Evidence map›Paper›PMID 38791277›Full record

ArticleInternational journal of molecular sciences2024

Functional Characterization of a Spectrum of Genetic Variants in a Family with Succinic Semialdehyde Dehydrogenase Deficiency.

Miroslava Didiasova, Samuele Cesaro, Simon Feldhoff, Ilaria Bettin, Nana Tiegel, Vera Füssgen, Mariarita Bertoldi, Ritva Tikkanen

Abstract readCase Reports
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. A crucial active site network of titratable residues guides catalysis and NADProtein science : a publication of the Protein Society · 2025
    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.

Miroslava DidiasovaInstitute of Biochemistry, Medical Faculty, University of Giessen, Friedrichstrasse 24, DE-35390 Giessen, Germany.
Samuele CesaroDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie, 8, 37134 Verona, Italy.ORCID 0009-0005-0922-7652
Simon FeldhoffInstitute of Biochemistry, Medical Faculty, University of Giessen, Friedrichstrasse 24, DE-35390 Giessen, Germany.ORCID 0000-0002-1202-6596
Ilaria BettinDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie, 8, 37134 Verona, Italy.ORCID 0000-0002-9151-9187
Nana TiegelInstitute of Biochemistry, Medical Faculty, University of Giessen, Friedrichstrasse 24, DE-35390 Giessen, Germany.
Vera FüssgenInstitute of Biochemistry, Medical Faculty, University of Giessen, Friedrichstrasse 24, DE-35390 Giessen, Germany.
Mariarita BertoldiDepartment of Neuroscience, Biomedicine and Movement Sciences, University of Verona, Strada Le Grazie, 8, 37134 Verona, Italy.ORCID 0000-0002-2337-9928
Ritva TikkanenInstitute of Biochemistry, Medical Faculty, University of Giessen, Friedrichstrasse 24, DE-35390 Giessen, Germany.ORCID 0000-0002-8393-1825

Funding

De Neu Asociación de Enfermedades de los NeurotrasmisoresSSADH AssociationSSADH-Defizit e.V. 2018-001-Tik and 2019-01-Bertoldi
6 · The paper itself

Abstract

Succinic semialdehyde dehydrogenase (SSADH) is a mitochondrial enzyme involved in the catabolism of the neurotransmitter γ-amino butyric acid. Pathogenic variants in the gene encoding this enzyme cause SSADH deficiency, a developmental disease that manifests as hypotonia, autism, and epilepsy. SSADH deficiency patients usually have family-specific gene variants. Here, we describe a family exhibiting four different SSADH variants: Val90Ala, Cys93Phe, and His180Tyr/Asn255Asp (a double variant). We provide a structural and functional characterization of these variants and show that Cys93Phe and Asn255Asp are pathogenic variants that affect the stability of the SSADH protein. Due to the impairment of the cofactor NAD

Indexed as

Amino Acid Metabolism, Inborn ErrorsDevelopmental DisabilitiesSuccinate-Semialdehyde DehydrogenaseFemaleGenetic VariationHumansMaleMutationPedigreeProtein FoldingSuccinate-Semialdehyde Dehydrogenasealdehyde dehydrogenaseschaperonesGABAmitochondrianeurotransmitter diseasesprotein folding

Identifiers

PMID38791277
PMCPMC11121183

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.