Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase
about
The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tetheringLens epithelium-derived growth factor deSumoylation by Sumo-specific protease-1 regulates its transcriptional activation of small heat shock protein and the cellular responseVirological and cellular roles of the transcriptional coactivator LEDGF/p75Transcriptional co-activator LEDGF interacts with Cdc7-activator of S-phase kinase (ASK) and stimulates its enzymatic activityLEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integrationA tripartite DNA-binding element, comprised of the nuclear localization signal and two AT-hook motifs, mediates the association of LEDGF/p75 with chromatin in vivoExpression of hepatoma-derived growth factor family members in the adult central nervous system.HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchImpact of Chromatin on HIV ReplicationStructural basis for functional tetramerization of lentiviral integraseEmbryonic Lethality Due to Arrested Cardiac Development in Psip1/Hdgfrp2 Double-Deficient MiceAllosteric Inhibition of Human Immunodeficiency Virus IntegraseA Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding siteSmall Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based DesignCrystal structures of novel allosteric peptide inhibitors of HIV integrase identify new interactions at the LEDGF binding siteAllosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturationThe A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase InhibitorsMultimode, Cooperative Mechanism of Action of Allosteric HIV-1 Integrase InhibitorsNew Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of ActionMultiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motifRetroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selectionSolution structure of the HIV-1 integrase-binding domain in LEDGF/p75LEDGF/p75 proteins with alternative chromatin tethers are functional HIV-1 cofactorsNon-catalytic site HIV-1 integrase inhibitors disrupt core maturation and induce a reverse transcription block in target cellsNuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel DNA-binding domainInteraction of HRP-2 isoforms with HDGF: chromatin binding of a specific heteromerRetroviral DNA IntegrationLEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivityDifferential 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.Virus evolution reveals an exclusive role for LEDGF/p75 in chromosomal tethering of HIV.Role of PSIP1/LEDGF/p75 in lentiviral infectivity and integration targeting.The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication.Screening for antiviral inhibitors of the HIV integrase-LEDGF/p75 interaction using the AlphaScreen luminescent proximity assay.Integration site selection by retroviral vectors: molecular mechanism and clinical consequences.Specificity of antinuclear autoantibodies recognizing the dense fine speckled nuclear pattern: Preferential targeting of DFS70/LEDGFp75 over its interacting partner MeCP2An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule.Dynamics of the ternary complex formed by c-Myc interactor JPO2, transcriptional co-activator LEDGF/p75, and chromatin.The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase.
P2860
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P2860
Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase
description
2004 nî lūn-bûn
@nan
2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Identification of an evolution ...... 75) that binds HIV-1 integrase
@ast
Identification of an evolution ...... 75) that binds HIV-1 integrase
@en
Identification of an evolution ...... 75) that binds HIV-1 integrase
@nl
type
label
Identification of an evolution ...... 75) that binds HIV-1 integrase
@ast
Identification of an evolution ...... 75) that binds HIV-1 integrase
@en
Identification of an evolution ...... 75) that binds HIV-1 integrase
@nl
prefLabel
Identification of an evolution ...... 75) that binds HIV-1 integrase
@ast
Identification of an evolution ...... 75) that binds HIV-1 integrase
@en
Identification of an evolution ...... 75) that binds HIV-1 integrase
@nl
P2093
P2860
P3181
P356
P1476
Identification of an evolution ...... 75) that binds HIV-1 integrase
@en
P2093
Alan Engelman
Eric Devroe
Peter Cherepanov
P2860
P304
P3181
P356
10.1074/JBC.M406307200
P407
P577
2004-11-19T00:00:00Z