About: Nathalie Arhel

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) wetenschapper (nl) дослідниця (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtuese (sq) ricercatrice (it)
rdfs:label	Nathalie Arhel (en) Nathalie Arhel (es) Nathalie Arhel (nl) Nathalie Arhel (sl) Nathalie Arhel (ast)
skos:prefLabel	Nathalie Arhel (en) Nathalie Arhel (es) Nathalie Arhel (nl) Nathalie Arhel (sl) Nathalie Arhel (ast)
name	Nathalie Arhel (en) Nathalie Arhel (es) Nathalie Arhel (nl) Nathalie Arhel (sl) Nathalie Arhel (ast)
given name	wds:Q42767978-CD1E8FED-0A85-4417-8151-00DF4C33C250
given name	Nathalie
instance of	wds:Q42767978-82CB9D32-B01D-47DE-BA03-8E0DEF59B943
instance of	Homo sapiens
skos:altLabel	Nathalie Jane Arhel (en)
occupation	wds:Q42767978-69F840DC-3DA7-4C22-80E8-CBD73BEE9F81
employer	wds:Q42767978-574A5540-5C72-4F10-B7BB-115AFF513AC1 wds:Q42767978-BC50371A-2070-45E7-B572-C6310E3FB6CD
sex or gender	wds:Q42767978-1ECF0ABE-D04F-4A73-83C8-3CD79F923B31
VIAF ID	wds:Q42767978-B7EC5587-5F5F-4A50-BF72-E50D7A87B859
GND ID	wds:Q42767978-ee257d70-c2bc-4d56-9e3b-9c666dd9d38c
IdRef ID	wds:Q42767978-09C1BFAE-113A-49FF-A8DE-CEF35E3563F1
WorldCat Identities ID (superseded)	wds:Q42767978-B2BCB2BA-6112-49C2-AA78-972D101F8E78
VIAF ID	http://viaf.org/viaf/103261370
GND ID	https://d-nb.info/gnd/139936203
IdRef ID	http://www.idref.fr/188421106/id
occupation	researcher
employer	Institute of Human Genetics Délégation Languedoc Roussillon
sex or gender	female organism
VIAF ID	103261370
GND ID	139936203
IdRef ID	188421106
WorldCat Identities ID (superseded)	viaf-103261370
ORCID iD	wds:Q42767978-6F4218BD-7459-48A4-B1F3-1A35FB4E085C
ORCID iD	https://orcid.org/0000-0001-5309-1725
ORCID iD	0000-0001-5309-1725
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42767978
is author of	HIV-derived vectors for therapy and vaccination against HIV. Revisiting HIV-1 uncoating The inability to disrupt the immunological synapse between infected human T cells and APCs distinguishes HIV-1 from most other primate lentiviruses. Implications of Nef: host cell interactions in viral persistence and progression to AIDS. The role of the retinoblastoma protein (Rb) in the nuclear localization of BAG-1: implications for colorectal tumour cell survival TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core PML/TRIM19-Dependent Inhibition of Retroviral Reverse-Transcription by Daxx The cationic properties of SEVI underlie its ability to enhance human immunodeficiency virus infection HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore Quantitative four-dimensional tracking of cytoplasmic and nuclear HIV-1 complexes. Host proteins involved in HIV infection: new therapeutic targets. Role of Nef in primate lentiviral immunopathogenesis Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration Nuclear BAG-1 expression inhibits apoptosis in colorectal adenoma-derived epithelial cells. The retinoblastoma protein interacts with Bag-1 in human colonic adenoma and carcinoma derived cell lines Superresolution imaging of HIV in infected cells with FlAsH-PALM TRIM5α is a SUMO substrate Nuclear import defect of human immunodeficiency virus type 1 DNA flap mutants is not dependent on the viral strain or target cell type HIV trafficking in host cells: motors wanted! Lack of endogenous TRIM5 -mediated restriction in rhesus macaque dendritic cells Microtubule-associated proteins 1 (MAP1) promote human immunodeficiency virus type I (HIV-1) intracytoplasmic routing to the nucleus Correction: Human Nucleoporins Promote HIV-1 Docking at the Nuclear Pore, Nuclear Import and Integration. Wild-type and central DNA flap defective HIV-1 lentiviral vector genomes: intracellular visualization at ultrastructural resolution levels TRIM8 is required for virus-induced IFN response in human plasmacytoid dendritic cells HIV-1 capsid interacts with cytoskeletal-associated proteins for intracytoplasmic routing to the nucleus CD95 co-stimulation blocks activation of naive T cells by inhibiting T cell receptor signaling CrAsH-quantum dot nanohybrids for smart targeting of proteins. Endogenous TRIM5α Function Is Regulated by SUMOylation and Nuclear Sequestration for Efficient Innate Sensing in Dendritic Cells Transportin-1 binds to the HIV-1 capsid via a nuclear localization signal and triggers uncoating A doubly responsive probe for the detection of Cys4-tagged proteins. Role of non-motile microtubule-associated proteins in virus trafficking. L’observation microscopique du virus VIH-1 dans les cellules infectées HIV capsid and productive infection: taking steps in the right direction Residual HIV-1 DNA Flap-independent nuclear import of cPPT/CTS double mutant viruses does not support spreading infection RanBP2 regulates the anti-retroviral activity of TRIM5α by SUMOylation at a predicted phosphorylated SUMOylation motif [SUMO regulates the capacity of TRIM5α to inhibit HIV-1] In vitro screening of a FDA approved chemical library reveals potential inhibitors of SARS-CoV-2 replication Vpu modulates DNA repair to suppress innate sensing and hyper-integration of HIV-1 Early HIV replication revisited Bisarsenical labeling of HIV-1 for real-time fluorescence microscopy. [Transportin-1 orchestrates HIV-1 uncoating and nuclear entry] Daxx Inhibits HIV-1 Reverse Transcription and Uncoating in a SUMO-Dependent Manner Identifying enhancers of innate immune signaling as broad-spectrum antivirals active against emerging viruses

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