Evidence map›Paper›PMID 30082319›Full record

ArticleThe Journal of biological chemistry2018

Domains with highest heparan sulfate-binding affinity reside at opposite ends in BMP2/4

Paul C Billings, Evan Yang, Christina Mundy, Maurizio Pacifici

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Regenerative Glycopeptide Scaffolds Enhance BMP-4 Activity To Treat Pediatric Glioma.Regenerative engineering and translational medicine · 2025
    Article
  2. Article
  3. Article
  4. Osteochondroma formation is independent of heparanase expression as revealed in a mouse model of hereditary multiple exostoses.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2022
    Article
  5. Collagen-Based Osteogenic Nanocoating of Microrough Titanium Surfaces.International journal of molecular sciences · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Heparanase and the hallmarks of cancer.Journal of translational medicine · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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 1 institution in 1 country.

Paul C BillingsFrom the Translational Research Program in Pediatric Orthopaedics, Division of Orthopaedic Surgery, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104 BillingsP@email.chop.edu.
Evan YangFrom the Translational Research Program in Pediatric Orthopaedics, Division of Orthopaedic Surgery, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Christina MundyFrom the Translational Research Program in Pediatric Orthopaedics, Division of Orthopaedic Surgery, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.ORCID 0000-0003-3328-5965
Maurizio PacificiFrom the Translational Research Program in Pediatric Orthopaedics, Division of Orthopaedic Surgery, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Children's Hospital of Philadelphia · US

Funding

Pathogenic Mechanisms in Hereditary Multiple Exostoses SyndromeR01AR061758 · NIAMS · CHILDREN'S HOSP OF PHILADELPHIA · PI Maurizio Pacifici · 2011 to 2026
$6.3M
NIAMS NIH HHS R01 AR061758
6 · The paper itself

Abstract

Signaling proteins, including bone morphogenetic proteins (BMPs), specifically interact with heparan sulfate (HS). These interactions regulate protein distribution and function and are largely mediated by domains rich in basic amino acids. The N-terminal region of BMP2 and BMP4 contains one such domain with a typical Cardin-Weintraub (CW) motif, but it is unclear whether the same occurs in BMP5, BMP6, and BMP7 that constitute a separate evolutionary subgroup. Peptides spanning the N-terminal domain of BMP2/4 interacted with substrate-bound HS with nanomolar affinity, but peptides spanning BMP5/6/7 N-terminal domain did not. We re-examined the entire BMP5/6/7 sequences and identified a novel CW-like motif at their C terminus. Peptides spanning this domain displayed high-affinity HS binding, but corresponding BMP2/4 C-terminal peptides did not, likely because of acidic or noncharged residue substitutions. Peptides pre-assembled into NeutrAvidin tetramers displayed the same exact binding selectivity of respective monomers but bound HS with greater affinity. Tests of possible peptide biological activities showed that the HS-binding N-terminal BMP2/4 and C-terminal BMP5/6/7 peptides stimulated chondrogenesis

Indexed as

Amino Acid SequenceAnimalsBinding, CompetitiveBinding SitesBone Morphogenetic ProteinsCartilageCell DifferentiationHeparan SulfateHumansProtein BindingSequence Homology, Amino AcidSignal TransductionBone Morphogenetic ProteinsHeparan Sulfatebone morphogenetic protein (BMP)Cardein-Weintraub motifcartilage biologycell signalingchondrogenesisheparan sulfateheparin-binding domainheparin-binding proteinhyaluronic acid

Identifiers

PMID30082319
PMCPMC6139562
OpenAlexW2887580371

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.