Evidence map›Paper›PMID 26807759›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology

Intrinsically disordered proteins and biomineralization.

Adele L Boskey, Eduardo Villarreal-Ramirez

Abstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Nucleic Acids as Emerging Regulators of Calcium Phosphate Biomineralization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. ACS omega · 2024
    Article
  19. Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024
    Review
  20. Review

3 more citing papers are in PubMed but not listed here.

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.

Adele L BoskeyMusculoskeletal Integrity Program, Hospital for Special Surgery, New York, NY 10021, USA. Electronic address: Boskeya@HSS.edu.
Eduardo Villarreal-RamirezMusculoskeletal Integrity Program, Hospital for Special Surgery, New York, NY 10021, USA. Electronic address: villarrealer@unam.mx.

Funding

MECHANISM OF HARD TISSUE MINERALIZATIONR01DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1985 to 2010
$4.9M
Noncollagenous Protein Interaction in BiomineralizationR21DE022716 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 2012 to 2013
$471k
MECHANISM OF HARD TISSUE MINERALIZATIONR37DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1987 to 1996
–
NIDCR NIH HHS R01 DE004141NIDCR NIH HHS R21 DE022716NIDCR NIH HHS R37 DE004141
6 · The paper itself

Abstract

In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners. These partners include the component ions of the mineral being deposited, the crystals themselves, the template on which the initial crystals form, and other intrinsically disordered proteins and peptides. This review speculates why intrinsically disordered proteins are so important for biomineralization, providing illustrations from the SIBLING (small integrin binding N-glycosylated) proteins and their peptides. It is concluded that the flexible structure, and the ability of the intrinsically disordered proteins to bind to a multitude of surfaces is crucial, but details on the precise-interactions, energetics and kinetics of binding remain to be determined.

Indexed as

Calcification, PhysiologicAnimalsBinding SitesHumansIntrinsically Disordered ProteinsKineticsModels, MolecularPeptidesProtein BindingProtein Structure, SecondarySurface PropertiesIntrinsically Disordered ProteinsPeptidesBiomineralizationHydroxyapatiteIntrinsically disordered proteinsPhosphophoryn

Identifiers

PMID26807759
PMCPMC4875856

What OpenQuestion holds

Textmetadata
LicenceTDM
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.