Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75 - Test2 - elhamkhani - TriplyDB

Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering Lens epithelium-derived growth factor deSumoylation by Sumo-specific protease-1 regulates its transcriptional activation of small heat shock protein and the cellular response Transient and stable knockdown of the integrase cofactor LEDGF/p75 reveals its role in the replication cycle of human immunodeficiency virus Virological and cellular roles of the transcriptional coactivator LEDGF/p75 Transcriptional co-activator LEDGF interacts with Cdc7-activator of S-phase kinase (ASK) and stimulates its enzymatic activity LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration A tripartite DNA-binding element, comprised of the nuclear localization signal and two AT-hook motifs, mediates the association of LEDGF/p75 with chromatin in vivo Impact of Chromatin on HIV Replication Structural basis for functional tetramerization of lentiviral integrase Allosteric Inhibition of Human Immunodeficiency Virus Integrase A Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75 Small Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based Design New Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of Action Interrogating HIV integrase for compounds that bind- a SAMPL challenge Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif Retroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selection LEDGF/p75 proteins with alternative chromatin tethers are functional HIV-1 cofactors Retroviral DNA Integration LEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivity HRP2 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.Augmentation of reverse transcription by integrase through an interaction with host factor, SIP1/Gemin2 Is critical for HIV-1 infection.Molecular modeling study on the allosteric inhibition mechanism of HIV-1 integrase by LEDGF/p75 binding site inhibitors.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.Mass spectrometry-based footprinting of protein-protein interactions An unusual helix turn helix motif in the catalytic core of HIV-1 integrase binds viral DNA and LEDGF.Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding Novel approaches to inhibiting HIV-1 replication.Preclinical profile of BI 224436, a novel HIV-1 non-catalytic-site integrase inhibitor SUMOylation of the lens epithelium-derived growth factor/p75 attenuates its transcriptional activity on the heat shock protein 27 promoter.Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.Association of single nucleotide polymorphisms in the lens epithelium-derived growth factor (LEDGF/p75) with HIV-1 infection outcomes in Brazilian HIV-1+ individuals Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75.Seeing is believing: structure of the catalytic domain of HIV-1 integrase in complex with human LEDGF/p75.Molecular mechanisms of retroviral integration site selection.Phage display-directed discovery of LEDGF/p75 binding cyclic peptide inhibitors of HIV replication.Efficient Transduction of LEDGF/p75 Mutant Cells by Gain-of-Function HIV-1 Integrase Mutant Viruses.The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005 թվականի հունիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Nature Structural & Molecular Biology

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Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75

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Alan Engelman

http://www.w3.org/2001/XMLSchema#string

Gerhard Wagner

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Peter Cherepanov

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Shaila Rahman

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Zhen-Yu J Sun

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P2860

Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation

Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp

Spatial and temporal dynamics of two alternatively spliced regulatory factors, lens epithelium-derived growth factor (ledgf/p75) and p52, in the nucleus

LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells

Specificity of interaction of INI1/hSNF5 with retroviral integrases and its functional significance

LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes

A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery

The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds

RNA recognition via the SAM domain of Smaug

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

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526-532

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scholarly article

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894829

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10.1038/NSMB937

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6

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12

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Goedele Maertens

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2005-05-15T00:00:00Z

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7846509

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15895093

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