Evidence map›Paper›PMID 35789182›Full record

ArticleScientific reports2022

Pathogenicity of missense variants affecting the collagen IV α5 carboxy non-collagenous domain in X-linked Alport syndrome.

Joel T Gibson, Omid Sadeghi-Alavijeh, Daniel P Gale, Hansjörg Rothe, Genomics England Research Consortium, Judy Savige

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 55% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. An Alport variant illuminates the bioactivity of the collagen IVbioRxiv : the preprint server for biology · 2026
    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 at 6 institutions in 2 countries.

Joel T GibsonDepartment of Medicine (Melbourne Health and Northern Health), The University of Melbourne, Parkville, VIC, 3050, Australia.
Omid Sadeghi-AlavijehDepartment of Renal Medicine, University College London, London, UK.
Daniel P GaleDepartment of Renal Medicine, University College London, London, UK.
Hansjörg RotheCentre for Nephrology and Metabolic Disorders, 02943, Weisswasser, Germany.
Genomics England Research Consortium
Judy SavigeDepartment of Medicine (Melbourne Health and Northern Health), The University of Melbourne, Parkville, VIC, 3050, Australia. jasavige@unimelb.edu.au.
Genomics England · GBQueen Mary University of London · GBWilliam Harvey Research Institute · GBUniversity of Melbourne · AUMelbourne Health · AUUniversity College London · GB

Funding

Cancer Research UKDepartment of HealthMedical Research Council MR/S021329/1Wellcome Trust
6 · The paper itself

Abstract

X-linked Alport syndrome is a genetic kidney disease caused by pathogenic COL4A5 variants, but little is known of the consequences of missense variants affecting the NC1 domain of the corresponding collagen IV α5 chain. This study examined these variants in a normal (gnomAD) and other databases (LOVD, Clin Var and 100,000 Genomes Project) to determine their pathogenicity and clinical significance. Males with Cys substitutions in the collagen IV α5 NC1 domain reported in LOVD (n = 25) were examined for typical Alport features, including age at kidney failure. All NC1 variants in LOVD (n = 86) were then assessed for structural damage using an online computational tool, Missense3D. Variants in the ClinVar, gnomAD and 100,000 Genomes Project databases were also examined for structural effects. Predicted damage associated with NC1 substitutions was then correlated with the level of conservation of the affected residues. Cys substitutions in males were associated with the typical features of X-linked Alport syndrome, with a median age at kidney failure of 31 years. NC1 substitutions predicted to cause structural damage were overrepresented in LOVD (p < 0.001), and those affecting Cys residues or 'buried' Gly residues were more common than expected (both p < 0.001). Most NC1 substitutions in gnomAD (88%) were predicted to be structurally-neutral. Substitutions affecting conserved residues resulted in more structural damage than those affecting non-conserved residues (p < 0.001). Many pathogenic missense variants affecting the collagen IV α5 NC1 domain have their effect through molecular structural damage and 3D modelling is a useful tool in their assessment.

Indexed as

Mutation, MissenseNephritis, HereditaryCollagen Type IVHumansMaleRenal InsufficiencyCOL4A5 protein, humanCollagen Type IV

Identifiers

PMID35789182
PMCPMC9253329
OpenAlexW4283789323

What OpenQuestion holds

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LicenceCC BY
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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.