Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding.
about
The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitroU2AF homology motifs: protein recognition in the RRM worldBiased exon/intron distribution of cryptic and de novo 3' splice sitesAlternative Conformations at the RNA-binding Surface of the N-terminal U2AF65 RNA Recognition MotifNovel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AFU2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein InteractionsU2AF binding selects for the high conservation of the C. elegans 3' splice site.Exon repression by polypyrimidine tract binding proteinDrosophila Sex-lethal protein mediates polyadenylation switching in the female germline.RNA induces conformational changes in the SF1/U2AF65 splicing factor complexAnalysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicingThe polypyrimidine tract binding protein (PTB) represses splicing of exon 6B from the beta-tropomyosin pre-mRNA by directly interfering with the binding of the U2AF65 subunitMultiple RNA binding domains of Bruno confer recognition of diverse binding sites for translational repression.Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.Building specificity with nonspecific RNA-binding proteins.Large-scale comparative analysis of splicing signals and their corresponding splicing factors in eukaryotes.A conditional role of U2AF in splicing of introns with unconventional polypyrimidine tractsSolution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shiftFRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.Aberrant 3' splice sites in human disease genes: mutation pattern, nucleotide structure and comparison of computational tools that predict their utilization.Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65.Structuring of the 3' splice site by U2AF65.
P2860
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P2860
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
name
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@ast
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@en
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor
@nl
type
label
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@ast
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@en
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor
@nl
prefLabel
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@ast
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@en
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor
@nl
P2093
P2860
P356
P1433
P1476
Sex lethal and U2 small nuclea ...... ing multiple modes of binding.
@en
P2093
Andrew Rahn
Hiren Banerjee
Ravinder Singh
William Davis
P2860
P356
10.1261/RNA.2131603
P407
P577
2003-01-01T00:00:00Z