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TNPO3-mediated nuclear entry of the Rous sarcoma virus Gag protein is independent of the cargo-binding domain

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.03.12.989608Source: DataRank Database

TNPO3-mediated nuclear entry of the Rous sarcoma virus Gag protein is independent of the cargo-binding domain is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2020). On theSindex it has a DataRank of 0.

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Enrichment:Funding (3 grants)OA: greenTopics (32)IDs (PubMed, OpenAlex)SDGs (1)

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Authors (3)

Matthew S. Stake,Leslie J. Parent ORCID,Breanna L. Rice ORCID

Live enrichment

PubMed:19910364 OpenAlex:https://openalex.org/W3012449665

National Institutes of Health

Grant: 2R01CA076534-11

Nuclear Trafficking of the Retroviral Gag Protein

National Institutes of Health

Grant: 1S10OD010756-01A1

Leica SP5 confocal microscope for live-cell imaging

National Institutes of Health

Grant: 5F31CA196292-03

Interaction of Oncoretroviral Gag Protein with Host Nuclear Factors

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2020/04/21/2020.03.12.989608.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2020.03.12.989608

repositoryhttps://doi.org/10.1101/2020.03.12.989608

https://doi.org/10.1128/jvi.00640-20

Fields of Study

Nuclear Structure and FunctionRNA Research and SplicingGenomics and Chromatin Dynamics0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

Nuclear transportCell biologyImportinNuclear localization sequenceRous sarcoma virusNLSNuclear export signalBiologyGroup-specific antigenPlasma protein bindingCell nucleusVirologyNucleusVirusalpha KaryopherinsVirus AssemblyNuclear Localization SignalsActive Transport, Cell NucleusGene Products, gagSaccharomyces cerevisiaeKaryopherinsVirus Internalizationbeta KaryopherinsProtein TransportProtein DomainsNucleocapsid

Sustainable Development Goals

SDG 3: 3. Good health