The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification. - Test2 - elhamkhani - TriplyDB

The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.

The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.

http://www.wikidata.org/entity/Q33569825

about

An enhanced H/ACA RNP assembly mechanism for human telomerase RNA Small RNAs with big implications: new insights into H/ACA snoRNA function and their role in human disease Progress in structural studies of telomerase Structure of H/ACA RNP Protein Nhp2p Reveals Cis/Trans Isomerization of a Conserved Proline at the RNA and Nop10 Binding Interface In Human Pseudouridine Synthase 1 (hPus1), a C-Terminal Helical Insert Blocks tRNA from Binding in the Same Orientation as in the Pus1 Bacterial Homologue TruA, Consistent with Their Different Target Selectivities Inhibition of human dyskerin as a new approach to target ribosome biogenesis Structure-function relationships of archaeal Cbf5 during in vivo RNA-guided pseudouridylation.Digital genome-wide ncRNA expression, including SnoRNAs, across 11 human tissues using polyA-neutral amplification.New molecular engineering approaches for crystallographic studies of large RNAs Comparative study of two box H/ACA ribonucleoprotein pseudouridine-synthases: relation between conformational dynamics of the guide RNA, enzyme assembly and activity.Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1.Pseudouridine formation in archaeal RNAs: The case of Haloferax volcanii.rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells.Contribution of two conserved histidines to the dual activity of archaeal RNA guide-dependent and -independent pseudouridine synthase Cbf5.Identification of Genetic Differentiation between Waxy and Common Maize by SNP Genotyping.Accurate placement of substrate RNA by Gar1 in H/ACA RNA-guided pseudouridylation.Pseudouridine: still mysterious, but never a fake (uridine)!Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs.Ribosome biogenesis in the yeast Saccharomyces cerevisiae Specific RNA-protein interactions detected with saturation transfer difference NMR The genetics and clinical manifestations of telomere biology disorders.Human telomerase activity regulation.The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA.Telomere lengthening and other functions of telomerase.Updates on the biology and management of dyskeratosis congenita and related telomere biology disorders.H/ACA Box Small Nucleolar RNA 7A Promotes the Self-Renewal of Human Umbilical Cord Mesenchymal Stem Cells.Eukaryotic stand-alone pseudouridine synthases - RNA modifying enzymes and emerging regulators of gene expression?Telomeres in cancer: tumour suppression and genome instability.Progress in Human and Tetrahymena Telomerase Structure Determination.Pseudouridine in the Anticodon of Escherichia coli tRNATyr(QΨA) Is Catalyzed by the Dual Specificity Enzyme RluF.Archaeal proteins Nop10 and Gar1 increase the catalytic activity of Cbf5 in pseudouridylating tRNA.Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10.Protein synthesis: Stop the nonsense rRNA processing rRNA modification in the nucleus and cytosol Dysfunctional telomeres and hematological disorders.Biology and clinical relevance of noncoding sno/scaRNAs.

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The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.

http://www.wikidata.org/entity/Q33569825

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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name

The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

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JBC.R109.076893

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Journal of Biological Chemistry

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The box H/ACA ribonucleoprotei ...... nscriptional RNA modification.

@en

P2093

Adrian R Ferré-D'Amaré

http://www.w3.org/2001/XMLSchema#string

Tomoko Hamma

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P2860

Tools for integrated sequence-structure analysis with UCSF Chimera.

Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea

Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation

The K-loop, a general feature of the Pyrococcus C/D guide RNAs, is an RNA structural motif related to the K-turn.

Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity.

The kink-turn: a new RNA secondary structure motif

Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme

Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure

The Crystal Structure of E. coli rRNA Pseudouridine Synthase RluE

H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification

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805-809

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scholarly article

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10.1074/JBC.R109.076893

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2

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285

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2009-11-16T00:00:00Z

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19917616

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Post-transcriptional modification

ribonucleoprotein

protein structure

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2801282

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