Evidence map›Paper›PMID 32582108›Full record

ReviewFrontiers in microbiology2020

A Structural View on the Maturation of Lanthipeptides.

Marcel Lagedroste, Jens Reiners, C Vivien Knospe, Sander H J Smits, Lutz Schmitt

Abstract readReview
In one paragraph

Review in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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  13. Discovery of phosphorylated lantibiotics with proimmune activity that regulate the oral microbiome.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

5 authors.

Marcel LagedrosteInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Jens ReinersInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
C Vivien KnospeInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Sander H J SmitsInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Lutz SchmittInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides, which display diverse bioactivities (e.g., antifungal, antimicrobial, and antiviral). One characteristic of these lanthipeptides is the presence of thioether bonds, which are termed (methyl-) lanthionine rings. These modifications are installed by corresponding modification enzymes in a two-step modality. First, serine and threonine residues are dehydrated followed by a subsequent catalyzed cyclization reaction, in which the dehydrated serine and threonine residues are undergoing a Michael-type addition with cysteine residues. The dedicated enzymes are encoded by one or two genes and the classification of lanthipeptides is pending on this. The modification steps form the basis of distinguishing the different classes of lanthipeptides and furthermore reflect also important mechanistic differences. Here, we will summarize recent insights into the mechanisms and the structures of the participating enzymes, focusing on the two core modification steps - dehydration and cyclization.

Indexed as

biochemistryenzymeslanthionineprotein–protein interactionstructural biology

Identifiers

PMID32582108
PMCPMC7296275

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.