ReviewCurrent opinion in microbiology2011
Functional context, biosynthesis, and genetic encoding of pyrrolysine.
Review in Current opinion in microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 104 citations in OpenAlex.
- Pyrrolysine supply and demand shapes the translational landscape inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Methanogenesis from tetramethylammonium and choline inFrontiers in microbiology · 2026Article
- Identification of key steps in the evolution of anaerobic methanotrophy inScience advances · 2025Article
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- BeyondChemical reviews · 2025Review
- Pyrrolysine Aminoacyl-tRNA Synthetase as a Tool for Expanding the Genetic Code.International journal of molecular sciences · 2025Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
- Non-Canonical Amino Acids as Building Blocks for Peptidomimetics: Structure, Function, and Applications.Biomolecules · 2023Review
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Methyl-Based Methanogenesis: an Ecological and Genomic Review.Microbiology and molecular biology reviews : MMBR · 2023Review
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- Review
- Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.Communications biology · 2023Article
- Ancestral archaea expanded the genetic code with pyrrolysine.The Journal of biological chemistry · 2022Article
- Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022Review
- Recoding of stop codons expands the metabolic potential of two novel Asgardarchaeota lineages.ISME communications · 2021Article
- Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.International journal of molecular sciences · 2021Review
- An Ecological Basis for Dual Genetic Code Expansion in Marine Deltaproteobacteria.Frontiers in microbiology · 2021Article
- Expanding the Genetic Code for Neuronal Studies.Chembiochem : a European journal of chemical biology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In Methanosarcina spp., amber codons in methylamine methyltransferase genes are translated as the 22nd amino acid, pyrrolysine. The responsible pyl genes plus amber-codon containing methyltransferase genes have been identified in four archaeal and five bacterial genera, including one human pathogen. In Escherichia coli, the recombinant pylBCD gene products biosynthesize pyrrolysine from two molecules of lysine and the pylTS gene products direct pyrrolysine incorporation into protein. In the proposed biosynthetic pathway, PylB forms methylornithine from lysine, which is joined to another lysine by PylC, and oxidized to pyrrolysine by PylD. Structures of the catalytic domain of pyrrolysyl-tRNA synthetase (archaeal PylS or bacterial PylSc) revealed binding sites for tRNAPyl and pyrrolysine. PylS and tRNAPyl are now being exploited as an orthogonal pair in recombinant systems for introduction of useful modified amino acids into proteins.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.