Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
about
The interferon response inhibits HIV particle production by induction of TRIM22Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cellsD-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transductionProteins 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 cellsMutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiaeVpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retrovirusesEffect of mutations affecting the p6 gag protein on human immunodeficiency virus particle releaseAn early stage of Mason-Pfizer monkey virus budding is regulated by the hydrophobicity of the Gag matrix domain coreInhibition of HIV-1 particle assembly by 2',3'-cyclic-nucleotide 3'-phosphodiesteraseHIV type 1 Gag as a target for antiviral therapyTsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signalAn assembly domain of the Rous sarcoma virus Gag protein required late in buddingIdentification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipidsEstablishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeletonRole of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infectionDifferential membrane binding of the human immunodeficiency virus type 1 matrix proteinInhibitors of human immunodeficiency virus type 1 zinc fingers prevent normal processing of gag precursors and result in the release of noninfectious virus particlesHuman immunodeficiency virus type 1 Nef associates with a member of the p21-activated kinase familyNew insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cellsNucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cellsReal-time visualization of HIV-1 GAG trafficking in infected macrophagesSingle-Cell and Single-Cycle Analysis of HIV-1 ReplicationTargeting of Moloney murine leukemia virus gag precursor to the site of virus buddingSingle amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle productionLipids and membrane microdomains in HIV-1 replicationStructure of equine infectious anemia virus matrix protein.Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl SwitchEntropic switch regulates myristate exposure in the HIV-1 matrix proteinA unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsidSolution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix ProteinCrystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assemblyPhosphorylation-dependent human immunodeficiency virus type 1 infection and nuclear targeting of viral DNAIncorporation of 12-methoxydodecanoate into the human immunodeficiency virus 1 gag polyprotein precursor inhibits its proteolytic processing and virus production in a chronically infected human lymphoid cell lineEfficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domainPhosphorylation at serines 216 and 221 is important for Drosophila HeT-A Gag protein stabilityHuman cytomegalovirus UL99-encoded pp28 is required for the cytoplasmic envelopment of tegument-associated capsids.Considering protonation as a posttranslational modification regulating protein structure and function.A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
P2860
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P2860
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@ast
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@en
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@nl
type
label
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@ast
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@en
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@nl
prefLabel
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@ast
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@en
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@nl
P2860
P3181
P356
P1476
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
@en
P2093
P2860
P3181
P356
10.1073/PNAS.87.2.523
P407
P577
1990-01-01T00:00:00Z