A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA
about
Structural basis for cooperative RNA binding and export complex assembly by HIV RevImplications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response elementHIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexesThe new (dis)order in RNA regulationA structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1NMR structure of a 4 x 4 nucleotide RNA internal loop from an R2 retrotransposon: Identification of a three purine-purine sheared pair motif and comparison to MC-SYM predictionsThe Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE BindingHTLV-1 Rex Tunes the Cellular Environment Favorable for Viral ReplicationThe export receptor Crm1 forms a dimer to promote nuclear export of HIV RNARev-RRE Functional Activity Differs Substantially Among Primary HIV-1 Isolates.The HIV-1 Rev response element (RRE) adopts alternative conformations that promote different rates of virus replication.Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding.A long-awaited structure is rev-ealed.Limited nucleotide changes in the Rev response element (RRE) during HIV-1 infection alter overall Rev-RRE activity and Rev multimerization.Single-nucleotide changes in the HIV Rev-response element mediate resistance to compounds that inhibit Rev functionThe HIV-2 Rev-response element: determining secondary structure and defining folding intermediates.Cooperativity among Rev-associated nuclear export signals regulates HIV-1 gene expression and is a determinant of virus species tropismMulti-Faceted Post-Transcriptional Functions of HIV-1 Rev.A DEAD-box protein acts through RNA to promote HIV-1 Rev-RRE assemblyAn intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 rev prevents viral production.Transcriptional and posttranscriptional regulation of HIV-1 gene expressionRNA-guided assembly of Rev-RRE nuclear export complexesFunctional analyses reveal extensive RRE plasticity in primary HIV-1 sequences selected under selective pressureComparative analysis of RNA/protein dynamics for the arginine-rich-binding motif and zinc-finger-binding motif proteins encoded by HIV-1.The RNA-binding domain of influenzavirus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent mannerMapping the binding interface between an HIV-1 inhibiting intrabody and the viral protein RevRandomized codon mutagenesis reveals that the HIV Rev arginine-rich motif is robust to substitutions and that double substitution of two critical residues alters specificity.Regulation of transcription by long noncoding RNAs.Mathematical model of the Tat-Rev regulation of HIV-1 replication in an activated cell predicts the existence of oscillatory dynamics in the synthesis of viral componentsMeasuring cooperative Rev protein-protein interactions on Rev responsive RNA by fluorescence resonance energy transfer.RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complexDiverse mutants of HIV RRE IIB recognize wild-type Rev ARM or Rev ARM R35G-N40V.HIV Rev Assembly on the Rev Response Element (RRE): A Structural PerspectiveCooperative dimerization of a stably folded protein directed by a flexible RNA in the assembly of the HIV Rev dimer-RRE stem II complex.Host cell interactome of HIV-1 Rev includes RNA helicases involved in multiple facets of virus productionIdentification and Optimization of Thienopyridine Carboxamides as Inhibitors of HIV Regulatory Complexes.Thermodynamics of Rev-RNA interactions in HIV-1 Rev-RRE assembly.The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE AssemblyAn unusual topological structure of the HIV-1 Rev response element.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.
P2860
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P2860
A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA
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2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@ast
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@en
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@nl
type
label
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@ast
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@en
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@nl
prefLabel
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@ast
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@en
A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@nl
P2093
P2860
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A solution to limited genomic ...... tional HIV Rev oligomer on RNA
@en
P2093
Alan D Frankel
Iván D'Orso
Matthew D Daugherty
P2860
P304
P3181
P356
10.1016/J.MOLCEL.2008.07.016
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P577
2008-09-26T00:00:00Z