Evidence map›Paper›PMID 21311558›Full record

ArticleEMBO reports2011

Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region.

Sadaf-Ahmahni Hussain, Federico Carafoli, Erhard Hohenester

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

41 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Laminin N-terminus α31 expression during development is lethal and causes widespread tissue-specific defects in a transgenic mouse model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  8. Review
  9. Organization of the laminin polymer node.Matrix biology : journal of the International Society for Matrix Biology · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural biology of laminins.Essays in biochemistry · 2019
    Review
  17. A scar-like lesion is apparent in basement membrane after wound repair in vivo.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Article
  18. Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  19. Developing defined substrates for stem cell culture and differentiation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  20. Chimeric protein identification of dystrophic, Pierson and other laminin polymerization residues.Matrix biology : journal of the International Society for Matrix Biology · 2018
    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

3 authors at 1 institution in 1 country.

Sadaf-Ahmahni HussainDepartment of Life Sciences, Biophysics Section, Blackett Laboratory, Prince Consort Road, Imperial College London, London SW7 2AZ, UK.
Federico Carafoli
Erhard Hohenester
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D524840/1Wellcome TrustWellcome Trust 083942
6 · The paper itself

Abstract

The polymerization of laminin into a cell-associated network--a key step in basement membrane assembly--is mediated by the laminin amino-terminal (LN) domains at the tips of the three short arms of the laminin αβγ-heterotrimer. The crystal structure of a laminin α5LN-LE1-2 fragment shows that the LN domain is a β-jelly roll with several elaborate insertions that is attached like a flower head to the stalk-like laminin-type epidermal growth factor-like tandem. A surface loop that is strictly conserved in the LN domains of all α-short arms is required for stable ternary association with the β- and γ-short arms in the laminin network.

Indexed as

Protein Structure, QuaternaryAmino Acid SequenceAnimalsBasement MembraneBinding SitesLamininMiceModels, MolecularMolecular Sequence DataPolymerizationProtein BindingProtein MultimerizationProtein Structure, TertiaryLamininlaminin 1

Identifiers

PMID21311558
PMCPMC3059903
OpenAlexW2097652618

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.