Evidence map›Paper›PMID 19627527›Full record

ReviewOrthodontics & craniofacial research2009

Enamel matrix proteins; old molecules for new applications.

S P Lyngstadaas, J C Wohlfahrt, S J Brookes, M L Paine, M L Snead, J E Reseland

2 registry-linked trialsOpen access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Orthodontics & craniofacial research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to 2 registered trials, which are not on this map. Cited by 57 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 1 pooled it
9.7field-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.

NCT06041854 nacompletednot on this mapstarted 2022, after this paper: background citation

Comparison Between Allograft and Enamel Matrix Derivative and Allograft in Treatment of Intrabony Defects

TypeinterventionalSponsorMansoura UniversityRan2022 to 2024Enrolled20ConditionsIntrabony Periodontal DefectArmsFreeze-dried bone allograft combined with Enamel Matrix derivative, Freeze-dried bone allograft
NCT07581613 phase1 / phase2not yet recruitingnot on this mapstarted 2026, after this paper: background citation

A Novel Proline-rich Peptide Hydrogel for Periodontal Regeneration: a Multicenter Parallel-arm Randomized Clinical Trial

TypeinterventionalSponsorSiddharth ShanbhagRan2026 to 2030Enrolled40ConditionsPeriodontal Disease, Intrabony Periodontal DefectsArmsHydrogel
3 · Its place in the literature

Who cites it

57 citing papers in PubMed, 1 synthesis or guideline pooled it, 138 citations in OpenAlex.

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  20. Journal of clinical and experimental dentistry · 2022
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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

6 authors at 1 institution in 1 country.

S P LyngstadaasDepartment of Biomaterials, Faculty of Dentistry, University of Oslo, Oslo, Norway. spl@odont.uio.no
J C Wohlfahrt
S J Brookes
M L Paine
M L Snead
J E Reseland
University of Oslo · NO

Funding

ENAMEL MATRIX PROTEIN INTERACTIONR01DE013404 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PAINE, MICHAEL LANSDELL · 2000 to 2010
$3.5M
MOLECULAR MECHANISMS FOR EXTRACELLULAR PH CONTROL DURING AMELOGENESISR01DE019629 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PAINE, MICHAEL LANSDELL · 2009 to 2014
$2.9M
NIDCR NIH HHS R01 DE013404NIDCR NIH HHS R01 DE019629
6 · The paper itself

Abstract

Emdogain (enamel matrix derivative, EMD) is well recognized in periodontology, where it is used as a local adjunct to periodontal surgery to stimulate regeneration of periodontal tissues lost to periodontal disease. The biological effect of EMD is through stimulation of local growth factor secretion and cytokine expression in the treated tissues, inducing a regenerative process that mimics odontogenesis. The major (>95%) component of EMD is Amelogenins (Amel). No other active components have so far been isolated from EMD, and several studies have shown that purified amelogenins can induce the same effect as the complete EMD. Amelogenins comprise a family of highly conserved extracellular matrix proteins derived from one gene. Amelogenin structure and function is evolutionary well conserved, suggesting a profound role in biomineralization and hard tissue formation. A special feature of amelogenins is that under physiological conditions the proteins self-assembles into nanospheres that constitute an extracellular matrix. In the body, this matrix is slowly digested by specific extracellular proteolytic enzymes (matrix metalloproteinase) in a controlled process, releasing bioactive peptides to the surrounding tissues for weeks after application. Based on clinical and experimental observations in periodontology indicating that amelogenins can have a significant positive influence on wound healing, bone formation and root resorption, several new applications for amelogenins have been suggested. New experiments now confirm that amelogenins have potential for being used also in the fields of endodontics, bone regeneration, implantology, traumatology, and wound care.

Indexed as

AmelogeninCalcification, PhysiologicConserved SequenceDental Enamel ProteinsExtracellular Matrix ProteinsHumansMatrix MetalloproteinasesOsteogenesisPeriodontal DiseasesRegenerationRoot ResorptionWound HealingAmelogeninDental Enamel Proteinsenamel matrix proteinsExtracellular Matrix ProteinsMatrix Metalloproteinases

Identifiers

PMID19627527
PMCPMC2825346
OpenAlexW2170610568

What OpenQuestion holds

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Read underepoch 390

Registered trials

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.