Evidence mapPaperPMID 40146632Full record

ReviewThe FEBS journal2025

d-amino acids: new functional insights.

Loredano Pollegioni, Natasa Kustrimovic, Luciano Piubelli, Elena Rosini, Valentina Rabattoni, Silvia Sacchi

Abstract readReview
In one paragraph

Review in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. D-amino acid aminotransferase1 regulates grain chalkiness in rice by modulating endoplasmic reticulum stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. UntargetedTranslational psychiatry · 2026
    Article
  7. 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 · 2026
    Review
  8. Article
  9. Article
  10. MutantMicrobiology spectrum · 2025
    Article
  11. Crystal structure of D-aspartate oxidase from Cryptococcus humicola UJ1.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  12. Review
  13. Article
  14. D-Amino acid analysis in solution using the photochemical properties of protonated adenosine.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Loredano PollegioniThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.ORCID https://orcid.org/0000-0003-1733-7243
Natasa KustrimovicThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.
Luciano PiubelliThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.
Elena RosiniThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.
Valentina RabattoniThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.
Silvia SacchiThe Protein Factory 2.0 Laboratory, Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.ORCID https://orcid.org/0000-0002-2338-2561

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The d-enantiomers of amino acids (d-AAs) were initially considered "unnatural" molecules. They are primarily of microbial origin, present in low amounts, and without biological functions in eukaryotes. However, over the past few decades, sensitive analytical methods have uncovered the presence of both free and peptide-bound d-AAs in higher organisms. During the same period, the discovery of serine racemase-the enzyme that catalyzes the reversible formation of d-serine from l-serine-in rat brains demonstrated that mammals synthesize d-AAs. Notably, the enzymes responsible for d-AAs catabolism were identified almost 90 years ago. Subsequently, free d-AAs such as d-serine, d-aspartate, d-alanine, and d-cysteine have emerged as a novel and important class of signaling molecules in various organs, including the brain and endocrine system. Their involvement in a wide range of neurological disorders has drawn significant scientific interest. We have focused on novel findings, based on the latest analytical techniques, that have reshaped our understanding of physiological processes across diverse organisms, from plants to humans. Beyond neurotransmission, recent studies have highlighted the versatile roles of d-AAs in cancer, inflammation, immune regulation, kidney disease, and diabetes. Moreover, these studies suggest that the levels of d-AAs in blood and urine could serve as early biomarkers for conditions such as Alzheimer's disease, schizophrenia, and chronic kidney disease. Understanding the role of d-AAs in certain pathological states is helping to identify new therapeutic targets, offering promising opportunities for clinical applications in treating various diseases.

Indexed as

Amino AcidsAnimalsBrainHumansNeoplasmsRacemases and EpimerasesSerine RacemaseStereoisomerismAmino AcidsRacemases and EpimerasesSerine Racemasebiomarkersd‐aspartated‐cysteined‐enantiomersd‐serinesignaling

Identifiers

PMID40146632
PMCPMC12414876

What Socratic holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.