Evidence map›Paper›PMID 24159389›Full record

ReviewISRN dentistry2013

Dental enamel development: proteinases and their enamel matrix substrates.

John D Bartlett

Open access · diamondAbstract readReview
In one paragraph

Review in ISRN dentistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 1 pooled it
9.8field-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

126 citing papers in PubMed, 1 synthesis or guideline pooled it, 237 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. NovelGenes · 2026
    Article
  7. Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Antisense oligonucleotides-mediated rescue of theJournal of dental sciences · 2026
    Article
  12. JBMR plus · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. A proteomics approach to understand the hypomineralisation of second primary molars (HSPM). In-vitro study.European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry · 2025
    Article
  17. Review
  18. Review
  19. Posteruptive Loss of Proteins in Porcine Enamel.Journal of dental research · 2025
    Article
  20. Article

66 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

1 author.

John D BartlettHarvard School of Dental Medicine & Chair, Department of Mineralized Tissue Biology, The Forsyth Institute, 245 First Street, Cambridge MA 02142, USA.

Funding

Enamelysin Processing Mechanisms in AmelogenesisR01DE016276 · NIDCR · OHIO STATE UNIVERSITY · PI BARTLETT, JOHN D · 2006 to 2014
$4.4M
NIDCR NIH HHS R01 DE016276
6 · The paper itself

Abstract

This review focuses on recent discoveries and delves in detail about what is known about each of the proteins (amelogenin, ameloblastin, and enamelin) and proteinases (matrix metalloproteinase-20 and kallikrein-related peptidase-4) that are secreted into the enamel matrix. After an overview of enamel development, this review focuses on these enamel proteins by describing their nomenclature, tissue expression, functions, proteinase activation, and proteinase substrate specificity. These proteins and their respective null mice and human mutations are also evaluated to shed light on the mechanisms that cause nonsyndromic enamel malformations termed amelogenesis imperfecta. Pertinent controversies are addressed. For example, do any of these proteins have a critical function in addition to their role in enamel development? Does amelogenin initiate crystallite growth, does it inhibit crystallite growth in width and thickness, or does it do neither? Detailed examination of the null mouse literature provides unmistakable clues and/or answers to these questions, and this data is thoroughly analyzed. Striking conclusions from this analysis reveal that widely held paradigms of enamel formation are inadequate. The final section of this review weaves the recent data into a plausible new mechanism by which these enamel matrix proteins support and promote enamel development.

Identifiers

PMID24159389
PMCPMC3789414
OpenAlexW2055985848

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.