Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
about
Regulated degradation of the HIV-1 Vpu protein through a betaTrCP-independent pathway limits the release of viral particlesA promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machineryHost cell manipulation by the human pathogen Toxoplasma gondiiStructural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assemblyHIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1Building and remodelling Cullin-RING E3 ubiquitin ligasesVP8, the Major Tegument Protein of Bovine Herpesvirus 1, Interacts with Cellular STAT1 and Inhibits Interferon Beta SignalingLentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infectionExploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systemsReduced cul-5 activity causes aberrant follicular morphogenesis and germ cell loss in Drosophila oogenesis.Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complexSystematic identification of interactions between host cell proteins and E7 oncoproteins from diverse human papillomaviruses.Serine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu.HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1.Hepatitis B virus HBx protein interactions with the ubiquitin proteasome system.Chromatin dynamics of gene activation and repression in response to interferon alpha (IFN(alpha)) reveal new roles for phosphorylated and unphosphorylated forms of the transcription factor STAT2Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions.Molecular determinants for recognition of divergent SAMHD1 proteins by the lentiviral accessory protein Vpx.Modulation of gene expression in a human cell line caused by poliovirus, vaccinia virus and interferon.Cullin4 Is Pro-Viral during West Nile Virus Infection of Culex Mosquitoes.Changing the ubiquitin landscape during viral manipulation of the DNA damage response.Human papillomavirus type 16 E7 oncoprotein associates with the cullin 2 ubiquitin ligase complex, which contributes to degradation of the retinoblastoma tumor suppressorA functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infectionBroad and potent antiviral activity of the NAE inhibitor MLN4924.HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradationThe draft genome and transcriptome of Panagrellus redivivus are shaped by the harsh demands of a free-living lifestyleEctromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases.Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication proteinPoxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexesViral proteomics.A proteomic approach to identify candidate substrates of human adenovirus E4orf6-E1B55K and other viral cullin-based E3 ubiquitin ligases.Human immunodeficiency virus, restriction factors, and interferon.CUL4A ubiquitin ligase: a promising drug target for cancer and other human diseasesInteractions of bacterial proteins with host eukaryotic ubiquitin pathways.Poxvirus exploitation of the ubiquitin-proteasome system.Subversion of innate immune responses by bacterial hindrance of NF-κB pathway.The ubiquitin proteasome system - implications for cell cycle control and the targeted treatment of cancer.Human T-lymphotropic virus proteins and post-translational modification pathwaysThe ubiquitin-conjugating system: multiple roles in viral replication and infection.
P2860
Q21559507-1DD06D0F-D719-46D7-A69A-051AD1B94605Q24646885-3F0A805E-4E91-4BED-AA47-EF8B2A1E7D0FQ24650648-63037984-26F5-4B95-8A4F-DE95CAA1FA64Q24658171-7F98D231-E419-4D07-8BC6-33A5A0CAB3BCQ24681112-164F19B2-B987-4ACE-A92E-35D6A38458AFQ27027816-B0B5BDD6-E8B7-4EEA-8B95-26C67F2CCEEEQ28115701-15FC172A-A256-4C20-A4CC-89EB635BB4AFQ28472652-B2470D8D-46A7-4D27-871E-1F61AA8D0164Q33270514-B168BC8D-46DF-4BF4-A689-4D5F9E60C4F0Q33530110-AEA516A1-9CCC-4F7A-94CB-5D699A71FB8EQ33807551-5541FDF4-4CEA-46F6-BEDA-04A69F54D075Q34034114-798C53DD-B152-4772-9CC1-AB89570E2D68Q34122679-48FBE46D-DA31-45AC-B059-9D884F3D624DQ34146128-C4FA8FBF-2794-4086-B321-D2262F3F98DFQ34256688-EE9B3F11-AD30-4177-9E42-D420699880E2Q34580906-124A3D5D-20BA-4F2E-BE7A-7537F716027BQ35063436-96E4D074-BE8A-4216-B9DF-F4EAA5D3392AQ35214620-0A846147-DF6C-4E7F-A6F3-379B6B2445CFQ35450431-A8DC42AF-EFCF-4ED0-9466-316450E9F3EFQ35677536-EEC1BFCF-AD41-4E0F-B21B-D8AF765C11B3Q35760782-CB0D5FE9-128C-4252-AD1A-CE75AD18F1C3Q35854193-E42377E2-4772-4AAE-839F-091E9554C463Q36098917-C022DF23-099D-4D74-9A84-9AF72A27379AQ36099153-CC1DA54D-8949-478F-936A-CD82F6861767Q36524801-10F066DF-DCD1-41C4-826C-336B932E5778Q36559594-598A25DD-84E7-4FA5-8A78-501D1C87CEE1Q36709968-AA233F3E-E562-46DF-9CEC-44D6A8D180B1Q36740202-52614BC4-4C27-40BE-9AE4-AFC06660EEB0Q36747704-16BCA9B0-DE25-4E5A-9597-58B12AE82548Q36825432-1A94FDF2-D4B7-4D10-B5F3-CD00AC401ACEQ36842301-B0055264-303B-4ACD-9328-2F0B3C3521C1Q37451972-A0953D8C-EB3D-4415-806E-0D567E34DA14Q37582948-5AD2BF80-AFEB-4F4A-A04F-167423E83B64Q37609233-9CDD4978-C666-4458-BC8B-B4322901061BQ37902900-92895B1E-A82D-4291-9CA5-C7E2EC84E7C5Q37945194-64AC7E33-50A3-44E4-8082-AD587C6002D6Q37951705-D433992F-05F9-4836-8B04-22EC8C677DF1Q38087182-ADF9893D-315A-49F0-9BD8-984989B6E3A6Q38156859-1B6F6FE3-C758-4D38-A552-3922CD928E2FQ38210024-F04E65E4-8B9C-4E55-AA39-F78C0DC225BC
P2860
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@ast
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@en
type
label
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@ast
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@en
prefLabel
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@ast
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@en
P2860
P356
P1476
Viral modulators of cullin RING ubiquitin ligases: culling the host defense.
@en
P2093
Klaus Früh
Michele Barry
P2860
P356
10.1126/STKE.3352006PE21
P577
2006-05-16T00:00:00Z