Evidence map›Paper›PMID 38341867›Full record

ArticleOrganic letters2024

Thioimidate Solutions to Thioamide Problems during Thionopeptide Deprotection.

Jacob Byerly-Duke, Brett VanVeller

Abstract read
In one paragraph

Article in Organic letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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.

Jacob Byerly-DukeDepartment of Chemistry, Iowa State University, Ames, Iowa 50011, United States.
Brett VanVellerDepartment of Chemistry, Iowa State University, Ames, Iowa 50011, United States.ORCID 0000-0002-3792-0308

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 have structural and chemical similarity to peptide bonds, offering valuable insights when probing peptide backbone interactions, but are prone to side reactions during solid-phase peptide synthesis (SPPS). Thioimidates have been demonstrated to be effective protecting groups for thioamides during peptide elongation. We further demonstrate how thioimidates can assist thioamides through the most yield-crippling step of thionopeptide deprotection, allowing for the first isolation of an important benchmark α-helical peptide that had previously eluded synthesis and isolation.

Identifiers

PMID38341867
PMCPMC11031844

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.