Evidence map›Paper›PMID 25285575›Full record

ReviewOrganic & biomolecular chemistry2014

Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure.

Zachary E Reinert, W Seth Horne

Abstract readReview
In one paragraph

Review in Organic & biomolecular chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Heterogeneous H-bonding in a foldamer helix.Journal of the American Chemical Society · 2015
    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

2 authors.

Zachary E ReinertDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
W Seth Horne

Funding

Molecular Mimics of Protein Tertiary Folding from Primary Sequence InformationR01GM107161 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HORNE, WILLIAM SETH · 2013 to 2022
$2.6M
NIGMS NIH HHS R01 GM107161NIGMS NIH HHS R01GM107161
6 · The paper itself

Abstract

A variety of non-biological structural motifs have been incorporated into the backbone of natural protein sequences. In parallel work, diverse unnatural oligomers of de novo design (termed "foldamers") have been developed that fold in defined ways. In this Perspective article, we survey foundational studies on protein backbone engineering, with a focus on alterations made in the context of complex tertiary folds. We go on to summarize recent work illustrating the potential promise of these methods to provide a general framework for the construction of foldamer mimics of protein tertiary structures.

Indexed as

Protein EngineeringProtein FoldingProteinsProtein Structure, TertiaryProteins

Identifiers

PMID25285575
PMCPMC4211622

What OpenQuestion holds

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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.