Evidence map›Paper›PMID 16331974›Full record

ArticleBiochemistry2005

Spatially and temporally controlled biomineralization is facilitated by interaction between self-assembled dentin matrix protein 1 and calcium phosphate nuclei in solution.

Gen He, Sivakumar Gajjeraman, David Schultz, David Cookson, Chunlin Qin, William T Butler, Jianjun Hao, Anne George

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 158 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Acidic Osteoid Templates the Plywood Structure of Bone Tissue.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  7. Self-assembling peptide-laden electrospun scaffolds for guided mineralized tissue regeneration.Dental materials : official publication of the Academy of Dental Materials · 2022
    Article
  8. Article
  9. Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Notch expressed by osteocytes plays a critical role in mineralisation.Journal of molecular medicine (Berlin, Germany) · 2018
    Article
  18. Elevated solute transport at sites of diffuse matrix damage in cortical bone: Implications on bone repair.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2018
    Article
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Gen HeDepartment of Oral Biology, University of Illinois, Chicago, Illinois 60612, USA.
Sivakumar Gajjeraman
David Schultz
David Cookson
Chunlin Qin
William T Butler
Jianjun Hao
Anne George
The University of Texas Health Science Center at Houston · USUniversity of Illinois Chicago · US

Funding

CHARACTERIZATION OF DMP1--DENTIN PHOSPHOPROTEINR01DE011657 · NIDCR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GEORGE, ANNE · 1996 to 2018
$5.2M
Characterization of the structure and function of DMP2R01DE013836 · NIDCR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GEORGE, ANNE · 2002 to 2006
$1.3M
Characterization of DMP1 a dentin phosphoproteinR56DE011657 · NIDCR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GEORGE, ANNE · 2008 to 2008
$341k
NIDCR NIH HHS DE 11657NIDCR NIH HHS DE 13836NIDCR NIH HHS R01 DE011657NIDCR NIH HHS R01 DE013836NIDCR NIH HHS R56 DE011657
6 · The paper itself

Abstract

Bone and dentin biomineralization are well-regulated processes mediated by extracellular matrix proteins. It is widely believed that specific matrix proteins in these tissues modulate nucleation of apatite nanoparticles and their growth into micrometer-sized crystals via molecular recognition at the protein-mineral interface. However, this assumption has been supported only circumstantially, and the exact mechanism remains unknown. Dentin matrix protein 1 (DMP1) is an acidic matrix protein, present in the mineralized matrix of bone and dentin. In this study, we have demonstrated using synchrotron small-angle X-ray scattering that DMP1 in solution can undergo oligomerization and temporarily stabilize the newly formed calcium phosphate nanoparticle precursors by sequestering them and preventing their further aggregation and precipitation. The solution structure represents the first low-resolution structural information for DMP1. Atomic force microscopy and transmission electron microscopy studies further confirmed that the nascent calcium phosphate nuclei formed in solution were assembled into ordered protein-mineral complexes with the aid of oligomerized DMP1, recombinant and native. This study reveals a novel mechanism by which DMP1 might facilitate initiation of mineral nucleation at specific sites during bone and dentin mineralization and prevent spontaneous calcium phosphate precipitation in areas in which mineralization is not desirable.

Indexed as

Calcification, PhysiologicProtein ConformationCalcium PhosphatesExtracellular Matrix ProteinsMicroscopy, Atomic ForcePhosphoproteinsRecombinant ProteinsSolutionsSynchrotronsX-Rayscalcium phosphateCalcium PhosphatesExtracellular Matrix ProteinsPhosphoproteinsRecombinant ProteinsSolutions

Identifiers

PMID16331974
PMCPMC2656772
OpenAlexW2032158797

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.