Evidence map›Paper›PMID 22548447›Full record

ArticleJournal of the American Chemical Society2012

Extending foldamer design beyond α-helix mimicry: α/β-peptide inhibitors of vascular endothelial growth factor signaling.

Holly S Haase, Kimberly J Peterson-Kaufman, Sheeny K Lan Levengood, James W Checco, William L Murphy, Samuel H Gellman

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.6field-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

43 citing papers in PubMed, 99 citations in OpenAlex.

  1. Automation of the Azapeptide Submonomer Synthesis Method.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

6 authors at 1 institution in 1 country.

Holly S HaaseDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Kimberly J Peterson-Kaufman
Sheeny K Lan Levengood
James W Checco
William L Murphy
Samuel H Gellman
University of Wisconsin–Madison · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Protein Recognition by Peptidic FoldamersR01GM056414 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 1997 to 2023
$6.5M
Biomaterials for local regulation of growth factor signalingR01HL093282 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MURPHY, WILLIAM L. · 2009 to 2018
$3.3M
NHLBI NIH HHS HL093282NHLBI NIH HHS R01 HL093282NIGMS NIH HHS GM056414NIGMS NIH HHS R01 GM056414NIGMS NIH HHS T32 GM008349NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

Diverse strategies have been explored to mimic the surface displayed by an α-helical segment of a protein, with the goal of creating inhibitors of helix-mediated protein-protein interactions. Many recognition surfaces on proteins, however, are topologically more complex and less regular than a single α-helix. We describe efforts to develop peptidic foldamers that bind to the irregular receptor-recognition surface of vascular endothelial growth factor (VEGF). Our approach begins with a 19-residue α-peptide previously reported by Fairbrother et al. (Biochemistry 1998, 37, 17754) to bind to this surface on VEGF. Systematic evaluation of α→β replacements throughout this 19-mer sequence enabled us to identify homologues that contain up to ~30% β residues, retain significant affinity for VEGF, and display substantial resistance to proteolysis. These α/β-peptides can block VEGF-stimulated proliferation of human umbilical vein endothelial cells.

Indexed as

Amino Acid SequenceCell ProliferationHumansHuman Umbilical Vein Endothelial CellsModels, MolecularMolecular Sequence DataPeptidesProtein FoldingProtein Structure, SecondarySignal TransductionVascular Endothelial Growth Factor APeptidesVascular Endothelial Growth Factor A

Identifiers

PMID22548447
PMCPMC3551614
OpenAlexW2077525557

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.