Evidence map›Paper›PMID 36314921›Full record

ArticleMicrobiology spectrum2022

Structural and Functional Analysis of Peptides Derived from KEX2-Processed Repeat Proteins in Agaricomycetes Using Reverse Genetics and Peptidomics.

Eva Vogt, Lukas Sonderegger, Ying-Yu Chen, Tina Segessemann, Markus Künzler

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In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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 at 1 institution in 1 country.

Eva VogtETH Zürich, Department of Biology, Institute of Microbiology, Zürich, Switzerland.ORCID 0000-0002-3761-5266
Lukas SondereggerETH Zürich, Department of Biology, Institute of Microbiology, Zürich, Switzerland.
Ying-Yu ChenETH Zürich, Department of Biology, Institute of Microbiology, Zürich, Switzerland.
Tina SegessemannETH Zürich, Department of Biology, Institute of Microbiology, Zürich, Switzerland.
Markus KünzlerETH Zürich, Department of Biology, Institute of Microbiology, Zürich, Switzerland.ORCID 0000-0003-1275-0629
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bioactivities of fungal peptides are of interest for basic research and therapeutic drug development. Some of these peptides are derived from "KEX2-processed repeat proteins" (KEPs), a recently defined class of precursor proteins that contain multiple peptide cores flanked by KEX2 protease cleavage sites. Genome mining has revealed that KEPs are widespread in the fungal kingdom. Their functions are largely unknown. Here, we present the first in-depth structural and functional analysis of KEPs in a basidiomycete. We bioinformatically identified KEP-encoding genes in the genome of the model agaricomycete Coprinopsis cinerea and established a detection protocol for the derived peptides by overexpressing the C. cinerea KEPs in the yeast Pichia pastoris. Using this protocol, which includes peptide extraction and mass spectrometry with data analysis using the search engine Mascot, we confirmed the presence of several KEP-derived peptides in C. cinerea, as well as in the edible mushrooms Lentinula edodes, Pleurotus ostreatus, and Pleurotus eryngii. While CRISPR-mediated knockout of C. cinerea

Indexed as

AgaricalesFungal ProteinsReverse GeneticsGenome, FungalPeptidesProprotein ConvertasesFungal ProteinsPeptidesProprotein ConvertasesdikaritinsKEX2KEX2-processed repeat proteinsmycologypeptidesRiPPsSTE13

Identifiers

PMID36314921
PMCPMC9769878
OpenAlexW4307775792

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.