The minute virus of mice capsid specifically recognizes the 3' hairpin structure of the viral replicative-form DNA: mapping of the binding site by hydroxyl radical footprinting.
about
Symmetric-strand packaging of recombinant parvovirus LuIII genomes that retain only the terminal regions.Maintenance of the flip sequence orientation of the ears in the parvoviral left-end hairpin is a nonessential consequence of the critical asymmetry in the hairpin stemProtein species of the parvovirus minute virus of mice strain MVMp: involvement of phosphorylated VP-2 subtypes in viral morphogenesis.The major capsid protein VP2 of minute virus of mice (MVM) can form particles which bind to the 3'-terminal hairpin of MVM replicative-form DNA and package single-stranded viral progeny DNA.Parvoviral left-end hairpin ears are essential during infection for establishing a functional intranuclear transcription template and for efficient progeny genome encapsidation.Evidence of pervasive biologically functional secondary structures within the genomes of eukaryotic single-stranded DNA viruses.Adeno-associated virus type 2 protein interactions: formation of pre-encapsidation complexesThe minor capsid protein VP1 of the autonomous parvovirus minute virus of mice is dispensable for encapsidation of progeny single-stranded DNA but is required for infectivity.
P2860
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P2860
The minute virus of mice capsid specifically recognizes the 3' hairpin structure of the viral replicative-form DNA: mapping of the binding site by hydroxyl radical footprinting.
description
1991 nî lūn-bûn
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1991年の論文
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1991年論文
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1991年論文
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1991年論文
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1991年論文
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1991年論文
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1991年论文
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1991年论文
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1991年论文
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name
The minute virus of mice capsi ...... hydroxyl radical footprinting.
@en
type
label
The minute virus of mice capsi ...... hydroxyl radical footprinting.
@en
prefLabel
The minute virus of mice capsi ...... hydroxyl radical footprinting.
@en
P2860
P1433
P1476
The minute virus of mice capsi ...... hydroxyl radical footprinting
@en
P2093
P2860
P304
P407
P577
1991-09-01T00:00:00Z