Evidence map›Paper›PMID 24130249›Full record

ArticleJournal of dental research2013

Mineral association changes the secondary structure and dynamics of murine amelogenin.

J X Lu, Y S Xu, G W Buchko, W J Shaw

Abstract read
In one paragraph

Article in Journal of dental research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
–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

20 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Amelogenin-Derived Peptides in Bone Regeneration: A Systematic Review.International journal of molecular sciences · 2021
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. The energetic basis for hydroxyapatite mineralization by amelogenin variants provides insights into the origin ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Meeting report: a hard look at the state of enamel research.International journal of oral science · 2017
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Amelogenin and Enamel Biomimetics.Journal of materials chemistry. B
    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

4 authors.

J X LuPacific Northwest National Laboratory, Richland, WA 99352, USA.
Y S Xu
G W Buchko
W J Shaw

Funding

Structural, spatial, and temporal features guiding amelogenins transformation of calcium phosphate into enamelR01DE015347 · NIDCR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SHAW, WENDY J · 2005 to 2025
$8.2M
NIDCR NIH HHS DE-015347NIDCR NIH HHS R01 DE015347
6 · The paper itself

Abstract

Amelogenin is one of the key protein constituents responsible for the exquisite organization of the calcium phosphate crystals in enamel. Amelogenin forms into nanospheres in solution, while its association with hydroxyapatite is also essential to enamel development. Structural information of full-length amelogenin in either of these physiologically important forms has the potential to provide mechanistic information; however, these data are limited because of the difficulty of determining the structure of large protein complexes and proteins bound to surfaces. To obtain structural insights into amelogenin during these early stages of enamel development, we used a lysine-specific (13)C-, (15)N-labeled sample of murine amelogenin to provide insight into the structure of the hydroxyapatite (HAP)-binding domains of the protein. A combination of one-and two-dimensional solid-state NMR experiments was used to obtain molecular-level insights into the secondary structure and dynamics of full-length amelogenin within a nanosphere-gel and on the surface of HAP. Regions of amelogenin that appear to be primarily random coil in the nanosphere-gel adopt a β-strand structure and are less mobile with HAP binding, indicative of a structural switch upon binding that may be important in the role of amelogenin in enamel development.

Indexed as

AmelogeninAnimalsCarbon IsotopesDurapatiteGelsLysineMiceNanospheresNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, SecondaryAmelogeninCarbon IsotopesDurapatiteGelsLysineNitrogen Isotopesamelogeninbiomineralizationenamelnanospheresolid-state NMRstructural characterization

Identifiers

PMID24130249
PMCPMC3797538

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.