Evidence map›Paper›PMID 23001006›Full record

ArticleNature structural & molecular biology2012

Structural basis of fibrillar collagen trimerization and related genetic disorders.

Jean-Marie Bourhis, Natacha Mariano, Yuguang Zhao, Karl Harlos, Jean-Yves Exposito, E Yvonne Jones, Catherine Moali, Nushin Aghajari, David J S Hulmes

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Next-Generation Sequencing and Variant Analysis of Fibrillar (Pro)Collagens.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Review
  7. Review
  8. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. The Novel Association of a Single Nucleotide Variant in theCurrent issues in molecular biology · 2025
    Article
  13. An outcome-defining role for the triple-helical domain in regulating collagen-I assembly.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Review
  15. Article
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  17. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Jean-Marie BourhisFormation de Recherche en Evolution 3310, Institut de Biologie et Chimie des Protéines, Centre National de la Recherche Scientifique, Université Lyon 1, Lyon, France.
Natacha Mariano
Yuguang Zhao
Karl Harlos
Jean-Yves Exposito
E Yvonne Jones
Catherine Moali
Nushin Aghajari
David J S Hulmes
Institut de Biologie et de Chimie des Protéines · FRUniversity of Oxford · GBCentre for Human Genetics · GBCentre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

Cancer Research UK A5261Medical Research Council G09 000 84Medical Research Council G0900084Medical Research Council G9900061Medical Research Council G9900061(69203)Wellcome Trust 090532
6 · The paper itself

Abstract

The C propeptides of fibrillar procollagens have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. Mutations in C propeptides are associated with several, often lethal, genetic disorders affecting bone, cartilage, blood vessels and skin. Here we report the crystal structure of a C-propeptide domain from human procollagen III. It reveals an exquisite structural mechanism of chain recognition during intracellular trimerization of the procollagen molecule. It also gives insights into why some types of collagen consist of three identical polypeptide chains, whereas others do not. Finally, the data show striking correlations between the sites of numerous disease-related mutations in different C-propeptide domains and the degree of phenotype severity. The results have broad implications for understanding genetic disorders of connective tissues and designing new therapeutic strategies.

Indexed as

Amino Acid SequenceCollagen DiseasesCollagen Type IIICrystallography, X-RayHumansModels, MolecularMolecular Sequence DataMutationMutation, MissenseProtein MultimerizationProtein Structure, TertiaryCollagen Type III

Identifiers

PMID23001006
PMCPMC3465578
OpenAlexW2072250059

What OpenQuestion holds

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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.