The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating. - Test2 - elhamkhani - TriplyDB

The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating.

The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating.

http://www.wikidata.org/entity/Q39253660

about

Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection HIV Genome-Wide Protein Associations: a Review of 30 Years of Research Cellular and viral determinants of retroviral nuclear entry HIV-1 capsid: the multifaceted key player in HIV-1 infection Curing a viral infection by targeting the host: the example of cyclophilin inhibitors A model for cofactor use during HIV-1 reverse transcription and nuclear entry Time-Resolved Imaging of Single HIV-1 Uncoating In Vitro and in Living Cells Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes Principles of Virus Uncoating: Cues and the Snooker Ball Gene expression analysis of a panel of cell lines that differentially restrict HIV-1 CA mutants infection in a cyclophilin a-dependent manner Toward Personalized Gene Therapy: Characterizing the Host Genetic Control of Lentiviral-Vector-Mediated Hepatic Gene Delivery.Transfer of the amino-terminal nuclear envelope targeting domain of human MX2 converts MX1 into an HIV-1 resistance factor The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator 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.Cell-specific RNA aptamer against human CCR5 specifically targets HIV-1 susceptible cells and inhibits HIV-1 infectivity.Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.Microplate-based assay for identifying small molecules that bind a specific intersubunit interface within the assembled HIV-1 capsid.A Novel Entry/Uncoating Assay Reveals the Presence of at Least Two Species of Viral Capsids During Synchronized HIV-1 Infection.Dynamic allostery governs cyclophilin A-HIV capsid interplay TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm.Analysis of the mechanical properties of wild type and hyperstable mutants of the HIV-1 capsid.Molecular Architecture of the Retroviral Capsid.The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6.Evidence for biphasic uncoating during HIV-1 infection from a novel imaging assay.Accumulation of MxB/Mx2-resistant HIV-1 Capsid Variants During Expansion of the HIV-1 Epidemic in Human Populations Cyclophilin A protects mice against infection by influenza A virus.Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes.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.Contribution of PDZD8 to stabilization of the human immunodeficiency virus type 1 capsid.Cyclophilins as modulators of viral replication.Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.The role of immunophilins in viral infection.Cyclophilin A potentiates TRIM5α inhibition of HIV-1 nuclear import without promoting TRIM5α binding to the viral capsid.Reverse Transcription Mechanically Initiates HIV-1 Capsid Disassembly.RNA-Associated Early-Stage Antiviral Factor Is a Major Component of Lv2 Restriction.

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P2860

The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating.

http://www.wikidata.org/entity/Q39253660

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2012 nî lūn-bûn

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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The host proteins transportin ...... ng effects on HIV-1 uncoating.

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Alan Engelman

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Christopher Aiken

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Ilker Oztop

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Jinwoo Ahn

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Jiong Shi

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Lavanya Krishnan

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Matthew S Shotwell

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Vaibhav B Shah

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P2860

Transportin-SR, a nuclear import receptor for SR proteins

Structural insights into the catalytic mechanism of cyclophilin A

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

Cyclophilin A is required for TRIM5{alpha}-mediated resistance to HIV-1 in Old World monkey cells

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

RanGAP1 induces GTPase activity of nuclear Ras-related Ran

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

Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent

Structure of full-length HIV-1 CA: a model for the mature capsid lattice

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422-432

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10.1128/JVI.07177-11

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1

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23097435

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