Evidence map›Paper›PMID 21576914›Full record

ArticleCells, tissues, organs2011

Potential role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro.

E Le Norcy, S-Y Kwak, F B Wiedemann-Bidlack, E Beniash, Y Yamakoshi, J P Simmer, H C Margolis

Open access · bronzeAbstract read
In one paragraph

Article in Cells, tissues, organs, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  9. Meeting report: a hard look at the state of enamel research.International journal of oral science · 2017
    Article
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  11. Ultrastructure of early amelogenesis in wild-type,Molecular genetics & genomic medicine · 2016
    Article
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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

7 authors at 4 institutions in 1 country.

E Le NorcyDepartment of Biomineralization, The Forsyth Institute, Cambridge, Mass., USA.
S-Y Kwak
F B Wiedemann-Bidlack
E Beniash
Y Yamakoshi
J P Simmer
H C Margolis
Harvard University Press · USUniversity of Michigan–Ann Arbor · USBioMimetic Systems (United States) · USUniversity of Pittsburgh · US

Funding

Matrix Protein Regulation of Enamel Mineral FormationR01DE016376 · NIDCR · FORSYTH INSTITUTE · PI MARGOLIS, HENRY C · 2005 to 2009
$2.2M
NIDCR NIH HHS R01 DE016376NIDCR NIH HHS R01-DE016376
6 · The paper itself

Abstract

N-terminal and C-terminal (CT) domains of amelogenin have been shown to be essential for proper enamel formation. Recent studies have also suggested that although the C-terminus plays an apparent role in protein-mineral interactions, other amelogenin structural domains are involved. The objective was to explore the role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro. Spontaneous mineralization studies were carried out using the phosphorylated (+P) and nonphosphorylated (-P) N-terminus of the leucine-rich amelogenin peptide (LRAP) that lacks the hydrophilic CT domain. Mineralization progress was monitored via changes in solution pH. Mineral phases formed were characterized using TEM, selected area electron diffraction, and FT-IR. In controls, amorphous calcium phosphate was initially formed and subsequently transformed to randomly oriented hydroxyapatite (HA) plate-like crystals. In contrast to the control, LRAP(+P)-CT stabilized ACP formation for >1 day, while LRAP(-P)-CT accelerated the transformation of ACP to HA but had little effect on crystal shape or orientation. In conclusion, the N-terminal domain found in LRAP, as in amelogenins, appears to have the capacity to interact with forming calcium phosphate mineral phases. Results suggest that the N-terminal domain of amelogenin may play a direct role in early stages of enamel formation.

Indexed as

AmelogeninAmino Acid SequenceAnimalsCalcification, PhysiologicCalcium PhosphatesDental Enamel ProteinsHydrogen-Ion ConcentrationMolecular Sequence DataSpectroscopy, Fourier Transform InfraredStructure-Activity RelationshipSus scrofaTime FactorsAmelogeninCalcium PhosphatesDental Enamel Proteinsleucine-rich amelogenin peptide

Identifiers

PMID21576914
PMCPMC3178076
OpenAlexW2023950409

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.