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Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity

The Journal of Neuroscience(2016)10.1523/jneurosci.2649-15.2016Source: DataRank Database

Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity is a research paper published in The Journal of Neuroscience (2016). On theSindex it has a DataRank of 0.587. It has been cited 49 times.

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0.587DataRank · unranked

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49 citations

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Enrichment:Funding (1 grants)Impact (FWCI 1.55)OA: bronzeTopics (53)Linked Datasets (18)DataCite Reuse (18)IDs (PubMed, PMC, OpenAlex)Annotations (1)

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Context only (not used in score)

Findable (2/2)

Has DOI
Indexed in repositories

Accessible (0/2)

Interoperable (2/2)

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Reusable (0/3)

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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.587

From this paper's citation signal

Citation Network Contribution

Citation network not refreshed for this result

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Authors (8)

Jonas Englund,Rimante Minkeviciene ORCID,Mikko Koskinen,Mikael Segerstråle,Eero Ċastrén ORCID

Live enrichment

PubMed:27170127 PMC:PMC6601809 OpenAlex:https://openalex.org/W2365345520

European Research Council

Grant: 322742

FWCI

1.55

Citation Percentile

0.8%

Citation Trend

2017

2018

2019

2020

2021

2022

2023

2024

2025

2026

bronzeLicense: https://creativecommons.org/licenses/by-nc-sa/4.0/

journalhttps://www.jneurosci.org/content/jneuro/36/19/5299.full.pdf

HYBRIDhttps://www.jneurosci.org/content/jneuro/36/19/5299.full.pdf

publisherhttps://www.jneurosci.org/content/jneuro/36/19/5299.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1523/JNEUROSCI.2649-15.2016

journalhttps://doi.org/10.1523/jneurosci.2649-15.2016

Fields of Study

Neuroscience and Neuropharmacology ResearchCellular Mechanics and InteractionsNeurogenesis and neuroplasticity mechanismsBiologyMedicineActin CytoskeletonActinsAnimalsCell Line, TumorCells, CulturedDendritic SpinesFemaleHumansLong-Term PotentiationMaleNeurogenesisPhosphorylationProtein Processing, Post-TranslationalRatsTyrosine

MeSH Terms

ActinsAnimalsCells, CulturedFemaleHumansMaleActin CytoskeletonPhosphorylationProtein Processing, Post-TranslationalTyrosineLong-Term PotentiationCell Line, TumorDendritic SpinesRatsNeurogenesis

Keywords

Synaptic plasticityNeurosciencePhosphorylationPlasticityTyrosine phosphorylationNeuroplasticityTyrosineNonsynaptic plasticityCell biologyBiologyMetaplasticityChemistryBiochemistryMaterials scienceLTPActin cytoskeletonDendritic SpinesSpinogenesis

Additional file 8 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062514figshare

Additional file 9 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062517.v1figshare

Additional file 3 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062499figshare

Additional file 7 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062511.v1figshare

Additional file 7 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062511figshare

Additional file 8 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062514.v1figshare

Additional file 9 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062517figshare

Additional file 5 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062505figshare

Additional file 5 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062505.v1figshare

Additional file 6 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062508figshare

Additional file 3 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062499.v1figshare

Additional file 4 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062502.v1figshare

Additional file 4 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062502figshare

Additional file 6 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062508.v1figshare

Additional file 1 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062493.v1figshare

Additional file 2 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062496.v1figshare

Additional file 2 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062496figshare

Additional file 1 of Quantitative proteomic and phosphoproteomic analysis reveal the relationship between mitochondrial dysfunction and cytoskeletal remodeling in hiPSC-CMs deficient in PINK1

10.6084/m9.figshare.24062493figshare

Related Papers (1)

Biophysical model of the role of actin remodeling on dendritic spine morphology

N/A

2.2DataRank · unranked

PLOS ONE(2017)

co-cited

10.1371/journal.pone.0170113

Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity

FAIR Checklist

DataRank Breakdown

Authors (8)

Funding (1 grants)

Impact

Open Access

Topics

Linked Datasets (18)

Annotations (Europe PMC)

Related Papers (1)