Evidence map›Paper›PMID 28090201›Full record

ArticleFrontiers in neuroscience2016

The Inorganic Side of NGF: Copper(II) and Zinc(II) Affect the NGF Mimicking Signaling of the N-Terminus Peptides Encompassing the Recognition Domain of TrkA Receptor.

Giuseppe Pandini, Cristina Satriano, Adriana Pietropaolo, Fiorenza Gianì, Alessio Travaglia, Diego La Mendola, Vincenzo G Nicoletti, Enrico Rizzarelli

Open access · goldAbstract read
In one paragraph

Article in Frontiers in neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

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  10. Review
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  12. Peptides Derived from Angiogenin Regulate Cellular Copper Uptake.International journal of molecular sciences · 2021
    Article
  13. Peptides Derived from Growth Factors to Treat Alzheimer's Disease.International journal of molecular sciences · 2021
    Review
  14. Article
  15. The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells.International journal of molecular sciences · 2020
    Article
  16. Nerve growth factor catches copper in neuronal inning.Neural regeneration research · 2020
    Article
  17. Article
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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

8 authors at 5 institutions in 2 countries.

Giuseppe PandiniEndocrinology, Department of Clinical and Experimental Medicine, Garibaldi-Nesima Medical Center, University of CataniaCatania, Italy; Institute of Biostructures and Bioimages - Catania, National Research CouncilCatania, Italy.
Cristina SatrianoDepartment of Chemical Sciences, University of CataniaCatania, Italy; Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi BiologiciBari, Italy.
Adriana PietropaoloDepartment of Health Sciences, University of Catanzaro Catanzaro, Italy.
Fiorenza GianìEndocrinology, Department of Clinical and Experimental Medicine, Garibaldi-Nesima Medical Center, University of CataniaCatania, Italy; Institute of Biostructures and Bioimages - Catania, National Research CouncilCatania, Italy.
Alessio TravagliaCentre for Neural Science, New York University New York, NY, USA.
Diego La MendolaConsorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi BiologiciBari, Italy; Department of Pharmacy, University of PisaPisa, Italy.
Vincenzo G NicolettiConsorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi BiologiciBari, Italy; Section of Medical Biochemistry, Department of Biomedical and Biotechnological Sciences (BIOMETEC), University of CataniaCatania, Italy.
Enrico RizzarelliInstitute of Biostructures and Bioimages - Catania, National Research CouncilCatania, Italy; Department of Chemical Sciences, University of CataniaCatania, Italy; Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi BiologiciBari, Italy.
Consorzio Interuniversitario Reattività Chimica e Catalisi · ITInstitute of Biostructure and Bioimaging · ITNational Research Council · ITNew York University · USUniversity of Catania · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nerve growth factor (NGF) N-terminus peptide, NGF(1-14), and its acetylated form, Ac-NGF(1-14), were investigated to scrutinize the ability of this neurotrophin domain to mimic the whole protein. Theoretical calculations demonstrated that non-covalent forces assist the molecular recognition of TrkA receptor by both peptides. Combined parallel tempering/docking simulations discriminated the effect of the N-terminal acetylation on the recognition of NGF(1-14) by the domain 5 of TrkA (TrkA-D5). Experimental findings demonstrated that both NGF(1-14) and Ac-NGF(1-14) activate TrkA signaling pathways essential for neuronal survival. The NGF-induced TrkA internalization was slightly inhibited in the presence of Cu

Indexed as

Alzheimer's diseaseBDNFCREBionophoremetal ionsnanomedicineneurotrophinspeptidomimetics

Identifiers

PMID28090201
PMCPMC5201159
OpenAlexW2560873663

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.