Evidence map›Paper›PMID 38886036›Full record

ArticleMethods in enzymology2024

Thioimidates provide general access to thioamide, amidine, and imidazolone peptide-bond isosteres.

Jacob Byerly-Duke, Emily A O'Brien, Brendan J Wall, Brett VanVeller

Abstract read
In one paragraph

Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Jacob Byerly-DukeDepartment of Chemistry, Iowa State University, Ames, IA, United States.
Emily A O'BrienDepartment of Chemistry, Iowa State University, Ames, IA, United States.
Brendan J WallDepartment of Chemistry, Iowa State University, Ames, IA, United States.
Brett VanVellerDepartment of Chemistry, Iowa State University, Ames, IA, United States. Electronic address: bvv@iastate.edu.

Funding

Peptide backbone modifications to modulate peptide folding and functionR35GM142883 · NIGMS · IOWA STATE UNIVERSITY · PI Brett VanVeller · 2021 to 2026
$2.3M
NIGMS NIH HHS R35 GM142883
6 · The paper itself

Abstract

Thioamides, amidines, and heterocycles are three classes of modifications that can act as peptide-bond isosteres to alter the peptide backbone. Thioimidate protecting groups can address many of the problematic synthetic issues surrounding installation of these groups. Historically, amidines have received little attention in peptides due to limitations in methods to access them. The first robust and general procedure for the introduction of amidines into peptide backbones exploits the utility of thioimidate protecting groups as a means to side-step reactivity that ultimately renders existing methods unsuitable for the installation of amidines along the main-chain of peptides. Further, amidines formed on-resin can be reacted to form (4H)-imidazolone heteorcycles which have recently been shown to act as cis-amide isosteres. General methods for heterocyclic installation capable of geometrically restricting peptide conformation are also under-developed. This work is significant because it describes a generally applicable and divergent approach to access unexplored peptide designs and architectures.

Indexed as

AmidinesImidazolesPeptidesThioamidesAmidinesImidazolesimidazolonePeptidesThioamidesAmidineBackboneImidazolone peptideIsostereSolid-phaseThioamideThioimidate

Identifiers

PMID38886036
PMCPMC11894808

What OpenQuestion holds

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Registered trials

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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.