Flexible use of nuclear import pathways by HIV-1. - Test2 - elhamkhani - TriplyDB

Flexible use of nuclear import pathways by HIV-1.

Flexible use of nuclear import pathways by HIV-1.

http://www.wikidata.org/entity/Q33739260

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Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2)HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection MX2 is an interferon-induced inhibitor of HIV-1 infection HIV type 1 Gag as a target for antiviral therapy Cellular and viral determinants of retroviral nuclear entry HIV-1 capsid: the multifaceted key player in HIV-1 infection Misdelivery at the Nuclear Pore Complex-Stopping a Virus Dead in Its Tracks A model for cofactor use during HIV-1 reverse transcription and nuclear entry Cellular self-defense: how cell-autonomous immunity protects against pathogens Virus strategies for passing the nuclear envelope barrier HIV-1 reverse transcription Nuclear trafficking of retroviral RNAs and Gag proteins during late steps of replication The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways Dynamics and restriction of murine leukemia virus cores in mitotic and interphase cells KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication Gain-of-Sensitivity Mutations in a Trim5-Resistant Primary Isolate of Pathogenic SIV Identify Two Independent Conserved Determinants of Trim5α Specificity Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358 HIV-1 evades innate immune recognition through specific cofactor recruitment Structural basis for nuclear import of splicing factors by human Transportin 3 Gene expression analysis of a panel of cell lines that differentially restrict HIV-1 CA mutants infection in a cyclophilin a-dependent manner Lv4 Is a Capsid-Specific Antiviral Activity in Human Blood Cells That Restricts Viruses of the SIVMAC/SIVSM/HIV-2 Lineage Prior to Integration Retroviral DNA Integration Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates.Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration.Differential effects of human immunodeficiency virus type 1 capsid and cellular factors nucleoporin 153 and LEDGF/p75 on the efficiency and specificity of viral DNA integration Superresolution imaging of HIV in infected cells with FlAsH-PALM HIV-1 uncoating is facilitated by dynein and kinesin 1 HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus.Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration.Nuclear trafficking of the HIV-1 pre-integration complex depends on the ADAM10 intracellular domain.Structural basis for spumavirus GAG tethering to chromatin Microbial Natural Product Alternariol 5-O-Methyl Ether Inhibits HIV-1 Integration by Blocking Nuclear Import of the Pre-Integration Complex.HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2 Interactions between HIV-1 and the cell-autonomous innate immune system.

P2860

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P2860

Flexible use of nuclear import pathways by HIV-1.

http://www.wikidata.org/entity/Q33739260

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Flexible use of nuclear import pathways by HIV-1.

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Flexible use of nuclear import pathways by HIV-1.

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Flexible use of nuclear import pathways by HIV-1.

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Flexible use of nuclear import pathways by HIV-1.

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Flexible use of nuclear import pathways by HIV-1.

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Flexible use of nuclear import pathways by HIV-1.

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J.CHOM.2010.02.007

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Cell Host & Microbe

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Flexible use of nuclear import pathways by HIV-1.

@en

P2093

Alan Engelman

http://www.w3.org/2001/XMLSchema#string

Alok Mulky

http://www.w3.org/2001/XMLSchema#string

Dan R Littman

http://www.w3.org/2001/XMLSchema#string

Derya Unutmaz

http://www.w3.org/2001/XMLSchema#string

Ichiro Taniuchi

http://www.w3.org/2001/XMLSchema#string

Ilker Oztop

http://www.w3.org/2001/XMLSchema#string

Joerg G Baumann

http://www.w3.org/2001/XMLSchema#string

John G Julias

http://www.w3.org/2001/XMLSchema#string

John M Coffin

http://www.w3.org/2001/XMLSchema#string

Kenneth Shelton

http://www.w3.org/2001/XMLSchema#string

P2860

tRNAs promote nuclear import of HIV-1 intracellular reverse transcription complexes

Chimpanzee reservoirs of pandemic and nonpandemic HIV-1

How Viruses Enter Animal Cells

Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization

Identification of host proteins required for HIV infection through a functional genomic screen

Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex

Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor

The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells

HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway

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221-233

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scholarly article

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10.1016/J.CHOM.2010.02.007

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3

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7

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Joseph Sodroski

Stephen H. Hughes

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2010-03-01T00:00:00Z

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41943184

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20227665

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2841689

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