Evidence map›Paper›PMID 34272483›Full record

ArticleGenetics in medicine : official journal of the American College of Medical Genetics2021

Caffey disease is associated with distinct arginine to cysteine substitutions in the proα1(I) chain of type I procollagen.

Tibbe Dhooge, Delfien Syx, Trinh Hermanns-Lê, Ingrid Hausser, Geert Mortier, Jonathan Zonana, Sofie Symoens, Peter H Byers, Fransiska Malfait

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In one paragraph

Article in Genetics in medicine : official journal of the American College of Medical Genetics, 2021. 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
0.3field-weighted citation impact, top 39% 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, 3 citations in OpenAlex.

  1. A Novel Splice Variant in theHuman mutation · 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

9 authors at 6 institutions in 3 countries.

Tibbe DhoogeCenter for Medical Genetics, Department of Biomolecular Medicine, Ghent University, Ghent University Hospital, Ghent, Belgium.ORCID 0000-0002-1374-8259
Delfien SyxCenter for Medical Genetics, Department of Biomolecular Medicine, Ghent University, Ghent University Hospital, Ghent, Belgium.
Trinh Hermanns-LêDepartment of Dermatopathology, University Hospital of Sart-Tilman, Liège University, Liège, Belgium.
Ingrid HausserInstitute of Pathology, Heidelberg University Hospital, Heidelberg, Germany.
Geert MortierDepartment of Medical Genetics, Antwerp University Hospital and University of Antwerp, Antwerp, Belgium.
Jonathan ZonanaDepartment of Molecular and Medical Genetics, Oregon Health and Sciences University, Portland, OR, USA.
Sofie SymoensCenter for Medical Genetics, Department of Biomolecular Medicine, Ghent University, Ghent University Hospital, Ghent, Belgium.
Peter H ByersDepartment of Pathology and Division of Medical Genetics, Department of Medicine, University of Washington, Seattle, WA, USA.
Fransiska MalfaitCenter for Medical Genetics, Department of Biomolecular Medicine, Ghent University, Ghent University Hospital, Ghent, Belgium. Fransiska.Malfait@UGent.be.ORCID 0000-0002-5010-0304
Ghent University Hospital · BEHeidelberg University · DEOregon Health & Science University · USUniversity of Antwerp · BEUniversity of Liège · BEUniversity of Washington Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeInfantile Caffey disease is a rare disorder characterized by acute inflammation with subperiosteal new bone formation, associated with fever, pain, and swelling of the overlying soft tissue. Symptoms arise within the first weeks after birth and spontaneously resolve before the age of two years. Many, but not all, affected individuals carry the heterozygous pathogenic COL1A1 variant (c.3040C>T, p.(Arg1014Cys)).

methodsWe sequenced COL1A1 in 28 families with a suspicion of Caffey disease and performed ultrastructural, immunocytochemical, and biochemical collagen studies on patient skin biopsies.

resultsWe identified the p.(Arg1014Cys) variant in 23 families and discovered a novel heterozygous pathogenic COL1A1 variant (c.2752C>T, p.(Arg918Cys)) in five. Both arginine to cysteine substitutions are located in the triple helical domain of the proα1(I) procollagen chain. Dermal fibroblasts (one patient with p.(Arg1014Cys) and one with p.(Arg918Cys)) produced molecules with disulfide-linked proα1(I) chains, which were secreted only with p.(Arg1014Cys). No intracellular accumulation of type I procollagen was detected. The dermis revealed mild ultrastructural abnormalities in collagen fibril diameter and packing.

conclusionThe discovery of this novel pathogenic variant expands the limited spectrum of arginine to cysteine substitutions in type I procollagen. Furthermore, it confirms allelic heterogeneity in Caffey disease and impacts its molecular confirmation.

Indexed as

CysteineHyperostosis, Cortical, CongenitalArginineChild, PreschoolCollagen Type ICollagen Type I, alpha 1 ChainHumansMutationProcollagenArginineCOL1A1 protein, humanCollagen Type ICollagen Type I, alpha 1 ChainCysteineProcollagenProcollagen Type I

Identifiers

PMID34272483
OpenAlexW3182767839

What OpenQuestion holds

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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.