Evidence map›Paper›PMID 21780757›Full record

ArticleJournal of the American Chemical Society2011

Computational design of a β-peptide that targets transmembrane helices.

Scott J Shandler, Ivan V Korendovych, David T Moore, Kathryn B Smith-Dupont, Craig N Streu, Rustem I Litvinov, Paul C Billings, Feng Gai, Joel S Bennett, William F DeGrado

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Catalytic peptide assemblies.Chemical Society reviews · 2018
    Review
  10. Article
  11. Article
  12. Drugging Membrane Protein Interactions.Annual review of biomedical engineering · 2016
    Review
  13. Selective VIP Receptor Agonists Facilitate Immune Transformation for Dopaminergic Neuroprotection in MPTP-Intoxicated Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. α-Helix mimicry with α/β-peptides.Methods in enzymology · 2013
    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

10 authors at 1 institution in 1 country.

Scott J ShandlerDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Ivan V Korendovych
David T Moore
Kathryn B Smith-Dupont
Craig N Streu
Rustem I Litvinov
Paul C Billings
Feng Gai
Joel S Bennett
William F DeGrado
University of Pennsylvania · US

Funding

Subcellular Mechanisms pf Platelet ActivationP01HL040387 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI ABRAMS, CHARLES S. · 1988 to 2018
$35.5M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
BIOORGANIC MODELS FOR TRANSMEMBRANE PROTEINSR01GM060610 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2000 to 2009
$2.2M
NHLBI NIH HHS HL40387NHLBI NIH HHS P01 HL040387NIGMS NIH HHS GM54616NIGMS NIH HHS GM60610NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM060610NIGMS NIH HHS R37 GM054616NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

The design of β-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of β-peptides was designed to stably insert in TM orientations in phospholipid bilayers. Their secondary structures and orientation in the phospholipid bilayer was characterized using biophysical methods. Computational methods were then devised to design a β-peptide that targeted a TM helix of the integrin α(IIb)β(3). The designed peptide (β-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.

Indexed as

Amino Acid SequenceComputer-Aided DesignHumansModels, MolecularMolecular Sequence DataPeptidesPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein Structure, SecondaryPeptidesPlatelet Glycoprotein GPIIb-IIIa Complex

Identifiers

PMID21780757
PMCPMC3155016
OpenAlexW1965028293

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.