Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA. - Wikidata - awgldk - TriplyDB

Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA.

Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA.

http://www.wikidata.org/entity/Q27640301

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Dyskeratosis congenita mutations in the H/ACA domain of human telomerase RNA affect its assembly into a pre-RNP Solution structure and dynamics of the wild-type pseudoknot of human telomerase RNA Thermodynamics and NMR studies on Duck, Heron and Human HBV encapsidation signals A human-Tetrahymena pseudoknot chimeric telomerase RNA reconstitutes a nonprocessive enzyme in vitro that is defective in telomere elongation It all comes together at the ends: telomerase structure, function, and biogenesis Single-molecule analysis of telomerase structure and function The solution structure of an essential stem-loop of human telomerase RNA Structure and thermodynamics of a conserved U2 snRNA domain from yeast and human YNMG tetraloop formation by a dyskeratosis congenita mutation in human telomerase RNA.H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification Breaking pseudo-twofold symmetry in the poliovirus 3'-UTR Y-stem by restoring Watson-Crick base pairs Structurally conserved five nucleotide bulge determines the overall topology of the core domain of human telomerase RNA Structure of the yeast U2/U6 snRNA complex Pyrimidine motif triple helix in the Kluyveromyces lactis telomerase RNA pseudoknot is essential for function in vivo What a Difference an OH Makes: Conformational Dynamics as the Basis for the Ligand Specificity of the Neomycin-Sensing Riboswitch Thermodynamic characterization of the Saccharomyces cerevisiae telomerase RNA pseudoknot domain in vitro Improved free energy parameters for RNA pseudoknotted secondary structure prediction.Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: temperature-/urea-dependent folding kinetics and thermodynamics.Predicting loop-helix tertiary structural contacts in RNA pseudoknots.Entropic stabilization of the folded states of RNA due to macromolecular crowding Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.Coordination among tertiary base pairs results in an efficient frameshift-stimulating RNA pseudoknot.Functional analysis of the pseudoknot structure in human telomerase RNA.RNA pseudoknots: folding and finding.Architecture of human telomerase RNA.NMR spectroscopy of RNA.The Chemical Origin of Behavior is Rooted in Abiogenesis Analysis of a long-range interaction between conserved domains of human telomerase RNA.Refined secondary-structure models of the core of yeast and human telomerase RNAs directed by SHAPE.Conformational analysis of the telomerase RNA pseudoknot hairpin by Raman spectroscopy Functional importance of telomerase pseudoknot revealed by single-molecule analysis.Telomere biology of human hematopoietic stem cells.Identification and functional characterization of 2 variant alleles of the telomerase RNA template gene (TERC) in a patient with dyskeratosis congenita.A role for a novel 'trans-pseudoknot' RNA-RNA interaction in the functional dimerization of human telomerase.A novel pseudoknot element is essential for the action of a yeast telomerase.Single-molecule mechanical unfolding and folding of a pseudoknot in human telomerase RNA.Pseudoknot structures with conserved base triples in telomerase RNAs of ciliates RNA-PAIRS: RNA probabilistic assignment of imino resonance shifts.Expression of telomerase RNA template, but not telomerase reverse transcriptase, is limiting for telomere length maintenance in vivo RNA folding: conformational statistics, folding kinetics, and ion electrostatics.

P2860

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P2860

Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA.

http://www.wikidata.org/entity/Q27640301

description

2003 nî lūn-bûn

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2003 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2003 թվականի հունվարին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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name

Mutations linked to dyskeratos ...... equilibrium in telomerase RNA

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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Proceedings of the National Academy of Sciences of the United States of America

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Mutations linked to dyskeratos ...... equilibrium in telomerase RNA.

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P2093

Carla A Theimer

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L David Finger

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Lukas Trantirek

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P2860

A telomerase component is defective in the human disease dyskeratosis congenita

In vitro assembly of human H/ACA small nucleolar RNPs reveals unique features of U17 and telomerase RNAs

Analysis of the structure of human telomerase RNA in vivo

X-linked dyskeratosis congenita is predominantly caused by missense mutations in the DKC1 gene.

Solution structure of an RNA duplex including a C-U base pair

A novel family of RNA tetraloop structure forms the recognition site for Saccharomyces cerevisiae RNase III.

Structure of an RNA double helix including uracil-uracil base pairs in an internal loop

The structure of an RNA dodecamer shows how tandem U-U base pairs increase the range of stable RNA structures and the diversity of recognition sites

Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure

Human telomerase activation requires two independent interactions between telomerase RNA and telomerase reverse transcriptase

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10.1073/PNAS.242720799

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2

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100

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2003-01-13T00:00:00Z

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10952040

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12525685

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141015

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