about
Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugatesThe human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 buddingMechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15Human ESCRT-II complex and its role in human immunodeficiency virus type 1 releaseOverexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain functionAnalysis of human immunodeficiency virus type 1 Gag ubiquitinationLate assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis.Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4.Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infectionRetroviruses have differing requirements for proteasome function in the budding processRole of ESCRT-I in retroviral buddingProteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cellsThe trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 productionTsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)A role for ubiquitin ligase recruitment in retrovirus releaseProteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2No strings attached: the ESCRT machinery in viral budding and cytokinesisUbiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear importEquine infectious anemia virus utilizes host vesicular protein sorting machinery during particle releaseEndophilins interact with Moloney murine leukemia virus Gag and modulate virion productionVirus budding and the ESCRT pathwayALIX is recruited temporarily into HIV-1 budding sites at the end of gag assemblyPersistent and transient replication of full-length hepatitis C virus genomes in cell cultureHost Gene Expression Profiling of Dengue Virus Infection in Cell Lines and PatientsStructure and functional interactions of the Tsg101 UEV domain.Cumulative mutations of ubiquitin acceptor sites in human immunodeficiency virus type 1 gag cause a late budding defect.The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway.The ubiquitin-proteasome pathway and proteasome inhibitorsProduction of Infectious Dengue Virus in Aedes aegypti Is Dependent on the Ubiquitin Proteasome PathwayProteasome Inhibition Suppresses Dengue Virus Egress in Antibody Dependent InfectionIdentification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligaseMammalian Orc1 protein is selectively released from chromatin and ubiquitinated during the S-to-M transition in the cell division cycle.Tsg101, an inactive homologue of ubiquitin ligase e2, interacts specifically with human immunodeficiency virus type 2 gag polyprotein and results in increased levels of ubiquitinated gag.Rhabdoviruses and the cellular ubiquitin-proteasome system: a budding interaction.Ubiquitination is required for effective replication of coxsackievirus B3.Functional interchangeability of late domains, late domain cofactors and ubiquitin in viral budding.Role of ubiquitin and proteasomes in phagosome maturationUbiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus matrix protein is important for viral budding.Inhibition of lysosome and proteasome function enhances human immunodeficiency virus type 1 infection.The interferon-induced gene ISG15 blocks retrovirus release from cells late in the budding process.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
Ubiquitin is part of the retrovirus budding machinery
@en
Ubiquitin is part of the retrovirus budding machinery.
@nl
type
label
Ubiquitin is part of the retrovirus budding machinery
@en
Ubiquitin is part of the retrovirus budding machinery.
@nl
prefLabel
Ubiquitin is part of the retrovirus budding machinery
@en
Ubiquitin is part of the retrovirus budding machinery.
@nl
P2093
P2860
P356
P1476
Ubiquitin is part of the retrovirus budding machinery
@en
P2093
P2860
P304
13069-13074
P356
10.1073/PNAS.97.24.13069
P407
P577
2000-11-01T00:00:00Z