Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
about
Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3.The viruses in all of us: characteristics and biological significance of human endogenous retrovirus sequencesRole of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infectionSingle amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle productionFlexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid ProteinTy3 capsid mutations reveal early and late functions of the amino-terminal domainCross- and Co-Packaging of Retroviral RNAs and Their ConsequencesA multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free systemCharacterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation.Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packagingFunctional characterization of the human immunodeficiency virus type 1 genome by genetic footprintingRole of protein interactions in defining HIV-1 viral capsid shape and stability: a coarse-grained analysis.Multiple functions for the basic amino acids of the human T-cell leukemia virus type 1 matrix protein in viral transmissionVirus particle core defects caused by mutations in the human immunodeficiency virus capsid N-terminal domainCells with high cyclophilin A content support replication of human immunodeficiency virus type 1 Gag mutants with decreased ability to incorporate cyclophilin AAnalysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain.A putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assemblyRole of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle.Cryoelectron microscopic examination of human immunodeficiency virus type 1 virions with mutations in the cyclophilin A binding loop.Particle size determinants in the human immunodeficiency virus type 1 Gag proteinDetection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17.Analysis 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.Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.Assembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domainEfficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain.Isolation of human immunodeficiency virus type 1 cores: retention of Vpr in the absence of p6(gag).Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein.Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells.Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41.HIV-1 infection of non-dividing cells: evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import.Tripeptide interference with human immunodeficiency virus type 1 morphogenesis.p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing proteaseEffects of Gag mutation and processing on retroviral dimeric RNA maturation.Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation.Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1.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.Analysis of the N-terminal region of the murine leukemia virus nucleocapsid proteinHypervariable region 1 differentially impacts viability of hepatitis C virus strains of genotypes 1 to 6 and impairs virus neutralizationDefects in virion production caused by mutations affecting the C-terminal portion of the Moloney murine leukemia virus capsid protein.
P2860
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P2860
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@ast
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@en
type
label
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@ast
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@en
prefLabel
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@ast
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@en
P2860
P1433
P1476
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants.
@en
P2093
P2860
P304
P407
P577
1993-07-01T00:00:00Z