about
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A proteinHepatitis C virus internal ribosome entry site (IRES) stem loop IIId contains a phylogenetically conserved GGG triplet essential for translation and IRES folding.A plant virus replication system to assay the formation of RNA pseudotriloop motifs in RNA-protein interactionsStructure of the phylogenetically most conserved domain of SRP RNA.NMR structure of a ribosomal RNA hairpin containing a conserved CUCAA pentaloopSimultaneous recognition of HIV-1 TAR RNA bulge and loop sequences by cyclic peptide mimics of Tat proteinThe apical loop of the HIV-1 TAR RNA hairpin is stabilized by a cross-loop base pairSolution structure of the SL1 RNA of the M1 double-stranded RNA virus of Saccharomyces cerevisiae.NMR characterization of an oligonucleotide model of the miR-21 pre-elementTAR RNA loop: a scaffold for the assembly of a regulatory switch in HIV replication.In vitro selection identifies key determinants for loop-loop interactions: RNA aptamers selective for the TAR RNA element of HIV-1.A test of the model to predict unusually stable RNA hairpin loop stabilityStructural characterization of three RNA hexanucleotide loops from the internal ribosome entry site of poliovirusesCharacterization of a "kissing" hairpin complex derived from the human immunodeficiency virus genome.Visualizing transient low-populated structures of RNA.How binding of small molecule and peptide ligands to HIV-1 TAR alters the RNA motional landscape.Site-specific variations in RNA folding thermodynamics visualized by 2-aminopurine fluorescence.The retroviruses human immunodeficiency virus type 1 and Moloney murine leukemia virus adopt radically different strategies to regulate promoter-proximal polyadenylation.A small circular TAR RNA decoy specifically inhibits Tat-activated HIV-1 transcriptionIdentification of a novel HIV-1 TAR RNA bulge binding protein.The importance of a single G in the hairpin loop of the iron responsive element (IRE) in ferritin mRNA for structure: an NMR spectroscopy study.Structural and dynamic characterization of the upper part of the HIV-1 cTAR DNA hairpinTAR-RNA recognition by a novel cyclic aminoglycoside analogue.Structural and thermodynamic signatures that define pseudotriloop RNA hairpins.The Brome mosaic virus subgenomic promoter hairpin is structurally similar to the iron-responsive element and functionally equivalent to the minus-strand core promoter stem-loop C.The influence of monovalent cation size on the stability of RNA tertiary structures.Evidence for a base triple in the free HIV-1 TAR RNA.Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR.TAR RNA decoys inhibit tat-activated HIV-1 transcription after preinitiation complex formation.Local RNA conformational dynamics revealed by 2-aminopurine solvent accessibility.Structure of HIV TAR in complex with a Lab-Evolved RRM provides insight into duplex RNA recognition and synthesis of a constrained peptide that impairs transcription
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
An NMR study of the HIV-1 TAR element hairpin.
@en
An NMR study of the HIV-1 TAR element hairpin.
@nl
type
label
An NMR study of the HIV-1 TAR element hairpin.
@en
An NMR study of the HIV-1 TAR element hairpin.
@nl
prefLabel
An NMR study of the HIV-1 TAR element hairpin.
@en
An NMR study of the HIV-1 TAR element hairpin.
@nl
P356
P1433
P1476
An NMR study of the HIV-1 TAR element hairpin.
@en
P2093
Tinoco I Jr
P304
12522-12530
P356
10.1021/BI00097A032
P407
P577
1993-11-01T00:00:00Z