Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation.
about
Substitution of the Rev-response element in an HIV-1-based gene delivery system with that of SIVmac239 allows efficient delivery of Rev M10 into T-lymphocytes.Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.Sam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.Ty3 capsid mutations reveal early and late functions of the amino-terminal domainThe y271 and i274 amino acids in reverse transcriptase of human immunodeficiency virus-1 are critical to protein stabilityPrimer tRNAs for reverse transcriptionViral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants.Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assayA lentivirus packaging system based on alternative RNA transport mechanisms to express helper and gene transfer vector RNAs and its use to study the requirement of accessory proteins for particle formation and gene delivery.RNA trafficking signals in human immunodeficiency virus type 1.A single amino acid substitution in HIV-1 reverse transcriptase significantly reduces virion release.Mutational analysis of the hydrophobic tail of the human immunodeficiency virus type 1 p6(Gag) protein produces a mutant that fails to package its envelope protein.Mutations of the human immunodeficiency virus type 1 p6Gag domain result in reduced retention of Pol proteins during virus assembly.Particle size determinants in the human immunodeficiency virus type 1 Gag proteinAnalysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus-like particle assembly and release.The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly.Separable mechanisms of attachment and cell uptake during retrovirus infection.Assembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domainIdentification of a key target sequence to block human immunodeficiency virus type 1 replication within the gag-pol transframe domain.Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins.Gag-Pol supplied in trans is efficiently packaged and supports viral function in human immunodeficiency virus type 1.Virus maturation by budding.Placement of leucine zipper motifs at the carboxyl terminus of HIV-1 protease significantly reduces virion production.Effects of Gag mutation and processing on retroviral dimeric RNA maturation.Coding sequences upstream of the human immunodeficiency virus type 1 reverse transcriptase domain in Gag-Pol are not essential for incorporation of the Pr160(gag-pol) into virus particles.Essential domains for ribonucleoprotein complex formation required for retrotransposition of telomere-specific non-long terminal repeat retrotransposon SART1Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1.Extreme genetic fragility of the HIV-1 capsid.Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.Incorporation of human immunodeficiency virus type 1 reverse transcriptase into virus-like particlesThe role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycleIncorporation of Pr160(gag-pol) into virus particles requires the presence of both the major homology region and adjacent C-terminal capsid sequences within the Gag-Pol polyprotein.Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidationNoninfectious virus-like particles produced by Moloney murine leukemia virus-based retrovirus packaging cells deficient in viral envelope become infectious in the presence of lipofection reagentsFunctional complementation of nucleocapsid and late domain PTAP mutants of human immunodeficiency virus type 1 during replication.Incorporation of pol into human immunodeficiency virus type 1 Gag virus-like particles occurs independently of the upstream Gag domain in Gag-polThe conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 gag protein is important for virion assembly and release.Formation of the tRNALys packaging complex in HIV-1.Targeting human immunodeficiency virus type 1 assembly, maturation and budding.
P2860
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P2860
Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation.
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Characterization of deletion m ...... g-Pol precursor incorporation.
@ast
Characterization of deletion m ...... g-Pol precursor incorporation.
@en
type
label
Characterization of deletion m ...... g-Pol precursor incorporation.
@ast
Characterization of deletion m ...... g-Pol precursor incorporation.
@en
prefLabel
Characterization of deletion m ...... g-Pol precursor incorporation.
@ast
Characterization of deletion m ...... g-Pol precursor incorporation.
@en
P2093
P2860
P1433
P1476
Characterization of deletion m ...... g-Pol precursor incorporation.
@en
P2093
M L Hammarskjöld
N Srinivasakumar
P2860
P304
P577
1995-10-01T00:00:00Z