Evidence map›Paper›PMID 25048248›Full record

ArticleJournal of dental research2014

Matching 4.7-Å XRD spacing in amelogenin nanoribbons and enamel matrix.

B Sanii, O Martinez-Avila, C Simpliciano, R N Zuckermann, S Habelitz

Open access · greenAbstract read
In one paragraph

Article in Journal of dental research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Amyloid-like amelogenin nanoribbons template mineralization via a low-energy interface of ion binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Protein nanoribbons template enamel mineralization.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. 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 3 institutions in 1 country.

B SaniiLawrence Berkeley National Laboratory, Molecular Foundry, Berkeley, CA 94720, USA Keck Science Department, Claremont McKenna, Scripps and Pitzer Colleges, Claremont, CA 91711, USA.
O Martinez-AvilaUniversity of California, Department of Preventive and Restorative Dental Sciences, San Francisco, CA 94143, USA.
C SimplicianoUniversity of California, Department of Preventive and Restorative Dental Sciences, San Francisco, CA 94143, USA.
R N ZuckermannLawrence Berkeley National Laboratory, Molecular Foundry, Berkeley, CA 94720, USA.
S HabelitzUniversity of California, Department of Preventive and Restorative Dental Sciences, San Francisco, CA 94143, USA stefan.habelitz@ucsf.edu.
University of California, San Francisco · USLawrence Berkeley National Laboratory · USPitzer College · US

Funding

A New Concept of Amelogenin-guided Mineralization in EnamelR21DE023422 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HABELITZ, STEFAN FRIEDRICH · 2013 to 2014
$433k
NIDCR NIH HHS R21 DE023422PHS HHS R21-023422
6 · The paper itself

Abstract

The recent discovery of conditions that induce nanoribbon structures of amelogenin protein in vitro raises questions about their role in enamel formation. Nanoribbons of recombinant human full-length amelogenin (rH174) are about 17 nm wide and self-align into parallel bundles; thus, they could act as templates for crystallization of nanofibrous apatite comprising dental enamel. Here we analyzed the secondary structures of nanoribbon amelogenin by x-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR) and tested if the structural motif matches previous data on the organic matrix of enamel. XRD analysis showed that a peak corresponding to 4.7 Å is present in nanoribbons of amelogenin. In addition, FTIR analysis showed that amelogenin in the form of nanoribbons was comprised of β-sheets by up to 75%, while amelogenin nanospheres had predominantly random-coil structure. The observation of a 4.7-Å XRD spacing confirms the presence of β-sheets and illustrates structural parallels between the in vitro assemblies and structural motifs in developing enamel.

Indexed as

AmelogeninAmino Acid MotifsCalcium ChlorideDental EnamelHumansHydrogen-Ion ConcentrationMicroscopy, Atomic ForceNanoparticlesNanospheresPhosphatesPotassium ChloridePotassium CompoundsRecombinant ProteinsSpectroscopy, Fourier Transform InfraredX-Ray DiffractionAmelogeninCalcium ChloridePhosphatesPotassium ChloridePotassium Compoundspotassium phosphateRecombinant ProteinsdevelopmentFourier transform infrared spectroscopypowder diffractionsecondary protein structureself-assemblystructure

Identifiers

PMID25048248
PMCPMC4213250
OpenAlexW2164685818

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.