Evidence map›Paper›PMID 37833883›Full record

ArticleInternational journal of molecular sciences2023

The Biological Action and Structural Characterization of Eryngitin 3 and 4, Ribotoxin-like Proteins from

Sara Ragucci, Nicola Landi, Lucía Citores, Rosario Iglesias, Rosita Russo, Angela Clemente, Michele Saviano, Paolo Vincenzo Pedone, Angela Chambery, José Miguel Ferreras and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. 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
0.8field-weighted citation impact, top 24% 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, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
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

11 authors at 3 institutions in 2 countries.

Sara RagucciDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0002-2219-2424
Nicola LandiDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.
Lucía CitoresDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, Spain.ORCID 0000-0003-3784-5042
Rosario IglesiasDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, Spain.ORCID 0000-0002-5021-1733
Rosita RussoDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0002-2235-6302
Angela ClementeDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.
Michele SavianoInstitute of Crystallography, National Research Council, Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0001-5086-2459
Paolo Vincenzo PedoneDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.
Angela ChamberyDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0002-5136-0941
José Miguel FerrerasDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E-47011 Valladolid, Spain.ORCID 0000-0003-4816-5878
Antimo Di MaroDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0002-9595-9665
University of Campania "Luigi Vanvitelli" · ITUniversidad de Valladolid · ESNational Research Council · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribotoxin-like proteins (RL-Ps) are specific ribonucleases found in mushrooms that are able to cleave a single phosphodiester bond located in the sarcin-ricin loop (SRL) of the large rRNA. The cleaved SRL interacts differently with some ribosomal proteins (P-stalk). This action blocks protein synthesis because the damaged ribosomes are unable to interact with elongation factors. Here, the amino acid sequences of eryngitin 3 and 4, RL-Ps isolated from

Indexed as

AgaricalesAscomycotaPleurotusRicinEndoribonucleasesFruiting Bodies, FungalFungal ProteinsRibonucleasesRibosomal ProteinsEndoribonucleasesFungal ProteinsRibonucleasesRibosomal ProteinsRicinamino acid sequencegreen moldking trumpet mushroomMALDI-ToFribotoxin-like proteinssarcin–ricin loop

Identifiers

PMID37833883
PMCPMC10572553
OpenAlexW4386961798

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.