role for the binding to the receptor. Molecular dynamics simulations are then used to investigate the stability of complexes between trkA and peptides mimicking N-term@NGF. Steered molecular dynamics calculations are finally performed to investigate the process of detaching the peptide from the receptor. Three disruptive events are observed, the first involving the breaking of all intermolecular interactions except two salt bridges, which break subsequently.

Indexed as

Models, MolecularComputer SimulationMolecular MimicryNerve Growth FactorPeptidesProtein BindingProtein Structure, TertiaryReceptor, trkAThermodynamicsNerve Growth FactorPeptidesReceptor, trkA

Identifiers

PMID16798810
PMCPMC1557562
OpenAlexW1990137541

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.