HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2
about
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 efficiencyCellular and viral determinants of retroviral nuclear entryEpigenetic control of HIV-1 post integration latency: implications for therapyImpact of Chromatin on HIV ReplicationHIV-1 capsid: the multifaceted key player in HIV-1 infectionA model for cofactor use during HIV-1 reverse transcription and nuclear entryRetroviral integrations in gene therapy trialsThe Road Less Traveled: HIV's Use of Alternative Routes through Cellular PathwaysDynamics and restriction of murine leukemia virus cores in mitotic and interphase cellsCPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 ReplicationCrystal Structure of the N-Terminal Domain of Nup358/RanBP2HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358HIV-1 evades innate immune recognition through specific cofactor recruitmentA new class of multimerization selective inhibitors of HIV-1 integraseBioinformatics and HIV latency.Retroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selectionRetroviral DNA IntegrationThe RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexesCyclophilins 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 integrationHRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor.Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration.The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.Molecular mechanisms of retroviral integration site selection.Host and viral determinants for MxB restriction of HIV-1 infection.Understanding lentiviral vector chromatin targeting: working to reduce insertional mutagenic potential for gene therapy.Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant.Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.TOX4 and NOVA1 proteins are partners of the LEDGF PWWP domain and affect HIV-1 replicationA cyclophilin homology domain-independent role for Nup358 in HIV-1 infection.Decade-long safety and function of retroviral-modified chimeric antigen receptor T cells.Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.Target cell-mediated editing of HIV-1 cDNA by APOBEC3 proteins in human macrophages.Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus.Host Factors in Retroviral Integration and the Selection of Integration Target Sites.TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core.The Role of TNPO3 in HIV-1 Replication.Towards a Safer, More Randomized Lentiviral Vector Integration Profile Exploring Artificial LEDGF Chimeras.
P2860
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P2860
HIV integration targeting: a pathway involving Transportin-3 and the nuclear pore protein RanBP2
description
2011 nî lūn-bûn
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2011 թուականի Մարտին հրատարակուած գիտական յօդուած
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2011 թվականի մարտին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
@wuu
name
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@ast
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@en
type
label
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@ast
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@en
prefLabel
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@ast
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@en
P2093
P2860
P50
P1433
P1476
HIV integration targeting: a p ...... he nuclear pore protein RanBP2
@en
P2093
Alyssa Huegel
Charles C Berry
John A T Young
Keshet Ronen
Leo C James
Nirav Malani
Shoshannah L Roth
Sumit K Chanda
Troy L Brady
P2860
P304
P356
10.1371/JOURNAL.PPAT.1001313
P577
2011-03-10T00:00:00Z