ReviewThe Journal of biological chemistry2019
Chiral checkpoints during protein biosynthesis.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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.
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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.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Structure-Activity Relationship Study of Antimicrobial Peptide with Cross-Kingdom Activity.Biochemistry · 2026Article
- Biomolecular and cellular chirality: Novel diagnostic perspectives for diseases.APL bioengineering · 2026Review
- Enhanced proteolytic stability and distinct mechanisms of a D-amino acid-modified antimicrobial peptide against Pseudomonas aeruginosa.Scientific reports · 2026Article
- Chiral methionine oxidation reagents reveal stereospecific proteome modifications.bioRxiv : the preprint server for biology · 2026Article
- Sources and Metabolism of D-Amino Acids and Their Roles as Biomarkers in Kidney Disease: A Review.Medical science monitor : international medical journal of experimental and clinical research · 2026Review
- DTD1 modulates synaptic efficacy by maintaining D-serine and D-aspartate homeostasis.Science China. Life sciences · 2025Article
- When Paul Berg meets Donald Crothers: an achiral connection through protein biosynthesis.Nucleic acids research · 2024Article
- A translation proofreader of archaeal origin imparts multi-aldehyde stress tolerance to land plants.eLife · 2024Article
- Distinct localization of chiral proofreaders resolves organellar translation conflict in plants.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis.Nucleic acids research · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- D-Peptide and D-Protein Technology: Recent Advances, Challenges, and Opportunities.Chembiochem : a European journal of chemical biology · 2023Review
- Biological effects of the loss of homochirality in a multicellular organism.Nature communications · 2022Article
- Switching a conflicted bacterial DTD-tRNA code is essential for the emergence of mitochondria.Science advances · 2022Article
- Recruitment of archaeal DTD is a key event toward the emergence of land plants.Science advances · 2021Article
- Antibacterial Activity and Mechanism of Linalool againstMolecules (Basel, Switzerland) · 2021Article
- Promiscuous Ribozymes and Their Proposed Role in Prebiotic Evolution.Chemical reviews · 2020Review
- Genomic innovation of ATD alleviates mistranslation associated with multicellularity in Animalia.eLife · 2020Article
- Loss-of-FunctionFrontiers in neurology · 2020Article
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 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein chains contain only l-amino acids, with the exception of the achiral glycine, making the chains homochiral. This homochirality is a prerequisite for proper protein folding and, hence, normal cellular function. The importance of d-amino acids as a component of the bacterial cell wall and their roles in neurotransmission in higher eukaryotes are well-established. However, the wider presence and the corresponding physiological roles of these specific amino acid stereoisomers have been appreciated only recently. Therefore, it is expected that enantiomeric fidelity has to be a key component of all of the steps in translation. Cells employ various molecular mechanisms for keeping d-amino acids away from the synthesis of nascent polypeptide chains. The major factors involved in this exclusion are aminoacyl-tRNA synthetases (aaRSs), elongation factor thermo-unstable (EF-Tu), the ribosome, and d-aminoacyl-tRNA deacylase (DTD). aaRS, EF-Tu, and the ribosome act as "chiral checkpoints" by preferentially binding to l-amino acids or l-aminoacyl-tRNAs, thereby excluding d-amino acids. Interestingly, DTD, which is conserved across all life forms, performs "chiral proofreading," as it removes d-amino acids erroneously added to tRNA. Here, we comprehensively review d-amino acids with respect to their occurrence and physiological roles, implications for chiral checkpoints required for translation fidelity, and potential use in synthetic biology.
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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.