The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
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Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Human DTD1 encodes D-aminoacyl-tRNA deacylase 1, a conserved, free-standing trans-editing enzyme in translational quality control. Its principal reaction is hydrolysis of the ester bond linking a D-amino acid to tRNA:
D-aminoacyl-tRNA + H₂O → D-amino acid + free tRNA.
This reaction recycles otherwise unusable tRNA and limits entry of D-amino acids into nascent proteins. DTD1 also has a second, physiologically important proofreading activity: removal of achiral glycine mistakenly attached to tRNA^Ala. The mechanistic evidence is strong at the conserved-family level, but comparatively little accession-resolved experimentation has been reported for human A0A2R8YCT7 itself.
The supplied record is internally consistent: UniProt A0A2R8YCT7, gene DTD1, organism Homo sapiens, and Ensembl protein ENSP00000493969.1 are annotated as D-aminoacyl-tRNA deacylase, EC 3.1.1.96. Its reported InterPro/Pfam features—Daa-tRNA_deacyls_DTD (IPR003732), DTD-like superfamily (IPR023509), and Tyr_Deacylase/PF02580—match the experimentally defined DTD fold and DTD1 family. Canonical DTD1 occurs in bacteria and eukaryotes and is highly conserved; one comparative analysis reports approximately 39% sequence identity between E. coli and human DTD and identifies a human structure as PDB 2OKV. (das2019poisoningafungal pages 9-11, das2019poisoningafungal pages 11-16)
An accession caveat is necessary. The reviewed/canonical human protein is commonly represented as UniProt Q8TEA8, whereas A0A2R8YCT7 is an Ensembl-derived, unreviewed entry. Accordingly, literature about “human DTD1” supports the gene/family annotation, but should not automatically be interpreted as isoform-specific evidence for every feature of A0A2R8YCT7. No conflicting same-symbol gene or non-human DTD1 was substituted in this report.
| Topic | Best-supported conclusion | Evidence species/type | Confidence/limitations |
|---|---|---|---|
| Identity/accession | A0A2R8YCT7 is the supplied human Ensembl-derived DTD1 entry (ENSP00000493969.1), annotated as D-aminoacyl-tRNA deacylase and carrying DTD/Tyr-deacylase-family domains. Canonical human DTD1 is commonly represented by UniProt Q8TEA8; accession-level equivalence should not be assumed. | Supplied UniProt annotation; human protein references identify conserved DTD1 and structure 2OKV (das2019poisoningafungal pages 9-11, das2019poisoningafungal pages 11-16) | High for gene/family identity; moderate for the precise relationship between A0A2R8YCT7 and Q8TEA8 because accession-specific mapping was not established experimentally. |
| Enzyme reaction | Hydrolyzes the ester bond of a D-aminoacyl-tRNA, yielding free tRNA and the corresponding D-amino acid (EC 3.1.1.96). | Direct biochemical evidence in bacterial and yeast orthologs; conserved-family inference for human DTD1 (soutourina2000metabolismofdaminoacyltrnas pages 1-1, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2) | High for the DTD1 family; direct human kinetics were not available in the retrieved evidence. |
| Primary substrates | Broadly recognizes D-aminoacyl-tRNAs rather than only D-Tyr-tRNA; demonstrated ortholog substrates include D-Tyr-, D-Trp-, D-Asp-, and D-Phe-tRNAs, with cellular evidence implicating additional D-aminoacyl-tRNAs. | Direct bacterial/yeast biochemistry and genetics; ortholog inference for human (soutourina2000metabolismofdaminoacyltrnas pages 1-1, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2) | High for broad family specificity; exact human substrate range and kinetic preferences remain incompletely quantified. |
| Rejected/protected substrates | Correct L-aminoacyl-tRNAs are generally rejected through L-chiral exclusion. Cognate Gly-tRNA must be protected because glycine is achiral and therefore cannot be excluded by stereochemistry alone. | Conserved structural mechanism and bacterial biochemical studies (das2019poisoningafungal pages 11-16, kumar2024whenpaulberg pages 4-5) | High for the mechanistic principle; exceptions and substrate-dependent weak activities exist, so “absolute” rejection should not be assumed for every DTD1 ortholog. |
| Gly-tRNA editing and discriminator base | DTD1 also removes erroneous Gly-tRNA^Ala. Activity can be approximately 1,000-fold greater on Gly-tRNA^Ala than on cognate Gly-tRNA^Gly. The tRNA nucleotide at position 73 strongly controls this discrimination; eukaryotic and bacterial DTD1 systems have co-evolved different discriminator-base preferences. | Direct bacterial and comparative eukaryotic biochemistry; evolutionary inference for human (kumar2024whenpaulberg pages 5-6, kumar2023distinctlocalizationof pages 2-4) | High for DTD1-family biology; human-specific quantitative measurements were not retrieved. |
| Structure/mechanism | DTD1 adopts the DTD-like fold and functions as a homodimer with active sites at the subunit interface. An invariant cross-subunit Gly-cisPro motif captures the substrate’s chiral center, explaining rejection of L-aminoacyl-tRNAs and possible action on achiral glycine. A human DTD1 structure is deposited as PDB 2OKV. | Bacterial crystallography plus conserved-family analysis; human structural entry (das2019poisoningafungal pages 11-16, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 2-4) | High for fold, dimeric mechanism, and motif conservation; the retrieved evidence did not provide a peer-reviewed functional analysis of PDB 2OKV itself. |
| Cellular localization | Recent synthesis states that the single opisthokont DTD1 is colocalized to cytoplasm and mitochondria; an independent report cited in the 2023 study places human DTD1 in the nucleus. Thus human DTD1 may occur in multiple intracellular compartments, but it is not established here as exclusively cytosolic or mitochondrial. | Comparative/evolutionary synthesis and cited human localization report; no retrieved direct localization experiment for A0A2R8YCT7 (kumar2024whenpaulberg pages 6-7, kumar2023distinctlocalizationof pages 4-5) | Moderate. Compartment assignments require isoform-resolved human validation, particularly for A0A2R8YCT7. |
| Biological pathway | Acts as a free-standing trans-editing factor in aminoacyl-tRNA quality control, recycling mischarged tRNAs, preserving the usable tRNA pool, preventing D-amino-acid entry into proteins, and limiting Gly-for-Ala mistranslation. | Direct microbial genetics/biochemistry and conserved mechanistic inference for human (kumar2024whenpaulberg pages 3-4, das2019poisoningafungal pages 11-16, kumar2023distinctlocalizationof pages 1-2) | High for the conserved pathway; the relative contribution in specific human tissues is unresolved. |
| Human phenotypic evidence | A 2009 human study reported that human D-Tyr-tRNA^Tyr deacylase contributes to cellular resistance to D-amino acids, but quantitative details were unavailable in the retrieved material. No established Mendelian disorder or definitive human loss-of-function phenotype was identified in the gathered evidence. | Direct-human study located by DOI but full text unavailable; broader evidence is comparative (das2019poisoningafungal pages 9-11) | Limited to moderate; absence of a phenotype in this search is not evidence that none exists. |
| Applications/clinical status | DTD-family manipulation is being explored in microbial/plant systems for D-amino-acid sensitivity, translation-quality control, and stress tolerance. No validated human DTD1-targeted diagnostic, drug, or clinical trial was identified. | Experimental ortholog studies and recent mechanistic reviews, not human clinical implementation (kumar2024whenpaulberg pages 2-3, kumar2023distinctlocalizationof pages 1-2, kumar2023distinctlocalizationof pages 5-6) | Low for clinical translation; proposed applications remain preclinical and largely non-human. |
Table: Evidence-graded functional annotation of human DTD1, distinguishing direct human observations from conserved-family and ortholog-based inference. Accession, catalytic, localization, phenotypic, and translational limitations are made explicit.
DTD1 is a hydrolase that cleaves the aminoacyl ester linkage at the 3′ end of a mischarged D-aminoacyl-tRNA, releasing free tRNA and the corresponding D-amino acid. The historical name D-Tyr-tRNA^Tyr deacylase understates its breadth: bacterial experiments directly established D-Tyr-, D-Trp-, D-Asp-, and D-Phe-tRNAs as substrates, while genetic results implicated D-Ser-, D-Gln-, and—in yeast—D-Leu-tRNAs. Correct L-aminoacyl-tRNAs are generally rejected. (soutourina2000metabolismofdaminoacyltrnas pages 1-1, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2)
The enzyme therefore does not principally metabolize free D-amino acids. It acts after erroneous aminoacylation and recognizes a tRNA-linked substrate; D-Tyr-adenosine was not hydrolyzed, whereas a D-Tyr-bearing oligonucleotide generated from tRNA remained a substrate, indicating a requirement for RNA/acceptor-end determinants in addition to amino-acid chirality. (ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2)
The defining specificity is broad acceptance of multiple D-aminoacyl moieties coupled to exclusion of their L counterparts—hence the term chiral proofreading. DTD1 complements imperfect stereoselectivity at several earlier translational checkpoints, because aminoacyl-tRNA synthetases, elongation factors, and the ribosome do not provide absolute protection from D-amino-acid mischarging or utilization. Accumulated D-aminoacyl-tRNAs can both sequester the cellular tRNA pool and potentially deliver D-amino acids to proteins. (das2019poisoningafungal pages 9-11, kumar2023distinctlocalizationof pages 1-2)
DTD1 is not expected to hydrolyze every D-aminoacyl-tRNA equally. For example, Thermus thermophilus DTD was inactive against D-Ala-tRNA^Ala in one study, while AlaRS itself edited that substrate. The safest human annotation is therefore “broad D-aminoacyl-tRNA deacylase,” not “universal deacylase for every possible D-aminoacyl-tRNA.” (rybak2019stereospecificitycontrolin pages 9-10, rybak2019stereospecificitycontrolin pages 6-7)
Glycine is achiral and thus cannot be excluded by the enzyme’s L-chiral rejection mechanism. This apparent design problem has a useful outcome: DTD1 removes Gly-tRNA^Ala, generated when alanyl-tRNA synthetase mischarges glycine onto tRNA^Ala, thereby limiting glycine-for-alanine mistranslation. AlaRS error estimates cited in mechanistic work are approximately 1 glycine mischarge per 240 reactions and 1 serine mischarge per 500, compared with a general translation error frequency of roughly 10⁻⁴–10⁻³. (das2019poisoningafungal pages 11-16)
DTD1 must nevertheless avoid destroying correctly charged Gly-tRNA^Gly. In bacterial systems, activity is approximately 1,000-fold higher toward Gly-tRNA^Ala than cognate Gly-tRNA^Gly. The discriminator nucleotide at tRNA position 73 is central: bacterial DTD1 preferentially acts on purine-73 substrates, allowing U73-containing bacterial tRNA^Gly to escape while A73-containing tRNA^Ala is edited. A purine-to-pyrimidine change can alter activity by approximately 100-fold. EF-Tu supplies additional protection, although discriminator-base selection appears especially important. (kumar2024whenpaulberg pages 5-6, das2019poisoningafungal pages 11-16)
Eukaryotic DTD1 evolved the inverse discriminator preference in association with archaeal-derived cytosolic tRNA^Gly carrying A73. This means the exact tRNA context—not merely the attached amino acid—helps determine DTD1 activity. These principles are strongly supported across DTD1 orthologs, but human A0A2R8YCT7-specific kinetic constants were not retrieved. (kumar2024whenpaulberg pages 5-6)
DTD1 has a distinctive DTD-like fold and forms a functional homodimer. The foundational E. coli crystal structure, solved at 1.55 Å, showed that the two subunits assemble into a barrel-like core with extensive interface contacts; the monomer contains 145 residues and the dimer interface covers approximately 1,080 Ų. The active sites lie at the dimer interface. (ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 2-4, ferrifioni2001structureofcrystallinedtyrtrnatyr pages 4-5)
Later mechanistic work identified an invariant, cross-subunit Gly-cisPro motif: a motif from one protomer captures the chiral center of substrate entering the active site formed with the other protomer. This provides the structural basis for rejecting L-aminoacyl-tRNAs while accepting diverse D-aminoacyl-tRNAs. Because glycine lacks a chiral center, it can enter this architecture, explaining DTD1’s Gly-tRNA activity. The solved human DTD1 structure, PDB 2OKV, supports conservation of this family architecture, although the retrieved sources did not provide accession-specific catalytic analysis of that structure. (das2019poisoningafungal pages 11-16, kumar2024whenpaulberg pages 4-5)
DTD1 acts intracellularly where charged tRNAs undergo translation and proofreading. Current evolutionary synthesis states that opisthokonts—fungi and animals—use a single DTD1 colocalized to cytoplasm and mitochondria. Their mitochondrial tRNA^Gly changed from U73 to A73, protecting cognate mitochondrial Gly-tRNA^Gly from the evolved eukaryotic DTD1 specificity. A separate human study cited by the 2023 PNAS paper also reported nuclear localization. Thus, the evidence is most consistent with a multi-compartment intracellular protein rather than an extracellular, membrane, or exclusively cytosolic enzyme. (kumar2024whenpaulberg pages 6-7, kumar2023distinctlocalizationof pages 4-5)
This localization assignment requires caution for A0A2R8YCT7 specifically. The retrieved literature did not establish which human isoform carries mitochondrial targeting information or quantify the cytoplasmic, mitochondrial, and nuclear fractions. Isoform-resolved imaging and fractionation would be needed to assign A0A2R8YCT7 definitively.
Plant results provide a useful contrast, not direct human evidence. Arabidopsis DTD1-GFP was confined to cytosol, or cytosol and nucleus during overexpression, and was absent from organellar proteomic fractions. Forced targeting of catalytically active plant DTD1 to organelles was toxic, whereas a catalytic A103F mutant was not, demonstrating that compartmentation can be essential when DTD1 specificity conflicts with organellar tRNA^Gly discriminator bases. (kumar2023distinctlocalizationof pages 2-4, kumar2023distinctlocalizationof pages 4-5)
DTD1 functions in the aminoacyl-tRNA quality-control arm of protein synthesis, downstream of aminoacyl-tRNA synthetases and alongside other editing systems. Its immediate biochemical roles are:
Microbial knockout evidence supports this pathway assignment. Inactivation of DTD/DTD1 exacerbates D-amino-acid toxicity because D-aminoacyl-tRNAs accumulate. In E. coli, effects were observed for D-Tyr, D-Trp, D-Asp, D-Ser, and D-Gln; among 19 D-amino acids screened in yeast, D-Tyr and D-Leu showed enhanced toxicity in the deacylase-deficient strain. These are ortholog data, not human phenotype measurements, but they directly demonstrate the conserved biochemical logic. (soutourina2000metabolismofdaminoacyltrnas pages 1-1, kumar2024whenpaulberg pages 3-4)
DTD1 is best regarded as a translation-quality-control enzyme, not a conventional signaling molecule. No well-supported receptor, kinase cascade, or transcriptional signaling pathway was identified as its primary function.
A key direct-human paper is Zheng et al., “Human D-Tyr-tRNA(Tyr) deacylase contributes to the resistance of the cell to D-amino acids,” Biochemical Journal 417:85–94, published in 2009, DOI 10.1042/BJ20080617, URL: https://doi.org/10.1042/BJ20080617. Its title and subsequent authoritative citations support a cellular D-amino-acid-resistance role for human DTD1, but the full text was not retrievable through the available evidence tools; exact knockdown, overexpression, substrate, and kinetic values are therefore not reproduced here.
No established Mendelian syndrome, approved biomarker, DTD1-directed therapeutic, or human clinical trial emerged from this search. High-throughput associations—for example, expression changes or protein detection in disease proteomes—should not be interpreted as demonstrating a causal DTD1 disease mechanism without targeted validation.
The major recent advance is a systems-level explanation for how DTD1 substrate specificity co-evolves with cellular compartmentation and tRNA identity.
Kumar et al., PNAS, published June 5, 2023 showed experimentally that plants avoid a lethal DTD1–organellar tRNA^Gly conflict by excluding DTD1 from mitochondria and chloroplasts and using the mechanistically distinct DTD2 in organelles. Arabidopsis DTD1 showed approximately 100-fold preference associated with pyrimidine versus purine discriminator bases, and organelle-targeted active DTD1 was toxic. DOI: 10.1073/pnas.2219292120; URL: https://doi.org/10.1073/pnas.2219292120. (kumar2023distinctlocalizationof pages 1-2, kumar2023distinctlocalizationof pages 2-4, kumar2023distinctlocalizationof pages 4-5)
Kumar and Sankaranarayanan, Nucleic Acids Research, published February 9, 2024 integrated historical and current evidence into a model in which DTD1’s action on achiral glycine is physiologically exploited to proofread Gly-tRNA^Ala, while tRNA discriminator-base evolution prevents destructive editing of Gly-tRNA^Gly. DOI: 10.1093/nar/gkae117; URL: https://doi.org/10.1093/nar/gkae117. (kumar2024whenpaulberg pages 2-3, kumar2024whenpaulberg pages 4-5, kumar2024whenpaulberg pages 5-6)
These papers refine rather than replace the primary annotation: DTD1 is a chiral proofreader whose specificity depends jointly on amino-acid stereochemistry and tRNA identity.
DTD-family biology has potential applications in manipulating D-amino-acid sensitivity, microbial fitness, translation fidelity, and—in plants—stress tolerance and organellar engineering. However, such work remains preclinical and predominantly concerns microbial or plant orthologs. The current evidence does not support targeting human DTD1 therapeutically.
The most defensible expert interpretation is that human DTD1 is a conserved housekeeping proofreader with two coupled functions: broad deacylation of D-aminoacyl-tRNAs and selective clearance of Gly-tRNA^Ala. Evidence for the reaction, fold, dimeric mechanism, and translation-quality-control role is strong. Evidence for exact human substrate kinetics, tissue-specific importance, isoform-resolved localization, and clinical relevance remains limited.
References
(das2019poisoningafungal pages 9-11): K Das. Poisoning a fungal pathogen by d-amino acids. Unknown journal, 2019.
(das2019poisoningafungal pages 11-16): K Das. Poisoning a fungal pathogen by d-amino acids. Unknown journal, 2019.
(soutourina2000metabolismofdaminoacyltrnas pages 1-1): Julie Soutourina, Pierre Plateau, and Sylvain Blanquet. Metabolism of d-aminoacyl-trnas inescherichia coli and saccharomyces cerevisiae cells*. The Journal of Biological Chemistry, 275:32535-32542, Oct 2000. URL: https://doi.org/10.1074/jbc.m005166200, doi:10.1074/jbc.m005166200. This article has 177 citations.
(ferrifioni2001structureofcrystallinedtyrtrnatyr pages 1-2): Maria-Laura Ferri-Fioni, Emmanuelle Schmitt, Julie Soutourina, Pierre Plateau, Yves Mechulam, and Sylvain Blanquet. Structure of crystallined-tyr-trnatyr deacylase. The Journal of Biological Chemistry, 276:47285-47290, Dec 2001. URL: https://doi.org/10.1074/jbc.m106550200, doi:10.1074/jbc.m106550200. This article has 51 citations.
(kumar2024whenpaulberg pages 4-5): Pradeep Kumar and Rajan Sankaranarayanan. When paul berg meets donald crothers: an achiral connection through protein biosynthesis. Nucleic Acids Research, 52:2130-2141, Feb 2024. URL: https://doi.org/10.1093/nar/gkae117, doi:10.1093/nar/gkae117. This article has 1 citations and is from a highest quality peer-reviewed journal.
(kumar2024whenpaulberg pages 5-6): Pradeep Kumar and Rajan Sankaranarayanan. When paul berg meets donald crothers: an achiral connection through protein biosynthesis. Nucleic Acids Research, 52:2130-2141, Feb 2024. URL: https://doi.org/10.1093/nar/gkae117, doi:10.1093/nar/gkae117. This article has 1 citations and is from a highest quality peer-reviewed journal.
(kumar2023distinctlocalizationof pages 2-4): Pradeep Kumar, Kandhalu Sagadevan Dinesh Babu, Avinash Kumar Singh, Dipesh Kumar Singh, Aswan Nalli, Shivapura Jagadeesha Mukul, Ankit Roy, Mohd Mazeed, Bakthisaran Raman, Shobha P. Kruparani, Imran Siddiqi, and Rajan Sankaranarayanan. Distinct localization of chiral proofreaders resolves organellar translation conflict in plants. Proceedings of the National Academy of Sciences of the United States of America, Jun 2023. URL: https://doi.org/10.1073/pnas.2219292120, doi:10.1073/pnas.2219292120. This article has 7 citations and is from a highest quality peer-reviewed journal.
(ferrifioni2001structureofcrystallinedtyrtrnatyr pages 2-4): Maria-Laura Ferri-Fioni, Emmanuelle Schmitt, Julie Soutourina, Pierre Plateau, Yves Mechulam, and Sylvain Blanquet. Structure of crystallined-tyr-trnatyr deacylase. The Journal of Biological Chemistry, 276:47285-47290, Dec 2001. URL: https://doi.org/10.1074/jbc.m106550200, doi:10.1074/jbc.m106550200. This article has 51 citations.
(kumar2024whenpaulberg pages 6-7): Pradeep Kumar and Rajan Sankaranarayanan. When paul berg meets donald crothers: an achiral connection through protein biosynthesis. Nucleic Acids Research, 52:2130-2141, Feb 2024. URL: https://doi.org/10.1093/nar/gkae117, doi:10.1093/nar/gkae117. This article has 1 citations and is from a highest quality peer-reviewed journal.
(kumar2023distinctlocalizationof pages 4-5): Pradeep Kumar, Kandhalu Sagadevan Dinesh Babu, Avinash Kumar Singh, Dipesh Kumar Singh, Aswan Nalli, Shivapura Jagadeesha Mukul, Ankit Roy, Mohd Mazeed, Bakthisaran Raman, Shobha P. Kruparani, Imran Siddiqi, and Rajan Sankaranarayanan. Distinct localization of chiral proofreaders resolves organellar translation conflict in plants. Proceedings of the National Academy of Sciences of the United States of America, Jun 2023. URL: https://doi.org/10.1073/pnas.2219292120, doi:10.1073/pnas.2219292120. This article has 7 citations and is from a highest quality peer-reviewed journal.
(kumar2024whenpaulberg pages 3-4): Pradeep Kumar and Rajan Sankaranarayanan. When paul berg meets donald crothers: an achiral connection through protein biosynthesis. Nucleic Acids Research, 52:2130-2141, Feb 2024. URL: https://doi.org/10.1093/nar/gkae117, doi:10.1093/nar/gkae117. This article has 1 citations and is from a highest quality peer-reviewed journal.
(kumar2023distinctlocalizationof pages 1-2): Pradeep Kumar, Kandhalu Sagadevan Dinesh Babu, Avinash Kumar Singh, Dipesh Kumar Singh, Aswan Nalli, Shivapura Jagadeesha Mukul, Ankit Roy, Mohd Mazeed, Bakthisaran Raman, Shobha P. Kruparani, Imran Siddiqi, and Rajan Sankaranarayanan. Distinct localization of chiral proofreaders resolves organellar translation conflict in plants. Proceedings of the National Academy of Sciences of the United States of America, Jun 2023. URL: https://doi.org/10.1073/pnas.2219292120, doi:10.1073/pnas.2219292120. This article has 7 citations and is from a highest quality peer-reviewed journal.
(kumar2024whenpaulberg pages 2-3): Pradeep Kumar and Rajan Sankaranarayanan. When paul berg meets donald crothers: an achiral connection through protein biosynthesis. Nucleic Acids Research, 52:2130-2141, Feb 2024. URL: https://doi.org/10.1093/nar/gkae117, doi:10.1093/nar/gkae117. This article has 1 citations and is from a highest quality peer-reviewed journal.
(kumar2023distinctlocalizationof pages 5-6): Pradeep Kumar, Kandhalu Sagadevan Dinesh Babu, Avinash Kumar Singh, Dipesh Kumar Singh, Aswan Nalli, Shivapura Jagadeesha Mukul, Ankit Roy, Mohd Mazeed, Bakthisaran Raman, Shobha P. Kruparani, Imran Siddiqi, and Rajan Sankaranarayanan. Distinct localization of chiral proofreaders resolves organellar translation conflict in plants. Proceedings of the National Academy of Sciences of the United States of America, Jun 2023. URL: https://doi.org/10.1073/pnas.2219292120, doi:10.1073/pnas.2219292120. This article has 7 citations and is from a highest quality peer-reviewed journal.
(rybak2019stereospecificitycontrolin pages 9-10): Mariia Yu Rybak, Alexey V Rayevsky, Olga I Gudzera, and Michael A Tukalo. Stereospecificity control in aminoacyl-trna-synthetases: new evidence of d-amino acids activation and editing. Nucleic Acids Research, 47:9777-9788, Sep 2019. URL: https://doi.org/10.1093/nar/gkz756, doi:10.1093/nar/gkz756. This article has 16 citations and is from a highest quality peer-reviewed journal.
(rybak2019stereospecificitycontrolin pages 6-7): Mariia Yu Rybak, Alexey V Rayevsky, Olga I Gudzera, and Michael A Tukalo. Stereospecificity control in aminoacyl-trna-synthetases: new evidence of d-amino acids activation and editing. Nucleic Acids Research, 47:9777-9788, Sep 2019. URL: https://doi.org/10.1093/nar/gkz756, doi:10.1093/nar/gkz756. This article has 16 citations and is from a highest quality peer-reviewed journal.
(ferrifioni2001structureofcrystallinedtyrtrnatyr pages 4-5): Maria-Laura Ferri-Fioni, Emmanuelle Schmitt, Julie Soutourina, Pierre Plateau, Yves Mechulam, and Sylvain Blanquet. Structure of crystallined-tyr-trnatyr deacylase. The Journal of Biological Chemistry, 276:47285-47290, Dec 2001. URL: https://doi.org/10.1074/jbc.m106550200, doi:10.1074/jbc.m106550200. This article has 51 citations.