HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation - Test2 - elhamkhani - TriplyDB

HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation

HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation

http://www.wikidata.org/entity/Q36967370

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New insights into an X-traordinary viral protein Mechanism of allosteric activation of SAMHD1 by dGTP Structural basis of lentiviral subversion of a cellular protein degradation pathway Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.Cyclin L2 is a critical HIV dependency factor in macrophages that controls SAMHD1 abundance.VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases Determinants for degradation of SAMHD1, Mus81 and induction of G2 arrest in HIV-1 Vpr and SIVagm Vpr.Structural Basis of Clade-specific Engagement of SAMHD1 (Sterile α Motif and Histidine/Aspartate-containing Protein 1) Restriction Factors by Lentiviral Viral Protein X (Vpx) Virulence Factors.Cellular and Biochemical Mechanisms of the Retroviral Restriction Factor SAMHD1.Vpx rescue of HIV-1 from the antiviral state in mature dendritic cells is independent of the intracellular deoxynucleotide concentration.Inhibition of Vpx-Mediated SAMHD1 and Vpr-Mediated Host Helicase Transcription Factor Degradation by Selective Disruption of Viral CRL4 (DCAF1) E3 Ubiquitin Ligase Assembly SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr).Degradation of SAMHD1 by Vpx Is Independent of Uncoating.The Deoxynucleoside Triphosphate Triphosphohydrolase Activity of SAMHD1 Protein Contributes to the Mitochondrial DNA Depletion Associated with Genetic Deficiency of Deoxyguanosine Kinase.Substrate Specificity of SAMHD1 Triphosphohydrolase Activity Is Controlled by Deoxyribonucleoside Triphosphates and Phosphorylation at Thr592.HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase.SAMHD1: Recurring roles in cell cycle, viral restriction, cancer, and innate immunity.The aryl hydrocarbon receptor and interferon gamma generate antiviral states via transcriptional repression The role of SAMHD1 expression and its relation to HIV-2 (Vpx) gene production

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P2860

HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation

http://www.wikidata.org/entity/Q36967370

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

HIV-2 and SIVmac accessory vir ...... oteasome-dependent degradation

@en

type

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HIV-2 and SIVmac accessory vir ...... oteasome-dependent degradation

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HIV-2 and SIVmac accessory vir ...... oteasome-dependent degradation

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JBC.M113.469007

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Journal of Biological Chemistry

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HIV-2 and SIVmac accessory vir ...... oteasome-dependent degradation

@en

P2093

Jennifer Mehrens

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

Jinwoo Ahn

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

Maria DeLucia

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

Ying Wu

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

P2860

SAMHD1-deficient CD14+ cells from individuals with Aicardi-Goutières syndrome are highly susceptible to HIV-1 infection

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

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

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

SAMHD1 restricts HIV-1 reverse transcription in quiescent CD4(+) T-cells

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

Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection

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

Characterization of the Deoxynucleotide Triphosphate Triphosphohydrolase (dNTPase) Activity of the EF1143 Protein from Enterococcus faecalis and Crystal Structure of the Activator-Substrate Complex

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19116-19126

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scholarly article

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10.1074/JBC.M113.469007

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26

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288

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2013-05-15T00:00:00Z

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23677995

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3696684

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