Evidence map›Paper›PMID 21825148›Full record

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

Hierarchical self-assembly of amelogenin and the regulation of biomineralization at the nanoscale.

Ping-An Fang, James F Conway, Henry C Margolis, James P Simmer, Elia Beniash

Open access · bronzeAbstract 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 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 202 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Mineral dissolution by dimeric complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Role of amelogenin phosphorylation in regulating dental enamel formation.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  13. Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

34 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

5 authors at 3 institutions in 1 country.

Ping-An FangDepartment of Oral Biology, Center for Craniofacial Regeneration, McGowan Institute for Regenerative Medicine, University of Pittsburgh, 3501 Terrace Street, PA 15261, USA.
James F Conway
Henry C Margolis
James P Simmer
Elia Beniash
University of Pittsburgh · USHarvard University Press · USUniversity of Michigan–Ann Arbor · US

Funding

Matrix Protein Regulation of Enamel Mineral FormationR01DE016376 · NIDCR · FORSYTH INSTITUTE · PI MARGOLIS, HENRY C · 2005 to 2009
$2.2M
Formation of the Enamel-Dentin InterfaceR01DE016703 · NIDCR · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BENIASH, ELIA · 2006 to 2010
$1.4M
NIDCR NIH HHS R01 DE016376NIDCR NIH HHS R01DE016376NIDCR NIH HHS R01 DE016703NIDCR NIH HHS R01DE016703
6 · The paper itself

Abstract

Enamel is a highly organized hierarchical nanocomposite, which consists of parallel arrays of elongated apatitic crystallites forming an intricate three-dimensional microstructure. Amelogenin, the major extracellular matrix protein of dental enamel, regulates the formation of these crystalline arrays via cooperative interactions with forming mineral phase. Using cryoelectron microscopy, we demonstrate that amelogenin undergoes stepwise hierarchical self-assembly. Furthermore, our results indicate that interactions between amelogenin hydrophilic C-terminal telopeptides are essential for oligomer formation and for subsequent steps of hierarchical self-assembly. We further show that amelogenin assemblies stabilize mineral prenucleation clusters and guide their arrangement into linear chains that organize as parallel arrays. The prenucleation clusters subsequently fuse together to form needle-shaped mineral particles, leading to the formation of bundles of crystallites, the hallmark structural organization of the forming enamel at the nanoscale. These findings provide unique insight into the regulation of biological mineralization by specialized macromolecules and an inspiration for bottom-up strategies for the materials design.

Indexed as

AmelogeninAnimalsCalcification, PhysiologicCalcium PhosphatesCryoelectron MicroscopyImage Processing, Computer-AssistedMiceNanoparticlesAmelogenincalcium phosphateCalcium Phosphates

Identifiers

PMID21825148
PMCPMC3161614
OpenAlexW2019916074

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.