Evidence map›Paper›PMID 22342723›Full record

ArticleBiochemical and biophysical research communications2012

Post-translational modification of osteopontin: effects on in vitro hydroxyapatite formation and growth.

Adele L Boskey, Brian Christensen, Hayat Taleb, Esben S Sørensen

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

24 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Increased osteopontin contributes to inhibition of bone mineralization in FGF23-deficient mice.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2014
    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

4 authors at 2 institutions in 2 countries.

Adele L BoskeyMusculoskeletal Integrity Program, Hospital for Special Surgery, New York, NY 10021, USA. boskeya@hss.edu
Brian Christensen
Hayat Taleb
Esben S Sørensen
Aarhus University · DKHospital for Special Surgery · US

Funding

MECHANISM OF HARD TISSUE MINERALIZATIONR01DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1985 to 2010
$4.9M
MECHANISM OF HARD TISSUE MINERALIZATIONR37DE004141 · NIDCR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1987 to 1996
–
NIDCR NIH HHS DE04141NIDCR NIH HHS R01 DE004141NIDCR NIH HHS R37 DE004141
6 · The paper itself

Abstract

The manuscript tests the hypothesis that posttranslational modification of the SIBLING family of proteins in general and osteopontin in particular modify the abilities of these proteins to regulate in vitro hydroxyapatite (HA) formation. Osteopontin has diverse effects on hydroxyapatite (HA) mineral crystallite formation and growth depending on the extent of phosphorylation. We hypothesized that different regions of full-length OPN would also have distinct effects on the mineralization process. Thrombin fragmentation of milk OPN (mOPN) was used to test this hypothesis. Three fragments were tested in a de novo HA formation assay; an N-terminal fragment (aa 1-147), a central fragment (aa 148-204) denoted SKK-fragment and a C-terminal fragment (aa 205-262). Compared to intact mOPN the C- and N-terminal fragments behaved comparably, promoting HA formation and growth, but the central SKK-fragment acted as a mineralization inhibitor. In a seeded growth experiment all fragments inhibited mineral proliferation, but the SKK-fragment was the most effective inhibitor. These effects, seen in HA-formation and seeded growth assays in a gelatin gel system and in a pH-stat experiment were lost when the protein or fragments were dephosphorylated. Effects of the fully phosphorylated protein and fragments were also altered in the presence of fibrillar collagen. The diverse effects can be explained in terms of the intrinsically disordered nature of OPN and its fragments which enable them to interact with their multiple partners.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCattleCollagenDurapatiteMilk ProteinsMolecular Sequence DataOsteopontinThrombinCollagenDurapatiteMilk ProteinsOsteopontinThrombin

Identifiers

PMID22342723
PMCPMC3299831
OpenAlexW1979524249

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.