RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins
about
Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation.Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG boxStructural basis of the RNA-binding specificity of human U1A proteinStructure and interactions of the translation initiation factor eIF1Novel DNA-binding properties of the RNA-binding protein TIAR.Molecular cloning of a RNA binding protein, S1-1Interaction of the RNA-binding domain of the hnRNP C proteins with RNAFunctional domains of the human splicing factor ASF/SF2NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A proteinRNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domainThe hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localizationAnalysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factorsU2AF homology motifs: protein recognition in the RRM worldFunctions of heterogeneous nuclear ribonucleoproteins in stem cell potency and differentiationNMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helixThree-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilusCrystal structure of the ribosomal protein S6 from Thermus thermophilusRibosomal protein L6: structural evidence of gene duplication from a primitive RNA binding proteinCrystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding proteinThe yeast nucleolar protein Nop4p contains four RNA recognition motifs necessary for ribosome biogenesis.Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA.Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolusPUB1: a major yeast poly(A)+ RNA-binding protein.The yeast NOP4 gene product is an essential nucleolar protein required for pre-rRNA processing and accumulation of 60S ribosomal subunits.TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function.Further biochemical and kinetic characterization of human eukaryotic initiation factor 4HMutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activityLa protein and its associated small nuclear and nucleolar precursor RNAsRecognition of nascent RNA by the human La antigen: conserved and divergent features of structure and functionSynthetic lethality with fibrillarin identifies NOP77p, a nucleolar protein required for pre-rRNA processing and modificationCharacterization of the major hnRNP proteins from Drosophila melanogaster.Contribution of the tyrosines to the structure and function of the human U1A N-terminal RNA binding domain.Bioassaying putative RNA-binding motifs in a protein encoded by a gene that influences courtship and visually mediated behavior in Drosophila: in vitro mutagenesis of nonA.Mutational definition of RNA-binding and protein-protein interaction domains of heterogeneous nuclear RNP C1.Analysis of RNA-binding proteins by in vitro genetic selection: identification of an amino acid residue important for locking U1A onto its RNA target.Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin.Two distinct temperature-sensitive alleles at the elav locus of Drosophila are suppressed nonsense mutations of the same tryptophan codon.The RNA binding site of bacteriophage MS2 coat protein.Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains.
P2860
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P2860
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins
description
1991 nî lūn-bûn
@nan
1991 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի մարտին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@ast
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@en
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@nl
type
label
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@ast
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@en
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@nl
prefLabel
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@ast
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@en
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@nl
P2093
P2860
P356
P1476
RNA-binding domain of the A pr ...... similar to ribosomal proteins
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.6.2495
P407
P577
1991-03-15T00:00:00Z