Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase.
about
Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factorsDifferential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F.Human cytidine deaminase APOBEC3H restricts HIV-1 replicationIdentification of APOBEC3DE as another antiretroviral factor from the human APOBEC familyIdentification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3GThe role of cullin 5-containing ubiquitin ligasesThe role of ubiquitylation in immune defence and pathogen evasionCharacterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsMultiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development.Polymorphisms of CUL5 are associated with CD4+ T cell loss in HIV-1 infected individuals.Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication.Identifying determinants of cullin binding specificity among the three functionally different Drosophila melanogaster Roc proteins via domain swapping.Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteinsAPOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms.Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression.Innate immune signaling induces high levels of TC-specific deaminase activity in primary monocyte-derived cells through expression of APOBEC3A isoformsIdentification of two APOBEC3F splice variants displaying HIV-1 antiviral activity and contrasting sensitivity to VifN-terminal hemagglutinin tag renders lysine-deficient APOBEC3G resistant to HIV-1 Vif-induced degradation by reduced polyubiquitination.Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC.APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif.Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligaseOn the solution conformation and dynamics of the HIV-1 viral infectivity factorIdentification of a novel HIV-1 inhibitor targeting Vif-dependent degradation of human APOBEC3G protein.Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycleCytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation.The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells.Role of APOBEC3F Gene Variation in HIV-1 Disease Progression and Pneumocystis Pneumonia.The Role of Elongin BC-Containing Ubiquitin Ligases.Induction of antiviral cytidine deaminases does not explain the inhibition of hepatitis B virus replication by interferons.APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load.APOBEC3 cytidine deaminases: distinct antiviral actions along the retroviral life cycle.Running loose or getting lost: how HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif proteinFoamy virus infection in primates.Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination.APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.
P2860
Q24317568-CC9829FA-04EA-46A9-A9F0-3A0756694B2DQ24537623-F83E5D32-321A-4A94-AC7B-1E92C96BBC73Q24544264-A942F3DE-CEB7-47F0-A501-ECD2DE8085FAQ24653682-AEBA994F-BE1D-43F7-A5DF-20F78693EE1FQ24670173-090E14C7-B0A3-4F36-B26D-B72E95CCD604Q24672209-4B9B7CC0-4476-4D44-88B3-C6309F065F72Q24681427-367E1D89-C419-4F37-B0DD-6EFCF001200AQ26749274-D9BA3DAF-B541-48D6-99DA-40B670F551CBQ26860775-2913A434-A80D-465B-AC61-431DFFE41219Q28482052-D4EBBC97-616E-40E2-8FFF-8FE33206484FQ30381745-BA5B6D32-18FC-4C62-A0B9-722053AC01FEQ33270513-70B6471F-442D-4B53-B65D-EC85E3FB1B8EQ33289183-0781F104-629E-4BC0-912B-4EA2504E8F47Q33349452-68F44FAB-C219-465E-A523-A4D2778155BCQ33359573-815601A3-4379-4721-836F-1F2AE5CE6B52Q33393637-D00BDDFB-B581-45B7-B074-1B559E53E5B8Q33826968-54119029-D722-4AA7-93DF-5FE305FE0565Q34012844-73B63301-0F02-4B04-BF7A-60C46A63FEA8Q34107265-B312CD8C-1335-4CD7-A7AC-853D3E1EF351Q34121572-B205E4C7-6657-48A5-B385-3780DBAC7A78Q34166447-4967173A-2AA3-43F7-9146-6A411CC2C755Q34179686-AA21660C-11C5-41FA-856E-8AD26DFC9461Q34353493-9BB7D323-E5FC-45FD-ACA7-012660025363Q34416419-06E340B6-C228-4653-86A8-F7B99EA66305Q34416665-7178BBE9-2912-405F-8216-932489F465F3Q34695564-7672754C-DBCF-4A78-9D3E-E9F2352C0004Q35113711-41295D0E-2E0C-4106-A53C-4152D70F5C17Q35451347-A53F0534-DCFF-451F-9C7B-B9955A40992BQ35819383-C6A155F3-8453-423E-9A33-E76FAC59B1DBQ35914312-0B1E4606-3A77-481C-BAA2-46C2710B617EQ35916117-FF265C42-3526-4A74-AEFD-376ECE56EED3Q35945852-2FE9EF83-A9E3-4E3D-85AF-4584D9D618E6Q35971082-74B24978-5F23-4C69-8EBF-52432AA181A6Q36099079-185DE6C1-D72A-485C-846A-71F03C44E605Q36316091-353F8C85-5C56-400E-9DCA-FFF67433146BQ36366147-06A8B42F-4143-4B39-8855-49FE2AFCB9BDQ36432758-8A363398-B505-4B6D-A2F8-ED48D727C748Q36548744-98225B4F-E4D2-445F-93C2-92A555E5BF3CQ36559921-A63573C2-3D25-4327-8374-3CAC5364C878Q36827236-773688B4-D6D8-4C0E-AE74-0EFA9B51121A
P2860
Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@ast
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@en
type
label
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@ast
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@en
prefLabel
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@ast
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@en
P2093
P2860
P1433
P1476
Regulation of Apobec3F and hum ...... 5-ElonB/C E3 ubiquitin ligase.
@en
P2093
Bindong Liu
Phuong Thi Nguyen Sarkis
Xiao-Fang Yu
P2860
P304
P356
10.1128/JVI.79.15.9579-9587.2005
P577
2005-08-01T00:00:00Z