Evidence map›Paper›PMID 37805834›Full record

ArticleProtein science : a publication of the Protein Society2023

On the regulation of human D-aspartate oxidase.

Valentina Rabattoni, Zoraide Motta, Matteo Miceli, Gianluca Molla, Alex Fissore, Salvatore Adinolfi, Loredano Pollegioni, Silvia Sacchi

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Aspartate in the Brain: A Review.Neurochemical research · 2025
    Review
  4. On the regulation of human D-aspartate oxidase.Protein science : a publication of the Protein Society · 2023
    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

8 authors at 2 institutions in 1 country.

Valentina Rabattoni"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.
Zoraide Motta"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.
Matteo Miceli"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.
Gianluca Molla"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.
Alex FissoreDipartimento di Scienza e Tecnologia del Farmaco, Università di Torino, Torino, Italy.
Salvatore AdinolfiDipartimento di Scienza e Tecnologia del Farmaco, Università di Torino, Torino, Italy.
Loredano Pollegioni"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.
Silvia Sacchi"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.ORCID 0000-0002-2338-2561
University of Insubria · ITUniversity of Turin · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human flavoenzyme D-aspartate oxidase (hDASPO) controls the level of D-aspartate in the brain, a molecule acting as an agonist of NMDA receptors and modulator of AMPA and mGlu5 receptors. hDASPO-induced D-aspartate degradation prevents age-dependent deterioration of brain functions and is related to psychiatric disorders such as schizophrenia and autism. Notwithstanding this crucial role, less is known about hDASPO regulation. Here, we report that hDASPO is nitrosylated in vitro, while no evidence of sulfhydration and phosphorylation is apparent: nitrosylation affects the activity of the human flavoenzyme to a limited extent. Furthermore, hDASPO interacts with the primate-specific protein pLG72 (a well-known negative chaperone of D-amino acid oxidase, the enzyme deputed to D-serine degradation in the human brain), yielding a ~114 kDa complex, with a micromolar dissociation constant, promoting the flavoenzyme inactivation. At the cellular level, pLG72 and hDASPO generate a cytosolic complex: the expression of pLG72 negatively affects the hDASPO level by reducing its half-life. We propose that pLG72 binding may represent a protective mechanism aimed at avoiding cytotoxicity due to H

Indexed as

OxidoreductasesSchizophreniaAnimalsCarrier ProteinsD-Aspartate OxidaseD-Aspartic AcidHumansCarrier ProteinsD-Aspartate OxidaseD-Aspartic AcidOxidoreductasesD-aspartateflavooxidaseneurotransmissionpLG72post-translational modificationprotein-protein interaction

Identifiers

PMID37805834
PMCPMC10588558
OpenAlexW4387432964

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.