Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection. - Test2 - elhamkhani - TriplyDB

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

http://www.wikidata.org/entity/Q34242229

about

Natural polymorphisms in human APOBEC3H and HIV-1 Vif combine in primary T lymphocytes to affect viral G-to-A mutation levels and infectivity HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies Global landscape of HIV-human protein complexes The restriction factors of human immunodeficiency virus HIV Genome-Wide Protein Associations: a Review of 30 Years of Research The role of cullin 5-containing ubiquitin ligases Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all From systems to structure: bridging networks and mechanism The APOBEC3 family of retroelement restriction factors The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways Structural Insights into HIV-1 Vif-APOBEC3F Interaction Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction APOBEC3 Interference during Replication of Viral Genomes Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G Activation of HIV-1 from latent infection via synergy of RUNX1 inhibitor Ro5-3335 and SAHA Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Cyclin F/FBXO1 Interacts with HIV-1 Viral Infectivity Factor (Vif) and Restricts Progeny Virion Infectivity by Ubiquitination and Proteasomal Degradation of Vif Protein through SCFcyclin F E3 Ligase Machinery Identification of HIV-1 Vif regions required for CBF-β interaction and APOBEC3 suppression A conflict of interest: the evolutionary arms race between mammalian APOBEC3 and lentiviral Vif.Small molecules that inhibit Vif-induced degradation of APOBEC3G.GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex Core binding factor beta plays a critical role by facilitating the assembly of the Vif-cullin 5 E3 ubiquitin ligase.Evolutionarily conserved requirement for core binding factor beta in the assembly of the human immunodeficiency virus/simian immunodeficiency virus Vif-cullin 5-RING E3 ubiquitin ligase.Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.The virus-induced protein APOBEC3G inhibits anoikis by activation of Akt kinase in pancreatic cancer cells.HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinants Role of cullin-elonginB-elonginC E3 complex in bovine immunodeficiency virus and maedi-visna virus Vif-mediated degradation of host A3Z2-Z3 proteins Core-binding factor subunit beta is not required for non-primate lentiviral Vif-mediated APOBEC3 degradation.Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein. Importance of the C-terminal unstructured tail.Autophagy plays an important role in the containment of HIV-1 in nonprogressor-infected patients.Identification of benzodiazepine Ro5-3335 as an inhibitor of CBF leukemia through quantitative high throughput screen against RUNX1-CBFβ interaction Insights into the dual activity of SIVmac239 Vif against human and African green monkey APOBEC3G.Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C.Cellular requirements for bovine immunodeficiency virus Vif-mediated inactivation of bovine APOBEC3 proteins.Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligase Mass spectrometry-based proteomic approaches for discovery of HIV-host interactions.

P2860

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P2860

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

http://www.wikidata.org/entity/Q34242229

description

2011 nî lūn-bûn

@nan

2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@ast

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@en

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@nl

type

label

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@ast

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@en

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@nl

prefLabel

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@ast

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@en

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@nl

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Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.

@en

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Alma Burlingame

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

Brett D Anderson

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

Cathal Mahon

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

Charles S Craik

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

David Stanley

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

Dong Young Kim

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

Eunju Kwon

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

John D Gross

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

Joshua Kane

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

Judd F Hultquist

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

P2860

APOBEC3 proteins mediate the clearance of foreign DNA from human cells

Global landscape of HIV-human protein complexes

Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate

E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification

Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

Recognition of the polyubiquitin proteolytic signal

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability

P2888

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371-375

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scholarly article

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10.1038/NATURE10693

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7381

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481

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Reuben S Harris

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2011-12-21T00:00:00Z

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51905157

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1035335911

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22190037

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3310910

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