Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac. - Wikidata - wikimedia - TriplyDB

Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

http://www.wikidata.org/entity/Q36136752

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New insights into an X-traordinary viral protein SAMHD1-Dependent and -Independent Functions of HIV-2/SIV Vpx Protein Identification and characterization of naturally occurring splice variants of SAMHD1 Mechanism of allosteric activation of SAMHD1 by dGTP Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase SAMHD1 restricts HIV-1 reverse transcription in quiescent CD4(+) T-cells Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection Animal Models for HIV Cure Research The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP Functional organization of human SAMHD1 and mechanisms of HIV-1 restriction Cullin4A and cullin4B are interchangeable for HIV Vpr and Vpx action through the CRL4 ubiquitin ligase complex The ribonuclease activity of SAMHD1 is required for HIV-1 restriction HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus.Immunopathogenesis of simian immunodeficiency virus infection in nonhuman primates Identification of cellular proteins interacting with the retroviral restriction factor SAMHD1 Nuclear import of SAMHD1 is mediated by a classical karyopherin α/β1 dependent pathway and confers sensitivity to VpxMAC induced ubiquitination and proteasomal degradation.Effects of human SAMHD1 polymorphisms on HIV-1 susceptibility.dNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.The Vpx lentiviral accessory protein targets SAMHD1 for degradation in the nucleus.Macrophages and their relevance in Human Immunodeficiency Virus Type I infection.Contribution of SAM and HD domains to retroviral restriction mediated by human SAMHD1.The retroviral restriction ability of SAMHD1, but not its deoxynucleotide triphosphohydrolase activity, is regulated by phosphorylation Structural basis of cellular dNTP regulation by SAMHD1.Substrates and Inhibitors of SAMHD1.Cyclin L2 is a critical HIV dependency factor in macrophages that controls SAMHD1 abundance.Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation Molecular determinants for recognition of divergent SAMHD1 proteins by the lentiviral accessory protein Vpx.SAMHD1 specifically restricts retroviruses through its RNase activity.Complement-Opsonized HIV-1 Overcomes Restriction in Dendritic Cells.SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation.Phospho-dependent Regulation of SAMHD1 Oligomerisation Couples Catalysis and Restriction.Restriction of HIV-1 Requires the N-Terminal Region of MxB as a Capsid-Binding Motif but Not as a Nuclear Localization Signal The SAMHD1 dNTP Triphosphohydrolase Is Controlled by a Redox Switch.Impact of cellular autophagy on viruses: Insights from hepatitis B virus and human retroviruses.Functional analysis of the relationship between Vpx and the restriction factor SAMHD1.SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons Host restriction factors in retroviral infection: promises in virus-host interaction.The efficiency of Vpx-mediated SAMHD1 antagonism does not correlate with the potency of viral control in HIV-2-infected individuals.Interferon block to HIV-1 transduction in macrophages despite SAMHD1 degradation and high deoxynucleoside triphosphates supply HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

http://www.wikidata.org/entity/Q36136752

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac.

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Alberto Brandariz-Nuñez

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

Felipe Diaz-Griffero

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

Jose Carlos Valle-Casuso

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

Jurgen Brojatsch

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

Monsef Benkirane

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

Nadine Laguette

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

Tommy E White

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P2860

SAMHD1 is a nucleic-acid binding protein that is mislocalized due to aicardi-goutières syndrome-associated mutations

The human immunodeficiency virus type 2 Vpx protein usurps the CUL4A-DDB1 DCAF1 ubiquitin ligase to overcome a postentry block in macrophage infection

Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response

Evolutionary and functional analyses of the interaction between the myeloid restriction factor SAMHD1 and the lentiviral Vpx protein

How SAMHD1 changes our view of viral restriction

SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx

SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates

Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein

Vpx is critical for reverse transcription of the human immunodeficiency virus type 2 genome in macrophages

Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli.

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10.1186/1742-4690-9-49

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9

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2012-06-12T00:00:00Z

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225302265

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