Pages that link to "Q46640850"
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The following pages link to Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex (Q46640850):
Displaying 50 items.
- Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p (Q24657415) (← links)
- Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation (Q24673381) (← links)
- Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase (Q27694602) (← links)
- Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. (Q27930245) (← links)
- A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum (Q27972876) (← links)
- p23 H implicated as cis/trans regulator of AlaXp-directed editing for mammalian cell homeostasis (Q28508493) (← links)
- Distinct domains of tRNA synthetase recognize the same base pair (Q28584834) (← links)
- Resampling and editing of mischarged tRNA prior to translation elongation (Q34151351) (← links)
- Characterization of benzoxaborole-based antifungal resistance mutations demonstrates that editing depends on electrostatic stabilization of the leucyl-tRNA synthetase editing cap (Q34209500) (← links)
- Amino-Acid-Dependent Shift in tRNA Synthetase Editing Mechanisms (Q34226243) (← links)
- Predicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes. (Q35165320) (← links)
- Mistranslation and its control by tRNA synthetases (Q35173034) (← links)
- Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons (Q35213173) (← links)
- Aminoacyl-tRNA synthetase complexes in evolution (Q35381830) (← links)
- Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific (Q35451324) (← links)
- Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation (Q35616247) (← links)
- Substrate Specificity of Bacterial Prolyl-tRNA Synthetase Editing Domain Is Controlled by a Tunable Hydrophobic Pocket (Q35728198) (← links)
- Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain (Q35844603) (← links)
- Role of coupled dynamics in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases (Q35915716) (← links)
- Bacterial transfer RNAs (Q35974736) (← links)
- The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code (Q36008178) (← links)
- Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine. (Q36088329) (← links)
- In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity (Q36502043) (← links)
- Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases (Q36528700) (← links)
- Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK (Q36696214) (← links)
- Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex (Q36793750) (← links)
- Development of tRNA synthetases and connection to genetic code and disease (Q36901628) (← links)
- Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed (Q36973475) (← links)
- Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase (Q37112012) (← links)
- Full implementation of the genetic code by tryptophanyl-tRNA synthetase requires intermodular coupling (Q37348960) (← links)
- A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes (Q37469532) (← links)
- tRNAs: cellular barcodes for amino acids. (Q37480875) (← links)
- Distinct tRNA recognition strategies used by a homologous family of editing domains prevent mistranslation (Q37680392) (← links)
- Cellular mechanisms that control mistranslation (Q37809740) (← links)
- Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis (Q38132082) (← links)
- Exploring the evolutionary diversity and assembly modes of multi-aminoacyl-tRNA synthetase complexes: lessons from unicellular organisms (Q38260221) (← links)
- Strictly conserved lysine of prolyl-tRNA Synthetase editing domain facilitates binding and positioning of misacylated tRNA(Pro.). (Q38741646) (← links)
- Characterization of 16S rRNA mutations that decrease the fidelity of translation initiation (Q40189792) (← links)
- Naturally Occurring Isoleucyl-tRNA Synthetase without tRNA-dependent Pre-transfer Editing (Q41209208) (← links)
- Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells (Q41862315) (← links)
- Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase (Q42203083) (← links)
- Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation (Q43251134) (← links)
- Interdomain communication modulates the tRNA-dependent pre-transfer editing of leucyl-tRNA synthetase. (Q44478323) (← links)
- Fluorothreonyl-tRNA deacylase prevents mistranslation in the organofluorine producer Streptomyces cattleya (Q46113351) (← links)
- Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase (Q46819076) (← links)
- Conformational and chemical selection by a trans-acting editing domain. (Q47998651) (← links)
- Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate (Q48358169) (← links)
- Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure (Q58559184) (← links)
- Stoichiometry of triple-sieve tRNA editing complex ensures fidelity of aminoacyl-tRNA formation (Q93003081) (← links)
- Genomic innovation of ATD alleviates mistranslation associated with multicellularity in Animalia (Q95940280) (← links)