trans-acting viral protease is necessary and sufficient for activation of avian leukosis virus reverse transcriptase.
about
Retrotransposition of nonviral RNAs in an avian packaging cell lineProteolytic processing and assembly of gag and gag-pol proteins of TED, a baculovirus-associated retrotransposon of the gypsy family.The gag domains required for avian retroviral RNA encapsidation determined by using two independent assays.Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles.v-Src enhances phosphorylation at Ser-282 of the Rous sarcoma virus integraseSelf-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1.Altered gag polyprotein cleavage specificity of feline immunodeficiency virus/human immunodeficiency virus mutant proteases as demonstrated in a cell-based expression system.Transport and processing of the Rous sarcoma virus Gag protein in the endoplasmic reticulum.Avian retroviral RNA encapsidation: reexamination of functional 5' RNA sequences and the role of nucleocapsid Cys-His motifs.Analysis of deletions and thermosensitive mutations in Rous sarcoma virus gag protein p10.Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteinsThe nonmyristylated Pr160gag-pol polyprotein of human immunodeficiency virus type 1 interacts with Pr55gag and is incorporated into viruslike particles.Processing of avian retroviral gag polyprotein precursors is blocked by a mutation at the NC-PR cleavage site.Role of the avian retroviral protease in the activation of reverse transcriptase during virion assemblyPR domain of rous sarcoma virus Gag causes an assembly/budding defect in insect cells.Evidence for a second function of the MA sequence in the Rous sarcoma virus Gag proteinAnalysis of cleavage site mutations between the NC and PR Gag domains of Rous sarcoma virusIn vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles.Proteolytic processing of Ty3 proteins is required for transposition.Reverse transcriptase and protease activities of avian leukosis virus Gag-Pol fusion proteins expressed in insect cells.Complementation studies with Rous sarcoma virus gag and gag-pol polyprotein mutants.Transposition of a Ty3 GAG3-POL3 fusion mutant is limited by availability of capsid protein.
P2860
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P2860
trans-acting viral protease is necessary and sufficient for activation of avian leukosis virus reverse transcriptase.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
trans-acting viral protease is ...... s virus reverse transcriptase.
@en
type
label
trans-acting viral protease is ...... s virus reverse transcriptase.
@en
prefLabel
trans-acting viral protease is ...... s virus reverse transcriptase.
@en
P2860
P1433
P1476
trans-acting viral protease is ...... s virus reverse transcriptase.
@en
P2093
P2860
P304
P407
P577
1991-11-01T00:00:00Z