Structural basis for cooperative RNA binding and export complex assembly by HIV Rev - sprookjes - yvandenbroek - TriplyDB

Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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HIV Genome-Wide Protein Associations: a Review of 30 Years of Research A structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1 Translational Control of the HIV Unspliced Genomic RNA The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE Binding Structural basis of the non-coding RNA RsmZ acting as a protein sponge HTLV-1 Rex Tunes the Cellular Environment Favorable for Viral Replication The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA Evolution of a species-specific determinant within human CRM1 that regulates the post-transcriptional phases of HIV-1 replication Effect of intercalator and Lewis acid-base branched peptide complex formation: boosting affinity towards HIV-1 RRE RNA Rev-RRE Functional Activity Differs Substantially Among Primary HIV-1 Isolates.Characterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNA 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 function The 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 tropism Multi-Faceted Post-Transcriptional Functions of HIV-1 Rev.A cell-penetrating antibody fragment against HIV-1 Rev has high antiviral activity: characterization of the paratope Transcriptional and posttranscriptional regulation of HIV-1 gene expression Comparative analysis of seven viral nuclear export signals (NESs) reveals the crucial role of nuclear export mediated by the third NES consensus sequence of nucleoprotein (NP) in influenza A virus replication.RNA-guided assembly of Rev-RRE nuclear export complexes Generation and use of antibody fragments for structural studies of proteins refractory to crystallization Biochemical analysis of the complex between the tetrameric export adapter protein Rec of HERV-K/HML-2 and the responsive RNA element RcRE pck30.Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway Nuclear magnetic resonance structure revealed that the human polyomavirus JC virus agnoprotein contains an α-helix encompassing the Leu/Ile/Phe-rich domain.The RNA-binding domain of influenzavirus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent manner Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.Branched peptide boronic acids (BPBAs): a novel mode of binding towards RNA.HIV control is mediated in part by CD8+ T-cell targeting of specific epitopes.Mapping the binding interface between an HIV-1 inhibiting intrabody and the viral protein Rev Comparison of SIV and HIV-1 genomic RNA structures reveals impact of sequence evolution on conserved and non-conserved structural motifs.Randomized 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.RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complex HIV Rev Assembly on the Rev Response Element (RRE): A Structural Perspective Cooperative dimerization of a stably folded protein directed by a flexible RNA in the assembly of the HIV Rev dimer-RRE stem II complex.

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

http://www.wikidata.org/entity/Q24569707

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2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

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Nature Structural & Molecular Biology

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Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

@en

P2093

Alan D Frankel

http://www.w3.org/2001/XMLSchema#string

Bella Liu

http://www.w3.org/2001/XMLSchema#string

Matthew D Daugherty

http://www.w3.org/2001/XMLSchema#string

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THE HIV-1 REV PROTEIN

Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element

HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes

A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA

HIV-1 Rev protein assembles on viral RNA one molecule at a time.

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Structural Basis for Dimerization in DNA Recognition by Gal4

Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP

Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex

Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

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1337-42

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scholarly article

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10.1038/NSMB.1902

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11

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17

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2010-11-01T00:00:00Z

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47450454

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1043152769

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20953181

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structural biology

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2988976

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