Evidence map›Paper›PMID 24909436›Full record

ArticleOrganic & biomolecular chemistry2014

Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation.

George A Lengyel, Zachary E Reinert, Brian D Griffith, W Seth Horne

Abstract readComparative Study
In one paragraph

Article 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  5. Article
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  9. Article
  10. Article
  11. Article
  12. Article
  13. Engineering β-sheets employingChemical science · 2016
    Article
  14. Article
  15. 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

4 authors.

George A LengyelDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
Zachary E Reinert
Brian D Griffith
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

The mimicry of protein tertiary structure by oligomers with unnatural backbones is a significant contemporary research challenge. Among common elements of secondary structure found in natural proteins, sheets have proven the most difficult to address. Here, we report the systematic comparison of different strategies for peptide backbone modification in β-sheets with the goal of identifying the best method for replacing a multi-stranded sheet in a protein tertiary fold. The most effective sheet modifications examined led to native-like tertiary folding behavior with a thermodynamic folded stability comparable to the prototype protein on which the modified backbones are based.

Indexed as

Amino Acid SequenceCircular DichroismMagnetic Resonance SpectroscopyMethylationMolecular Sequence DataPeptidesProtein FoldingProteinsProtein Structure, SecondaryThermodynamicsPeptidesProteins

Identifiers

PMID24909436
PMCPMC4129447

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.