Evidence map›Paper›PMID 23563189›Full record

ArticleJournal of structural biology2013

Localization and quantitative co-localization of enamelin with amelogenin.

Victoria Gallon, Lisha Chen, Xiudong Yang, Janet Moradian-Oldak

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The phosphorylation of serineMatrix biology : journal of the International Society for Matrix Biology · 2022
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  19. Review
  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 at 1 institution in 1 country.

Victoria GallonCenter for Craniofacial Molecular Biology, University of Southern California, Herman Ostrow School of Dentistry, Los Angeles, CA 90033, USA.
Lisha Chen
Xiudong Yang
Janet Moradian-Oldak
University of Southern California · US

Funding

MATRIX-BASED MINERAL (MBM) ENAMEL BIOMIMETICSR01DE013414 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Janet Oldak · 2001 to 2026
$8.6M
INTRINSICALLY DISORDERED PROTEINS IN BIOMINERALIZATIONR01DE020099 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI OLDAK, JANET · 2009 to 2013
$2.0M
NIDCR NIH HHS DE-013414NIDCR NIH HHS DE-020099NIDCR NIH HHS R01 DE013414NIDCR NIH HHS R01 DE020099
6 · The paper itself

Abstract

Enamelin and amelogenin are vital proteins in enamel formation. The cooperative function of these two proteins controls crystal nucleation and morphology in vitro. We quantitatively analyzed the co-localization between enamelin and amelogenin by confocal microscopy and using two antibodies, one raised against a sequence in the porcine 32 kDa enamelin region and the other raised against full-length recombinant mouse amelogenin. We further investigated the interaction of the porcine 32 kDa enamelin and recombinant amelogenin using immuno-gold labeling. This study reports the quantitative co-localization results for postnatal days 1-8 mandibular mouse molars. We show that amelogenin and enamelin are secreted into the extracellular matrix on the cuspal slopes of the molars at day 1 and that secretion continues to at least day 8. Quantitative co-localization analysis (QCA) was performed in several different configurations using large (45 μm height, 33 μm width) and small (7 μm diameter) regions of interest to elucidate any patterns. Co-localization patterns in day 8 samples revealed that enamelin and amelogenin co-localize near the secretory face of the ameloblasts and appear to be secreted approximately in a 1:1 ratio. The degree of co-localization decreases as the enamel matures, both along the secretory face of ameloblasts and throughout the entire thickness of the enamel. Immuno-reactivity against enamelin is concentrated along the secretory face of ameloblasts, supporting the theory that this protein together with amelogenin is intimately involved in mineral induction at the beginning of enamel formation.

Indexed as

AmeloblastsAmelogeninAnimalsAntibodiesDental Enamel ProteinsExtracellular MatrixMiceMicroscopy, ConfocalMolarSwineAmelogeninAntibodiesDental Enamel ProteinstuftelinAmelogeninConfocal microscopyEnamelinProtein–protein interactionQuantitative co-localization analysis

Identifiers

PMID23563189
PMCPMC3737400
OpenAlexW1991942955

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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.