Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
about
Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3The Influence of LINE-1 and SINE Retrotransposons on Mammalian GenomesGlobal identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP)5' to 3' mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition.Two-hybrid analysis of Ty3 capsid subdomain interactionsHIV-1 Gag co-opts a cellular complex containing DDX6, a helicase that facilitates capsid assemblyThe TY3 Gag3 spacer controls intracellular condensation and uncoatingFunction of a retrotransposon nucleocapsid proteinTy3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions.Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesisTy3 nucleocapsid controls localization of particle assemblySequence requirements for localization and packaging of Ty3 retroelement RNA.Exploring Ty1 retrotransposon RNA structure within virus-like particlesCritical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly.Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins.Structure prediction, molecular dynamics simulation and docking studies of D-specific dehalogenase from Rhizobium sp. RC1A Structured-based Model for the Decreased Activity of Ala222Val and Glu429Ala Methylenetetrahydrofolate Reductase (MTHFR) Mutants.Homologous Capsid Proteins Testify to the Common Ancestry of Retroviruses, Caulimoviruses, Pseudoviruses, and Metaviruses.TY3 GAG3 protein forms ordered particles in Escherichia coli.Identifying the assembly intermediate in which Gag first associates with unspliced HIV-1 RNA suggests a novel model for HIV-1 RNA packaging.
P2860
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P2860
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@ast
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@en
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain.
@nl
type
label
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@ast
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@en
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain.
@nl
prefLabel
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@ast
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@en
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Ty3 capsid mutations reveal early and late functions of the amino-terminal domain
@en
P2093
Anne Lamsa
G Wesley Hatfield
Jianlin Cheng
Kathryn Kosaka
Kunio Nagashima
Liza S Z Larsen
Nadejda Beliakova-Bethell
Rani Najdi
Suzanne Sandmeyer
P2860
P304
P3181
P356
10.1128/JVI.02207-06
P407
P50
P577
2007-07-01T00:00:00Z