HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation.
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The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnoverVpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 proteinUracil DNA N-glycosylase promotes assembly of human centromere protein AArchitecturally diverse proteins converge on an analogous mechanism to inactivate Uracil-DNA glycosylaseThe DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destructionDistinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4BCullin4A and cullin4B are interchangeable for HIV Vpr and Vpx action through the CRL4 ubiquitin ligase complexInteractions with DCAF1 and DDB1 in the CRL4 E3 ubiquitin ligase are required for Vpr-mediated G2 arrest.miRNA-1236 inhibits HIV-1 infection of monocytes by repressing translation of cellular factor VprBP.Vpr-host interactions during HIV-1 viral life cycle.Exposed hydrophobic residues in human immunodeficiency virus type 1 Vpr helix-1 are important for cell cycle arrest and cell deathHIV-1 Vpr redirects host ubiquitination pathway.HIV-1 Vpr triggers mitochondrial destruction by impairing Mfn2-mediated ER-mitochondria interaction.HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1.Alkylation sensitivity screens reveal a conserved cross-species functionome.The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1.VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligasesHIV-1 Vpr induces the degradation of ZIP and sZIP, adaptors of the NuRD chromatin remodeling complex, by hijacking DCAF1/VprBP.Defining the interactions and role of DCAF1/VPRBP in the DDB1-cullin4A E3 ubiquitin ligase complex engaged by HIV-1 Vpr to induce a G2 cell cycle arrest.The role of unintegrated DNA in HIV infectionTransmission electron microscopy for the evaluation and optimization of crystal growthCRL4-DDB1-VPRBP ubiquitin ligase mediates the stress triggered proteolysis of Mcm10.Uracil DNA glycosylase initiates degradation of HIV-1 cDNA containing misincorporated dUTP and prevents viral integration.RNA Viruses: RNA Roles in Pathogenesis, Coreplication and Viral LoadHIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradationHIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteinsDiverse fates of uracilated HIV-1 DNA during infection of myeloid lineage cells.HIV relies on neddylation for ubiquitin ligase-mediated functionsHepatitis B Virus Protein X Induces Degradation of Talin-1.Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.Viral takeover of the host ubiquitin system.Delineating HIV-associated neurocognitive disorders using transgenic models: the neuropathogenic actions of Vpr.HIV-1, ubiquitin and ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications.Merlin, a multi-suppressor from cell membrane to the nucleus.Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase.Molecular insights into NF2/Merlin tumor suppressor function.HIV-1 Vpr Protein Induces Proteasomal Degradation of Chromatin-associated Class I HDACs to Overcome Latent Infection of Macrophages.Virion-Associated Vpr Alleviates a Postintegration Block to HIV-1 Infection of Dendritic Cells.Geminivirus C2 protein might be the key player for geminiviral co- option of SCF-mediated ubiquitination
P2860
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P2860
HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@ast
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@en
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@nl
type
label
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@ast
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@en
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@nl
prefLabel
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@ast
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@en
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@nl
P2093
P2860
P356
P1476
HIV-1 Vpr loads uracil DNA gly ...... teasome-dependent degradation.
@en
P2093
Jennifer Guerrero-Santoro
Jinwoo Ahn
Vesna Rapic-Otrin
Zach Novince
P2860
P304
37333-37341
P356
10.1074/JBC.M110.133181
P407
P577
2010-09-24T00:00:00Z