Evidence map›Paper›PMID 33471299›Full record

ReviewMetabolic brain disease2021

A novel de novo heterozygous pathogenic variant in the SDHA gene results in childhood onset bilateral optic atrophy and cognitive impairment.

Yoav Zehavi, Ann Saada, Haneen Jabaly-Habib, Moshe Dessau, Avraham Shaag, Orly Elpeleg, Ronen Spiegel

Abstract readCase ReportsReview
PubMed Publisher
In one paragraph

Review in Metabolic brain disease, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. A Novel Human SDHA-Knockout Cell Line Model for the Functional Analysis of Clinically Relevant SDHA Variants.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  4. Article
  5. Article
  6. Review
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

7 authors at 5 institutions in 1 country.

Yoav ZehaviPediatric Department B' Emek Medical Center, 1834111, Afula, Israel.
Ann SaadaFaculty of Medicine, Hebrew University, Jerusalem, Israel.
Haneen Jabaly-HabibOphthalmology Unit Baruch Padeh Medical Center, Poriya, Israel.
Moshe DessauAzrieli Faculty of Medicine, Bar-Ilan University, Safed, Israel.
Avraham ShaagDepartment of Human Genetics, Hadassah Medical Center, Jerusalem, Israel.
Orly ElpelegFaculty of Medicine, Hebrew University, Jerusalem, Israel.
Ronen SpiegelPediatric Department B' Emek Medical Center, 1834111, Afula, Israel. spiegelr@zahav.net.il.ORCID 0000-0002-0108-4184
Hebrew University of Jerusalem · ILTechnion – Israel Institute of Technology · ILBar-Ilan University · ILHadassah Medical Center · ILPoriya Medical Center · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Isolated defects in the mitochondrial respiratory chain complex II (CII; succinate-ubiquinone oxidoreductase) are extremely rare and mainly result from bi-allelic mutations in one of the nuclear encoded subunits: SDHA, SDHB and SDHD, which comprise CII and the assembly CII factor SDHAF1. We report an adolescent female who presented with global developmental delay, intellectual disability and childhood onset progressive bilateral optic atrophy. Whole exome sequencing of the patient and her unaffected parents identified the novel heterozygous de novo variant c.1984C > T [NM_004168.4] in the SDHA gene. Biochemical assessment of CII in the patient's derived fibroblasts and lymphocytes displayed considerably decreased CII residual activity compared with normal controls, when normalized to the integral mitochondrial enzyme citrate synthase. Protein modeling of the consequent p.Arg662Cys variant [NP-004159.2] suggested that this substitution will compromise the structural integrity of the FAD-binding protein at the C-terminus that will ultimately impair the FAD binding to SDHA, thus decreasing the entire CII activity. Our study emphasizes the role of certain heterozygous SDHA mutations in a distinct clinical phenotype dominated by optic atrophy and neurological impairment. This is the second mutation that has been reported to cause this phenotype. Furthermore, it adds developmental delay and cognitive disability to the expanding spectrum of the disorder. We propose to add SDHA to next generation sequencing gene panels of optic atrophy.

Indexed as

HeterozygoteAdolescentAmino Acid SequenceCognitive DysfunctionElectron Transport Complex IIFemaleGenetic VariationHumansOptic AtrophyProtein Structure, SecondaryElectron Transport Complex IISDHA protein, humanMitochondrial diseaseOptic atrophyRespiratory chain complexSDHA gene

Identifiers

PMID33471299
OpenAlexW3124070872

What OpenQuestion holds

Textmetadata
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.