LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration.
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Virological and cellular roles of the transcriptional coactivator LEDGF/p75Structural basis for functional tetramerization of lentiviral integraseA Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase InhibitorsLEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivityHRP2 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.The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication.An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule.Retroviral integrase proteins and HIV-1 DNA integrationFRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75.Chromatinized templates reveal the requirement for the LEDGF/p75 PWWP domain during HIV-1 integration in vitro.Allosteric inhibition of HIV-1 integrase activity.Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein.Identification and characterization of PWWP domain residues critical for LEDGF/p75 chromatin binding and human immunodeficiency virus type 1 infectivity.Integrase, LEDGF/p75 and HIV replication.Biochemical and biophysical analyses of concerted (U5/U3) integration.HIV-1 Integrase-DNA Recognition Mechanisms.The Interaction Between Lentiviral Integrase and LEDGF: Structural and Functional InsightsLEDGINs, non-catalytic site inhibitors of HIV-1 integrase: a patent review (2006 - 2014).HIV-1 integrase multimerization as a therapeutic target.The 156KELK159 tetrapeptide of HIV-1 integrase is critical for lentiviral gene integration.Dynamic Oligomerization of Integrase Orchestrates HIV Nuclear EntryCorrelation of recombinant integrase activity and functional preintegration complex formation during acute infection by replication-defective integrase mutant human immunodeficiency virus.Defining the DNA substrate binding sites on HIV-1 integrase.Cellular and molecular mechanisms of HIV-1 integration targeting.Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Non-dividing CellsBiochemical functions of integrase-binding domain of lens epithelium-derived growth factor
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P2860
LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration.
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2007 nî lūn-bûn
@nan
2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
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2007年論文
@zh-tw
2007年论文
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2007年论文
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2007年论文
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name
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@en
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@nl
type
label
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@en
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@nl
prefLabel
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@en
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@nl
P2860
P1433
P1476
LEDGF/p75 interferes with the ...... ism of viral cDNA integration.
@en
P2093
Alan Engelman
Nidhanapati K Raghavendra
P2860
P356
10.1016/J.VIROL.2006.12.022
P407
P577
2007-01-26T00:00:00Z