Structural basis of translational control by Escherichia coli threonyl tRNA synthetase - Wikidata - awgldk - TriplyDB

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

http://www.wikidata.org/entity/Q27638853

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A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism Recurrent structural RNA motifs, Isostericity Matrices and sequence alignments Common peptides study of aminoacyl-tRNA synthetases Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA.Clustering RNA structural motifs in ribosomal RNAs using secondary structural alignment.Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis.Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.Regulation of translation initiation by RNA binding proteins Numerical integration methods and layout improvements in the context of dynamic RNA visualization.RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon A novel processive mechanism for DNA synthesis revealed by structure, modeling and mutagenesis of the accessory subunit of human mitochondrial DNA polymerase Expression, purification and preliminary X-ray diffraction studies of the transcriptional factor PyrR from Bacillus halodurans.Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed.Genes of Helicobacter pylori regulated by attachment to AGS cells.A domain for editing by an archaebacterial tRNA synthetase Predicting and modeling RNA architecture.Emergence and evolution.Piecemeal Buildup of the Genetic Code, Ribosomes, and Genomes from Primordial tRNA Building Blocks Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from Aeropyrum pernix and Sulfolobus tokodaii.RNAMotifScan: automatic identification of RNA structural motifs using secondary structural alignment.Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation.

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P2860

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

http://www.wikidata.org/entity/Q27638853

description

2002 nî lūn-bûn

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2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

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2002年論文

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2002年論文

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2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

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2002年论文

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name

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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type

label

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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prefLabel

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

@ast

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

@en

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

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P1433

Nature structural biology

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Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

@en

P2093

Alfredo Torres-Larios

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

Anne-Catherine Dock-Bregeon

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

Bernard Ehresmann

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Bernard Rees

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Chantal Ehresmann

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Joel Caillet

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Mathias Springer

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Pascale Romby

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Rajan Sankaranarayanan

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343-7

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scholarly article

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10.1038/NSB789

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5

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9

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2002-05-01T00:00:00Z

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11412928

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11953757

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Escherichia coli