Evidence map›Paper›PMID 33837859›Full record

ArticleAmino acids2021

Thiazole-amino acids: influence of thiazole ring on conformational properties of amino acid residues.

Monika Staś, Małgorzata A Broda, Dawid Siodłak

Open access · hybridAbstract read
In one paragraph

Article in Amino acids, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Azole γ-Peptides Helix Switching via Heterocycle Substitutions.Angewandte Chemie (International ed. in English) · 2026
    Article
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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

3 authors at 2 institutions in 2 countries.

Monika StaśFaculty of Chemistry, University of Opole, 45-052, Opole, Poland. plgmonika691@gmail.com.ORCID http://orcid.org/0000-0002-7854-0141
Małgorzata A BrodaFaculty of Chemistry, University of Opole, 45-052, Opole, Poland.ORCID http://orcid.org/0000-0002-4092-3593
Dawid SiodłakFaculty of Chemistry, University of Opole, 45-052, Opole, Poland. dsiodlak@uni.opole.pl.ORCID http://orcid.org/0000-0002-1686-5215
University of Opole · PLOpole University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modified thiazole-amino acid (Xaa-Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole-amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation; which is stabilised mainly by N-H⋯N

Indexed as

Amino AcidsHydrogen BondingMolecular ConformationPeptidesThiazolesAmino AcidsPeptidesThiazolesConformational analysisDFTHydrogen bondNon-standard amino acidsRamachandran mapThiazole

Identifiers

PMID33837859
PMCPMC8128816
OpenAlexW3147144636

What OpenQuestion holds

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LicenceCC BY
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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.