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Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

Cell Reports(2020)10.1016/j.celrep.2020.108538Source: DataRank Database

Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions is a research paper published in Cell Reports (2020). On theSindex it has a DataRank of 0. It has been cited 126 times.

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Open Access126 citations

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Enrichment:Funding (22 grants)Impact (FWCI 6.53)OA: goldTopics (53)IDs (PubMed, PMC, OpenAlex)Annotations (1)

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Findable (1/2)

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Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (14)

Sinem Usluer,Benjamin Bourgeois,Francesca Simonetti ORCID,Hana M. Odeh ORCID,Charlotte M. Fare ORCID

Live enrichment

PubMed:33357437 PMC:PMC7814465 OpenAlex:https://openalex.org/W3117521083

NINDS NIH HHS

Grant: F31 NS111870

Austrian Science Fund FWF

Grant: I 3792

Regulation of RGG-mediated Nuclear Import

Austrian Science Fund FWF

Grant: W 1226

Metabolic and Cardiovascular Disease

NINDS NIH HHS

Grant: R21 NS090205

NIGMS NIH HHS

Grant: T32 GM008275

Deutsche Forschungsgemeinschaft

Grant: unidentified

unidentified

National Institutes of Health

Grant: 1R21NS090205-01A1

Exploring and enhancing Karyopherin beta-2 disaggregate activity

Austrian Science Fund (FWF)

Grant: P 28854

Structural Studies of the ß-Catenin Destruction Complex

National Institutes of Health

Grant: 1F31NS111870-01

Engineering KapB2 to Disaggregate Disease-Linked Proteins

National Institutes of Health

Grant: 5T32GM008275-04

BIOPHYSICAL SPECTROSCOPY TRAINING PROGRAM

Fritz Thyssen Stiftung

National Institutes of Health

Target ALS

Amyotrophic Lateral Sclerosis Association

NOMIS Stiftung

G. Harold and Leila Y. Mathers Charitable Foundation

Association for Frontotemporal Degeneration

Österreichische Forschungsförderungsgesellschaft

Robert Packard Center for ALS Research, Johns Hopkins University

Deutsche Forschungsgemeinschaft

Swiss National Science Foundation

Austrian Science Fund FWF

FWCI

6.53

Citation Percentile

1.0%

Citation Trend

2021

2022

2023

2024

2025

2026

goldLicense: CC BY NC ND

journalhttp://www.cell.com/article/S2211124720315278/pdf

publisherhttp://www.cell.com/article/S2211124720315278/pdf

publisherhttps://api.elsevier.com/content/article/PII:S2211124720315278?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S2211124720315278?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.celrep.2020.108538

Fields of Study

Amyotrophic Lateral Sclerosis ResearchRNA Research and SplicingNeurogenetic and Muscular Disorders Research0301 basic medicine03 medical and health sciences0303 health sciences

MeSH Terms

ArginineDipeptidesHumansReceptors, Cytoplasmic and Nuclear

Keywords

ImportinNuclear transportNeurodegenerationCell biologyNuclear localization sequenceArginineBiologyC9orf72BiochemistryChemistryCytoplasmCell nucleusTrinucleotide repeat expansionAmino acidMedicineGenePhase separationChaperoneALSTdp-43Nuclear Transport ReceptorFtdDipeptide Repeat ProteinsNuclear Import ReceptorNneurodegenerationDipeptides: metabolismReceptors, Cytoplasmic and Nuclear610 Medicine & healthGenetics and Molecular Biology43ArticleALS; FTD; TDP-43; chaperone; dipeptide repeat proteins; importin; nneurodegeneration; nuclear import receptor; nuclear transport receptor; phase separation.Receptors, Cytoplasmic and Nuclear: metabolismTDP1300 General Biochemistry, Genetics and Molecular BiologyHumansphase separation.610 Medicine & healthinfo:eu-repo/classification/ddc/610DipeptidesGeneral BiochemistryArginine: metabolism11493 Department of Quantitative Biomedicine

Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

FAIR Checklist

Authors (14)

Funding (22 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)