Evidence map›Paper›PMID 21368178›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity.

Clair Baldock, Andres F Oberhauser, Liang Ma, Donna Lammie, Veronique Siegler, Suzanne M Mithieux, Yidong Tu, John Yuen Ho Chow, Farhana Suleman, Marc Malfois and 5 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

75 citing papers in PubMed, 199 citations in OpenAlex.

  1. Review
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  7. Article
  8. Review
  9. Review
  10. Article
  11. Elastic Fibre Proteins in Elastogenesis and Wound Healing.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Observational
  19. Review
  20. Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021
    Review

15 more citing papers are in PubMed but not listed here.

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

15 authors at 8 institutions in 3 countries.

Clair BaldockWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.
Andres F Oberhauser
Liang Ma
Donna Lammie
Veronique Siegler
Suzanne M Mithieux
Yidong Tu
John Yuen Ho Chow
Farhana Suleman
Marc Malfois
Sarah Rogers
Liang Guo
Thomas C Irving
Tim J Wess
Anthony S Weiss
University of Sydney · AUCardiff University · GBIllinois Institute of Technology · USThe University of Texas Medical Branch at Galveston · USDiamond Light Source · GBScience and Technology Facilities Council · GBUniversity of Manchester · GBWellcome Centre for Cell-Matrix Research · GB

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI VOLZ, KARL W · 2001 to 2011
$14.4M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
The Nano-mechanics of Polycystin-1R01DK073394 · NIDDK · UNIVERSITY OF TEXAS MED BR GALVESTON · PI OBERHAUSER, ANDRES F. · 2006 to 2010
$1.2M
NCRR NIH HHS P41 RR008630NIDDK NIH HHS R01 DK073394NIDDK NIH HHS R01DK073394NIGMS NIH HHS P41 GM103622
6 · The paper itself

Abstract

Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.

Indexed as

ElasticityOrgan SpecificityAnimalsEntropyHumansModels, MolecularNeutron DiffractionProtein ConformationScattering, Small AngleSolutionsTropoelastinVertebratesX-Ray DiffractionSolutionsTropoelastin

Identifiers

PMID21368178
PMCPMC3060269
OpenAlexW2121317825

What OpenQuestion holds

Textmetadata
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.