Evidence map›Paper›PMID 30302137›Full record

ReviewThe Japanese dental science review2018

Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein.

Yasuo Yamakoshi, James P Simmer

Open access · goldAbstract readReview
In one paragraph

Review in The Japanese dental science review, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 22 citations in OpenAlex.

  1. Beyond the diagnosis: UnravelingThe Japanese dental science review · 2026
    Review
  2. Article
  3. Article
  4. Translated MutantJournal of personalized medicine · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. 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

2 authors at 2 institutions in 2 countries.

Yasuo YamakoshiDepartment of Biochemistry and Molecular Biology, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan.
James P SimmerDepartment of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1210 Eisenhower Place, Ann Arbor, 48103, USA.
Tsurumi University · JPUniversity of Michigan · US

Funding

Structural and Functional Analysis of Dentin ProteinsR01DE018020 · NIDCR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SIMMER, JAMES P · 2008 to 2012
$1.7M
NIDCR NIH HHS R01 DE018020
6 · The paper itself

Abstract

Dentin sialophosphoprotein (DSPP) plays an important role in the formation of dentin. Understanding its structure and function would provide important insights into the regulation of dentin mineralization. For the past 15 years, we have been studying DSPP-derived proteins isolated from pig dentin. Porcine DSPP is synthesized and secreted by odontoblasts and processed into three proteins, i.e., dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP), by bone morphogenetic protein 1 and matrix metalloproteinase-20 and -2. DSP is a proteoglycan that forms covalent dimers, DGP is a phosphorylated glycoprotein, and DPP is a highly phosphorylated intrinsically disordered protein with genetic polymorphisms. Furthermore, DPP is not detected in dental pulp. This is possibly due to the existence of two mRNA variants of the

Indexed as

DentinDentin sialophosphoproteinGeneProteaseProteoglycanTooth

Identifiers

PMID30302137
PMCPMC6175968
OpenAlexW2888133144

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.