Evidence map›Paper›PMID 29946030›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Molecular model of human tropoelastin and implications of associated mutations.

Anna Tarakanova, Giselle C Yeo, Clair Baldock, Anthony S Weiss, Markus J Buehler

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Functions of prolyl hydroxylation in elastin.The Journal of biological chemistry · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024
    Review
  7. Review
  8. Review
  9. Elastic Fibre Proteins in Elastogenesis and Wound Healing.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021
    Review
  19. Tunable Protein Hydrogels: Present State and Emerging Development.Advances in biochemical engineering/biotechnology · 2021
    Article
  20. 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

5 authors.

Anna TarakanovaLaboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 01239.
Giselle C YeoSchool of Life and Environmental Sciences, The University of Sydney, Sydney, NSW 2006, Australia.
Clair BaldockWellcome Trust Centre for Cell-Matrix Research, Division of Cell Matrix Biology and Regenerative Medicine, School of Biological Sciences, Manchester Academic Health Science Centre, The University of Manchester, Manchester M13 9PT, United Kingdom.
Anthony S WeissSchool of Life and Environmental Sciences, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-8106-4836
Markus J BuehlerLaboratory for Atomistic and Molecular Mechanics, Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA 01239; mbuehler@mit.edu.

Funding

Models to Predict Protein Biomaterial PerformanceU01EB014976 · NIBIB · TUFTS UNIVERSITY MEDFORD · PI BUEHLER, MARKUS J., KAPLAN, DAVID L. · 2012 to 2020
$5.2M
Biotechnology and Biological Sciences Research Council BB/N015398/1NIBIB NIH HHS U01 EB014976Wellcome TrustWellcome Trust 088785/Z/09/Z
6 · The paper itself

Abstract

Protein folding poses unique challenges for large, disordered proteins due to the low resolution of structural data accessible in experiment and on the basis of short time scales and limited sampling attainable in computation. Such molecules are uniquely suited to accelerated-sampling molecular dynamics algorithms due to a flat-energy landscape. We apply these methods to report here the folded structure in water from a fully extended chain of tropoelastin, a 698-amino acid molecular precursor to elastic fibers that confer elasticity and recoil to tissues, finding good agreement with experimental data. We then study a series of artificial and disease-related mutations, yielding molecular mechanisms to explain structural differences and variation in hierarchical assembly observed in experiment. The present model builds a framework for studying assembly and disease and yields critical insight into molecular mechanisms behind these processes. These results suggest that proteins with disordered regions are suitable candidates for characterization by this approach.

Indexed as

Molecular Dynamics SimulationMutationHumansTropoelastinTropoelastindisordered proteinelastic fibermolecular dynamicsstructural proteintropoelastin

Identifiers

PMID29946030
PMCPMC6048532

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.