Evidence map›Paper›PMID 32937944›Full record

ReviewMolecules (Basel, Switzerland)2020

Identification of Key Functional Motifs of Native Amelogenin Protein for Dental Enamel Remineralisation.

Shama S M Dissanayake, Manikandan Ekambaram, Kai Chun Li, Paul W R Harris, Margaret A Brimble

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  13. Women in Bioorganic Chemistry.Molecules (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Advanced materials for enamel remineralization.Frontiers in bioengineering and biotechnology · 2022
    Review
  16. Review
  17. A N-Terminus Domain Determines Amelogenin's Stability to Guide the Development of Mouse Enamel Matrix.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2021
    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

5 authors at 2 institutions in 1 country.

Shama S M DissanayakeSchool of Chemical Sciences, 23 Symonds St, The University of Auckland, Auckland 1142, New Zealand.
Manikandan EkambaramPaediatric Dentistry, Biomaterials, Faculty of Dentistry, The University of Otago, Dunedin 9016, New Zealand.
Kai Chun LiPaediatric Dentistry, Biomaterials, Faculty of Dentistry, The University of Otago, Dunedin 9016, New Zealand.
Paul W R HarrisSchool of Chemical Sciences, 23 Symonds St, The University of Auckland, Auckland 1142, New Zealand.
Margaret A BrimbleSchool of Chemical Sciences, 23 Symonds St, The University of Auckland, Auckland 1142, New Zealand.ORCID 0000-0002-7086-4096
University of Auckland · NZUniversity of Otago · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dental caries or tooth decay is a preventable and multifactorial disease that affects billions of people globally and is a particular concern in younger populations. This decay arises from acid demineralisation of tooth enamel resulting in mineral loss from the subsurface. The remineralisation of early enamel carious lesions could prevent the cavitation of teeth. The enamel protein amelogenin constitutes 90% of the total enamel matrix protein in teeth and plays a key role in the biomineralisation of tooth enamel. The physiological importance of amelogenin has led to the investigation of the possible development of amelogenin-derived biomimetics against dental caries. We herein review the literature on amelogenin, its primary and secondary structure, comparison to related species, and its' in vivo processing to bioactive peptide fragments. The key structural motifs of amelogenin that enable enamel remineralisation are discussed. The presence of several motifs in the amelogenin structure (such as polyproline, N- and C-terminal domains and C-terminal orientation) were shown to play a critical role in the formation of particle shape during remineralization. Understanding the function/structure relationships of amelogenin can aid in the rational design of synthetic polypeptides for biomineralisation, halting enamel loss and leading to improved therapies for tooth decay.

Indexed as

AmelogeninAmino Acid MotifsAnimalsBiomimeticsCattleDental CariesDental EnamelDurapatiteHumansLeucineMicePeptidesProtein DomainsSwineTyrosineAmelogeninDurapatiteLeucinePeptidesTyrosineamelogeninamelogenin-derived peptidesdental cariesenamel remineralisationhydroxyapatiteleucine-rich amelogenin peptidestyrosine-rich amelogenin peptides

Identifiers

PMID32937944
PMCPMC7571260
OpenAlexW3085194795

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.