Evidence map›Paper›PMID 28196895›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif.

Tomas Wald, Frantisek Spoutil, Adriana Osickova, Michaela Prochazkova, Oldrich Benada, Petr Kasparek, Ladislav Bumba, Ophir D Klein, Radislav Sedlacek, Peter Sebo and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

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  12. Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Review
  13. Role of amelogenin phosphorylation in regulating dental enamel formation.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  14. 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

12 authors.

Tomas WaldInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Frantisek SpoutilLaboratory of Transgenic Models of Diseases, Division of Biogenesis and Biotechnology of Natural Compounds, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Adriana OsickovaInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Michaela ProchazkovaLaboratory of Transgenic Models of Diseases, Division of Biogenesis and Biotechnology of Natural Compounds, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.ORCID 0000-0002-3773-8995
Oldrich BenadaInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Petr KasparekLaboratory of Transgenic Models of Diseases, Division of Biogenesis and Biotechnology of Natural Compounds, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Ladislav BumbaInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Ophir D KleinProgram in Craniofacial Biology, University of California, San Francisco, CA 94143.
Radislav SedlacekLaboratory of Transgenic Models of Diseases, Division of Biogenesis and Biotechnology of Natural Compounds, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Peter SeboInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic.
Jan ProchazkaLaboratory of Transgenic Models of Diseases, Division of Biogenesis and Biotechnology of Natural Compounds, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic; osicka@biomed.cas.cz jan.prochazka@img.cas.cz.
Radim OsickaInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., 142 20 Prague 4, Czech Republic; osicka@biomed.cas.cz jan.prochazka@img.cas.cz.

Funding

Harnessing natural stem cell-based strategies for mammalian dental renewalR35DE026602 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KLEIN, OPHIR D · 2016 to 2023
$8.0M
NIDCR NIH HHS R35 DE026602
6 · The paper itself

Abstract

The formation of mineralized tissues is governed by extracellular matrix proteins that assemble into a 3D organic matrix directing the deposition of hydroxyapatite. Although the formation of bones and dentin depends on the self-assembly of type I collagen via the Gly-X-Y motif, the molecular mechanism by which enamel matrix proteins (EMPs) assemble into the organic matrix remains poorly understood. Here we identified a Y/F-x-x-Y/L/F-x-Y/F motif, evolutionarily conserved from the first tetrapods to man, that is crucial for higher order structure self-assembly of the key intrinsically disordered EMPs, ameloblastin and amelogenin. Using targeted mutations in mice and high-resolution imaging, we show that impairment of ameloblastin self-assembly causes disorganization of the enamel organic matrix and yields enamel with disordered hydroxyapatite crystallites. These findings define a paradigm for the molecular mechanism by which the EMPs self-assemble into supramolecular structures and demonstrate that this process is crucial for organization of the organic matrix and formation of properly structured enamel.

Indexed as

AmelogeninAmino Acid MotifsAmino Acid SequenceAnimalsBiological EvolutionDental EnamelDental Enamel ProteinsDurapatiteExtracellular Matrix ProteinsIntrinsically Disordered ProteinsMaleMiceProtein BindingAmelogeninDental Enamel ProteinsDurapatiteenamel matrix proteinsExtracellular Matrix ProteinsIntrinsically Disordered Proteinsameloblastinamelogeninbiomineralizationenamelintrinsically disordered protein

Identifiers

PMID28196895
PMCPMC5338493

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.