Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein - Wikidata - thesis-toulmin - TriplyDB

Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein

Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein

http://www.wikidata.org/entity/Q27667471

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Transfer RNA post-transcriptional processing, turnover, and subcellular dynamics in the yeast Saccharomyces cerevisiae Methylated nucleosides in tRNA and tRNA methyltransferases Structural and functional analyses of the archaeal tRNA m2G/m22G10 methyltransferase aTrm11 provide mechanistic insights into site specificity of a tRNA methyltransferase that contains common RNA-binding modules The methyltransferase adaptor protein Trm112 is involved in biogenesis of both ribosomal subunits Trm112 is required for Bud23-mediated methylation of the 18S rRNA at position G1575.Chemical Proteomic Profiling of Human Methyltransferases Structural and functional studies of Bud23-Trm112 reveal 18S rRNA N7-G1575 methylation occurs on late 40S precursor ribosomes Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112 Extending RosettaDock with water, sugar, and pH for prediction of complex structures and affinities for CAPRI rounds 20-27 The Stability of Ribosome Biogenesis Factor WBSCR22 Is Regulated by Interaction with TRMT112 via Ubiquitin-Proteasome Pathway Substrate Specificity of the HEMK2 Protein Glutamine Methyltransferase and Identification of Novel Substrates Trmt112 gene expression in mouse embryonic development Diversity in mechanism and function of tRNA methyltransferases.Insights into molecular plasticity in protein complexes from Trm9-Trm112 tRNA modifying enzyme crystal structure.Inclusion of the orientational entropic effect and low-resolution experimental information for protein-protein docking in Critical Assessment of PRedicted Interactions (CAPRI).How good is automated protein docking?Performance of ZDOCK in CAPRI rounds 20-26.Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.Protein and nucleic acid methylating enzymes: mechanisms and regulation Integrative computational modeling of protein interactions.Docking, scoring, and affinity prediction in CAPRI.Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification.Physical and functional interaction between the methyltransferase Bud23 and the essential DEAH-box RNA helicase Ecm16 Genome-wide Screening of Regulators of Catalase Expression: ROLE OF A TRANSCRIPTION COMPLEX AND HISTONE AND tRNA MODIFICATION COMPLEXES ON ADAPTATION TO STRESS.Score_set: a CAPRI benchmark for scoring protein complexes.Transcriptome-wide Analysis of Roles for tRNA Modifications in Translational Regulation.Binding synergy as an essential step for tRNA editing and modification enzyme codependence in Trypanosoma brucei.Defining the limits of homology modeling in information-driven protein docking.The targets of CAPRI rounds 20-27.Monitoring the 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) modification in eukaryotic tRNAs via the gamma-toxin endonuclease.Using a consensus approach based on the conservation of inter-residue contacts to rank CAPRI models.Improved flexible refinement of protein docking in CAPRI rounds 22-27.Flexible docking and refinement with a coarse-grained protein model using ATTRACT.Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.

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Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein

http://www.wikidata.org/entity/Q27667471

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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prefLabel

Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Nucleic Acids Research

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Mechanism of activation of met ...... on by the Trm112 'hub' protein

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Dominique Liger

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Herman van Tilbeurgh

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Liliana Mora

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Nathalie Scrima

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Noureddine Lazar

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Sabine Figaro

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Valérie Heurgué-Hamard

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P2860

Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications

Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding

Human AlkB homolog ABH8 Is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival

Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA.

HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1

Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase

The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1

Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase

The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases

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6249-6259

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scholarly article

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4761174

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10.1093/NAR/GKR176

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14

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39

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Richard H. Buckingham

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2011-04-07T00:00:00Z

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51037198

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21478168

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3152332

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