FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.
about
The MUC1 extracellular domain subunit is found in nuclear speckles and associates with spliceosomesDirect interaction between hnRNP-M and CDC5L/PLRG1 proteins affects alternative splice site choiceSplicing factors SF1 and U2AF associate in extraspliceosomal complexesPerturbation of chromatin structure globally affects localization and recruitment of splicing factorsCloning and characterization of a novel splice variant of human U2AF1L3 gene.Inhibition of RhoA signaling with increased Bves in trabecular meshwork cellsBves modulates tight junction associated signaling.Interactions of SR45, an SR-like protein, with spliceosomal proteins and an intronic sequence: insights into regulated splicing.Homeostatic levels of SRC-2 and SRC-3 promote early human adipogenesis.U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicingThe in vivo dynamics of TCERG1, a factor that couples transcriptional elongation with splicingSpatial mapping of splicing factor complexes involved in exon and intron definition.A FRET-based assay for characterization of alternative splicing events using peptide nucleic acid fluorescence in situ hybridizationIn vivo detection of RNA-binding protein interactions with cognate RNA sequences by fluorescence resonance energy transfer.Alternative splicing of U2AF1 reveals a shared repression mechanism for duplicated exons.Spatial Organization and Dynamics of Transcription Elongation and Pre-mRNA Processing in Live Cells.Probing nucleic acid interactions and pre-mRNA splicing by Förster Resonance Energy Transfer (FRET) microscopyMonitoring Keap1-Nrf2 interactions in single live cells.In vivo requirement of the small subunit of U2AF for recognition of a weak 3' splice site.The Arabidopsis splicing factors, AtU2AF65, AtU2AF35, and AtSF1 shuttle between nuclei and cytoplasms.The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells.Stoichiometries of U2AF35, U2AF65 and U2 snRNP reveal new early spliceosome assembly pathways.The cancer-associated U2AF35 470A>G (Q157R) mutation creates an in-frame alternative 5' splice site that impacts splicing regulation in Q157R patients.
P2860
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P2860
FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
@wuu
2005年学术文章
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2005年学术文章
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2005年学术文章
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name
FRET analyses of the U2AF comp ...... el self-interaction of U2AF35.
@en
type
label
FRET analyses of the U2AF comp ...... el self-interaction of U2AF35.
@en
prefLabel
FRET analyses of the U2AF comp ...... el self-interaction of U2AF35.
@en
P2093
P2860
P50
P356
P1433
P1476
FRET analyses of the U2AF comp ...... el self-interaction of U2AF35.
@en
P2093
Janet Chusainow
Laura Trinkle-Mulcahy
Paul M Ajuh
P2860
P304
P356
10.1261/RNA.7277705
P407
P577
2005-08-01T00:00:00Z