Evidence map›Paper›PMID 28650443›Full record

ArticleNature nanotechnology2017

Sulfated glycopeptide nanostructures for multipotent protein activation.

Sungsoo S Lee, Timmy Fyrner, Feng Chen, Zaida Álvarez, Eduard Sleep, Danielle S Chun, Joseph A Weiner, Ralph W Cook, Ryan D Freshman, Michael S Schallmo and 12 more

Open access · greenAbstract read
In one paragraph

Article in Nature nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 180 citations in OpenAlex.

  1. Article
  2. Review
  3. Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Regenerative Glycopeptide Scaffolds Enhance BMP-4 Activity To Treat Pediatric Glioma.Regenerative engineering and translational medicine · 2025
    Article
  15. Review
  16. Article
  17. A bioactive supramolecular and covalent polymer scaffold for cartilage repair in a sheep model.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Advances in Synthetic Grafts in Spinal Fusion Surgery.International journal of spine surgery · 2023
    Article
  20. Article

12 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

22 authors at 1 institution in 1 country.

Sungsoo S LeeSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Timmy FyrnerSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Feng ChenSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Zaida ÁlvarezSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Eduard SleepSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Danielle S ChunDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Joseph A WeinerDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Ralph W CookDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Ryan D FreshmanDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Michael S SchallmoDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Karina M KatchkoDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Andrew D SchneiderDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Justin T SmithDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Chawon YunDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Gurmit SinghDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Sohaib Z HashmiDepartment of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA.
Mark T McClendonSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Zhilin YuSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Stuart R StockDepartment of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, Illinois 60611, USA.
Wellington K HsuSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Erin L HsuSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Samuel I StuppSimpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA.
Northwestern University · US

Funding

Nanotechnology Strategies for Growth of Bones and TeethR01DE015920 · NIDCR · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SNEAD, MALCOLM L., STUPP, SAMUEL I · 2005 to 2015
$5.8M
NIDCR NIH HHS R01 DE015920
6 · The paper itself

Abstract

Biological systems have evolved to utilize numerous proteins with capacity to bind polysaccharides for the purpose of optimizing their function. A well-known subset of these proteins with binding domains for the highly diverse sulfated polysaccharides are important growth factors involved in biological development and tissue repair. We report here on supramolecular sulfated glycopeptide nanostructures, which display a trisulfated monosaccharide on their surfaces and bind five critical proteins with different polysaccharide-binding domains. Binding does not disrupt the filamentous shape of the nanostructures or their internal β-sheet backbone, but must involve accessible adaptive configurations to interact with such different proteins. The glycopeptide nanostructures amplified signalling of bone morphogenetic protein 2 significantly more than the natural sulfated polysaccharide heparin, and promoted regeneration of bone in the spine with a protein dose that is 100-fold lower than that required in the animal model. These highly bioactive nanostructures may enable many therapies in the future involving proteins.

Indexed as

Bone Morphogenetic Protein 2GlycopeptidesHumansNanostructuresProtein Structure, SecondaryBMP2 protein, humanBone Morphogenetic Protein 2Glycopeptides

Identifiers

PMID28650443
PMCPMC5553550
OpenAlexW2625065858

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.