Degradation of HIV-1 integrase by the N-end rule pathway - Wikidata - awgldk - TriplyDB

Degradation of HIV-1 integrase by the N-end rule pathway

Degradation of HIV-1 integrase by the N-end rule pathway

http://www.wikidata.org/entity/Q28140723

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Genome-wide association study identifies single nucleotide polymorphism in DYRK1A associated with replication of HIV-1 in monocyte-derived macrophages Effect of DNA repair protein Rad18 on viral infection LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons.Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration Interaction of HIV-1 integrase with DNA repair protein hRad18 Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75 Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase Fates of retroviral core components during unrestricted and TRIM5-restricted infection Consensus HIV-1 FSU-A integrase gene variants electroporated into mice induce polyfunctional antigen-specific CD4+ and CD8+ T cells Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway Retroviral DNA Integration The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication.Identifying potential survival strategies of HIV-1 through virus-host protein interaction networks.GCN2 phosphorylates HIV-1 integrase and decreases HIV-1 replication by limiting viral integration.Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins.Subcellular localization and expression of bamboo mosaic virus satellite RNA-encoded protein Evaluation of a system to screen for stimulators of non-specific DNA nicking by HIV-1 integrase: application to a library of 50,000 compounds.The N-end rule pathway and regulation by proteolysis Identification of RFPL3 protein as a novel E3 ubiquitin ligase modulating the integration activity of human immunodeficiency virus, type 1 preintegration complex using a microtiter plate-based assay Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect.Quantitative analysis of human immunodeficiency virus type 1-infected CD4+ cell proteome: dysregulated cell cycle progression and nuclear transport coincide with robust virus production von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step.Characterization of HIV-1 integrase N-terminal mutant viruses.Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway.The N-end rule and retroviral infection: no effect on integrase.Integrase, LEDGF/p75 and HIV replication.Posttranslational modifications of HIV-1 integrase by various cellular proteins during viral replication.Multivalency-assisted control of intracellular signaling pathways: application for ubiquitin- dependent N-end rule pathway.HIV-1, ubiquitin and ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications.The ends and means of artificially induced targeted protein degradation.Q2N and S65D substitutions of ubiquitin unravel functional significance of the invariant residues Gln2 and Ser65.Sequential deletion of the integrase (Gag-Pol) carboxyl terminus reveals distinct phenotypic classes of defective HIV-1.Molecular characterization of preintegration latency in human immunodeficiency virus type 1 infection.GCN5-dependent acetylation of HIV-1 integrase enhances viral integration.Prospective strategies for targeting HIV-1 integrase function.Allosteric HIV-1 Integrase Inhibitors Lead to Premature Degradation of the Viral RNA Genome and Integrase in Target Cells.Tumor-suppression function of transcription factor USF2 in prostate carcinogenesis.Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity.

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Degradation of HIV-1 integrase by the N-end rule pathway

http://www.wikidata.org/entity/Q28140723

description

2000 nî lūn-bûn

@nan

2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

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2000年论文

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name

Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Degradation of HIV-1 integrase by the N-end rule pathway

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Journal of Biological Chemistry

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Degradation of HIV-1 integrase by the N-end rule pathway

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P2093

L C Mulder

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

M A Muesing

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P2860

Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5

Constitutional mutations of the hSNF5/INI1 gene predispose to a variety of cancers

The N-end rule: functions, mysteries, uses

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

Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization

The mouse and human genes encoding the recognition component of the N-end rule pathway

c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function

In vivo half-life of a protein is a function of its amino-terminal residue

Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells

A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells

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29749-53

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scholarly article

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4827939

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10.1074/JBC.M004670200

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38

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275

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2000-09-22T00:00:00Z

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10893419

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