Human immunodeficiency virus type 1 capsid mutation N74D alters cyclophilin A dependence and impairs macrophage infection. - Wikidata - wikimedia - TriplyDB

Human immunodeficiency virus type 1 capsid mutation N74D alters cyclophilin A dependence and impairs macrophage infection.

Human immunodeficiency virus type 1 capsid mutation N74D alters cyclophilin A dependence and impairs macrophage infection.

http://www.wikidata.org/entity/Q35868118

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A model for cofactor use during HIV-1 reverse transcription and nuclear entry HIV-1 evades innate immune recognition through specific cofactor recruitment How SLX4 cuts through the mystery of HIV-1 Vpr-mediated cell cycle arrest.Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.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 Nuclear trafficking of the HIV-1 pre-integration complex depends on the ADAM10 intracellular domain.The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.Extreme genetic fragility of the HIV-1 capsid.Compensatory substitutions in the HIV-1 capsid reduce the fitness cost associated with resistance to a capsid-targeting small-molecule inhibitor.Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.A cyclophilin homology domain-independent role for Nup358 in HIV-1 infection.HIV-1 capsid-targeting domain of cleavage and polyadenylation specificity factor 6 Functional constraints on HIV-1 capsid: their impacts on the viral immune escape potency.Analysis of the mechanical properties of wild type and hyperstable mutants of the HIV-1 capsid.Enhanced autointegration in hyperstable simian immunodeficiency virus capsid mutants blocked after reverse transcription Nuclear Envelope Protein SUN2 Promotes Cyclophilin-A-Dependent Steps of HIV Replication The Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.What Integration Sites Tell Us about HIV Persistence Characterization of two distinct early post-entry blocks to HIV-1 in common marmoset lymphocytes.Cyclophilin A promotes HIV-1 reverse transcription but its effect on transduction correlates best with its effect on nuclear entry of viral cDNA.HIV-1 uncoating: connection to nuclear entry and regulation by host proteins.Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.Safeguard against DNA sensing: the role of TREX1 in HIV-1 infection and autoimmune diseases.Cyclophilin A potentiates TRIM5α inhibition of HIV-1 nuclear import without promoting TRIM5α binding to the viral capsid.Imaging HIV-1 Genomic DNA from Entry through Productive Infection Potent and reversible lentiviral vector restriction in murine induced pluripotent stem cells.Complex Interplay between HIV-1 Capsid and MX2-Independent Alpha Interferon-Induced Antiviral Factors.Direct Visualization of HIV-1 Replication Intermediates Shows that Capsid and CPSF6 Modulate HIV-1 Intra-nuclear Invasion and Integration HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry.Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid Capsid-Dependent Host Factors in HIV-1 Infection.The susceptibility of primate lentiviruses to nucleosides and Vpx during infection of dendritic cells is regulated by CA.Early cytoplasmic uncoating is associated with infectivity of HIV-1.Capsid-CPSF6 Interaction Is Dispensable for HIV-1 Replication in Primary Cells but Is Selected during Virus Passage In Vivo.Roles of Capsid-Interacting Host Factors in Multimodal Inhibition of HIV-1 by PF74.Identification of capsid mutations that alter the rate of HIV-1 uncoating in infected cells.In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects.Keeping your armour intact: how HIV-1 evades detection by the innate immune system: HIV-1 capsid controls detection of reverse transcription products by the cytosolic DNA sensor cGAS.The KT Jeang Retrovirology prize 2017: Michael Emerman.

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Human immunodeficiency virus type 1 capsid mutation N74D alters cyclophilin A dependence and impairs macrophage infection.

http://www.wikidata.org/entity/Q35868118

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2012 nî lūn-bûn

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Human immunodeficiency virus t ...... impairs macrophage infection.

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Human immunodeficiency virus t ...... impairs macrophage infection.

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Human immunodeficiency virus t ...... impairs macrophage infection.

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Human immunodeficiency virus t ...... impairs macrophage infection.

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Alan Engelman

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Derya Unutmaz

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Hongzhan Xu

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Ilker Oztop

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James Matous

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Jean Ndjomou

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KyeongEun Lee

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Taichiro Takemura

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Vineet N KewalRamani

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Zandrea Ambrose

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P2860

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

SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx

Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein

Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection

The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys

Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication

Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1

Evidence for direct involvement of the capsid protein in HIV infection of nondividing cells.

Primate lentiviral Vpx commandeers DDB1 to counteract a macrophage restriction.

Flexible use of nuclear import pathways by HIV-1.

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4708-4714

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10.1128/JVI.05887-11

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8

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86

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Stephen H. Hughes

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2012-02-01T00:00:00Z

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22301145

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3318671

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