Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays.
about
Global changes in the RNA binding specificity of HIV-1 gag regulate virion genesisCooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packagingEfficient encapsidation of human immunodeficiency virus type 1 vectors and further characterization of cis elements required for encapsidationSecondary structure model of the Mason-Pfizer monkey virus 5' leader sequence: identification of a structural motif common to a variety of retrovirusesThe human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structuresIs HIV-1 RNA dimerization a prerequisite for packaging? Yes, no, probably?A Structural Biology Approach Enables the Development of Antimicrobials Targeting Bacterial ImmunophilinsCrystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assemblyOn the Selective Packaging of Genomic RNA by HIV-1The Life-Cycle of the HIV-1 Gag-RNA ComplexFunctional characterization of the human immunodeficiency virus type 1 genome by genetic footprintingIn vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain.Analysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain.Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides.Nonreciprocal packaging of human immunodeficiency virus type 1 and type 2 RNA: a possible role for the p2 domain of Gag in RNA encapsidation.Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly.A heterologous, high-affinity RNA ligand for human immunodeficiency virus Gag protein has RNA packaging activityAssembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA.The gag domains required for avian retroviral RNA encapsidation determined by using two independent assays.Mutations within four distinct gag proteins are required to restore replication of human immunodeficiency virus type 1 after deletion mutagenesis within the dimerization initiation site.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.Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.Human immunodeficiency virus types 1 and 2 differ in the predominant mechanism used for selection of genomic RNA for encapsidationCharacterization of Rous sarcoma virus Gag particles assembled in vitro.The yeast Ty3 retrotransposon contains a 5'-3' bipartite primer-binding site and encodes nucleocapsid protein NCp9 functionally homologous to HIV-1 NCp7Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: influence of the binding of nucleic acids.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.Definition of a high-affinity Gag recognition structure mediating packaging of a retroviral RNA genome.cis-Acting elements important for retroviral RNA packaging specificity.The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequenceSequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection.The role of A-kinase anchoring protein 95-like protein in annealing of tRNALys3 to HIV-1 RNA.A high affinity binding site for the HIV-1 nucleocapsid protein.Mapping the RNA binding sites for human immunodeficiency virus type-1 gag and NC proteins within the complete HIV-1 and -2 untranslated leader regions.Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding.The conformation of the mature dimeric human immunodeficiency virus type 1 RNA genome requires packaging of pol protein.RNA sequences in the Moloney murine leukemia virus genome bound by the Gag precursor protein in the yeast three-hybrid system.HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation.
P2860
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P2860
Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays.
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
Specific binding of human immu ...... by RNA mobility shift assays.
@ast
Specific binding of human immu ...... by RNA mobility shift assays.
@en
type
label
Specific binding of human immu ...... by RNA mobility shift assays.
@ast
Specific binding of human immu ...... by RNA mobility shift assays.
@en
prefLabel
Specific binding of human immu ...... by RNA mobility shift assays.
@ast
Specific binding of human immu ...... by RNA mobility shift assays.
@en
P2093
P2860
P1433
P1476
Specific binding of human immu ...... by RNA mobility shift assays.
@en
P2093
P2860
P304
P407
P577
1993-12-01T00:00:00Z