Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology
about
Single-stranded DNA-binding proteins: multiple domains for multiple functionsStructure and semi-sequence-specific RNA binding of Nrd1A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteinsStructured and disordered regions cooperatively mediate DNA-binding autoinhibition of ETS factors ETV1, ETV4 and ETV5.Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.Comparative analyses of the thermodynamic RNA binding signatures of different types of RNA recognition motifs.The splicing activator DAZAP1 integrates splicing control into MEK/Erk-regulated cell proliferation and migration.RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains.The First Crystal Structure of the UP1 Domain of hnRNP A1 Bound to RNA Reveals a New Look for an Old RNA Binding Protein.Assembly of functional ribonucleoprotein complexes by AU-rich element RNA-binding protein 1 (AUF1) requires base-dependent and -independent RNA contacts.High-affinity interaction of hnRNP A1 with conserved RNA structural elements is required for translation and replication of enterovirus 71.hnRNP A1: the Swiss army knife of gene expression.The dynamic duo: combining NMR and small angle scattering in structural biology.Thermodynamic and phylogenetic insights into hnRNP A1 recognition of the HIV-1 exon splicing silencer 3 element.Tandem hnRNP A1 RNA recognition motifs act in concert to repress the splicing of survival motor neuron exon 7.A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43.The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.NMR studies on protein-nucleic acid interaction.Segmental Isotopic Labeling of Proteins for NMR Study Using Intein Technology.Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function.Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1.RGG-box in hnRNPA1 specifically recognizes the telomere G-quadruplex DNA and enhances the G-quadruplex unfolding ability of UP1 domain
P2860
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P2860
Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Solution structure of the two ...... nucleic acid binding topology
@ast
Solution structure of the two ...... nucleic acid binding topology
@en
Solution structure of the two ...... nucleic acid binding topology
@nl
type
label
Solution structure of the two ...... nucleic acid binding topology
@ast
Solution structure of the two ...... nucleic acid binding topology
@en
Solution structure of the two ...... nucleic acid binding topology
@nl
prefLabel
Solution structure of the two ...... nucleic acid binding topology
@ast
Solution structure of the two ...... nucleic acid binding topology
@en
Solution structure of the two ...... nucleic acid binding topology
@nl
P2860
P1476
Solution structure of the two ...... nucleic acid binding topology
@en
P2860
P2888
P304
P356
10.1007/S10858-012-9696-4
P577
2013-01-01T00:00:00Z
P5875
P6179
1015896176