Evidence map›Paper›PMID 9566980›Full record

ArticleThe Journal of cell biology1998

Calcium determines the supramolecular organization of fibrillin-rich microfibrils.

T J Wess, P P Purslow, M J Sherratt, J Ashworth, C A Shuttleworth, C M Kielty

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Fibulin-4 exerts a dual role in LTBP-4L-mediated matrix assembly and function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Tissue elasticity and the ageing elastic fibre.Age (Dordrecht, Netherlands) · 2009
    Review
  8. Review
  9. Article
  10. Article
  11. Fibrillin: from microfibril assembly to biomechanical function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002
    Review
  12. Fibrillin-rich microfibrils: elastic biopolymers of the extracellular matrix.Journal of muscle research and cell motility · 2002
    Review
  13. Article
  14. 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 2 institutions in 1 country.

T J WessDepartment of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA, United Kingdom. tjw3@stir.ac.uk
P P Purslow
M J Sherratt
J Ashworth
C A Shuttleworth
C M Kielty
University of Manchester · GBUniversity of Stirling · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microfibrils are ubiquitous fibrillin-rich polymers that are thought to provide long-range elasticity to extracellular matrices, including the zonular filaments of mammalian eyes. X-ray diffraction of hydrated bovine zonular filaments demonstrated meridional diffraction peaks indexing on a fundamental axial periodicity (D) of approximately 56 nm. A Ca2+-induced reversible change in the intensities of the meridional Bragg peaks indicated that supramolecular rearrangements occurred in response to altered concentrations of free Ca2+. In the presence of Ca2+, the dominant diffracting subspecies were microfibrils aligned in an axial 0.33-D stagger. The removal of Ca2+ caused an enhanced regularity in molecular spacing of individual microfibrils, and the contribution from microfibrils not involved in staggered arrays became more dominant. Scanning transmission electron microscopy of isolated microfibrils revealed that Ca2+ removal or addition caused significant, reversible changes in microfibril mass distribution and periodicity. These results were consistent with evidence from x-ray diffraction. Simulated meridional x-ray diffraction profiles and analyses of isolated Ca2+-containing, staggered microfibrillar arrays were used to interpret the effects of Ca2+. These observations highlight the importance of Ca2+ to microfibrils and microfibrillar arrays in vivo.

Indexed as

AnimalsBiopolymersCalciumCattleCiliary BodyComputer SimulationExtracellular MatrixExtracellular Matrix ProteinsFibrillinsMicrofilament ProteinsModels, MolecularX-Ray DiffractionBiopolymersCalciumExtracellular Matrix ProteinsFibrillinsMicrofilament Proteins

Identifiers

PMID9566980
PMCPMC2132742
OpenAlexW2134604924

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.