Evidence map›Paper›PMID 22715982›Full record

ArticleJournal of the American Chemical Society2012

Nucleation effects in peptide foldamers.

Anupam Patgiri, Stephen T Joy, Paramjit S Arora

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Helix Propensities of Amino Acid Residues via Thioester Exchange.Journal of the American Chemical Society · 2017
    Article
  9. ChemistrySelect · 2016
    Review
  10. Article
  11. Review
  12. An optimal hydrogen-bond surrogate for α-helices.Chemical communications (Cambridge, England) · 2016
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Effects of side chains in helix nucleation differ from helix propagation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Review
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

3 authors.

Anupam PatgiriDepartment of Chemistry, New York University, New York, New York 10003, USA.
Stephen T Joy
Paramjit S Arora

Funding

Biomolecular Recognition with Artificial Alpha-HelicesR01GM073943 · NIGMS · NEW YORK UNIVERSITY · PI ARORA, PARAMJIT S · 2005 to 2018
$4.4M
NIGMS NIH HHS GM073943NIGMS NIH HHS R01 GM073943
6 · The paper itself

Abstract

Oligomers composed of β(3)-amino acid residues and a mixture of α- and β(3)-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β(3)-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of "αααβ" repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.

Indexed as

Circular DichroismDeuteriumHydrogenMagnetic Resonance SpectroscopyPeptidesProtein FoldingDeuteriumHydrogenPeptides

Identifiers

PMID22715982
PMCPMC3399945

What OpenQuestion holds

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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.