Evidence map›Paper›PMID 33003385›Full record

ArticleInternational journal of molecular sciences2020

Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States.

Anna Maria Santoro, Alessandro D'Urso, Alessandra Cunsolo, Danilo Milardi, Roberto Purrello, Diego Sbardella, Grazia R Tundo, Donatella Diana, Roberto Fattorusso, Antonio Di Dato and 4 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. 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
0.6field-weighted citation impact, top 34% 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

7 citing papers in PubMed, 9 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

14 authors at 10 institutions in 2 countries.

Anna Maria SantoroIstituto di Cristallografia-CNR Sede Secondaria di Catania, Via P. Gaifami 9/18, 95126 Catania, Italy.
Alessandro D'UrsoDipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0002-0255-1792
Alessandra CunsoloDipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Danilo MilardiIstituto di Cristallografia-CNR Sede Secondaria di Catania, Via P. Gaifami 9/18, 95126 Catania, Italy.
Roberto PurrelloDipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Diego SbardellaIRCCS-Fondazione Bietti, 00198 Rome, Italy.
Grazia R TundoIRCCS-Fondazione Bietti, 00198 Rome, Italy.
Donatella DianaIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
Roberto FattorussoDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania "Luigi Vanvitelli" Via Vivaldi 43, 81100 Caserta, Italy.
Antonio Di DatoDipartimento di Farmacia, Università di Napoli "Federico II", Via D. Montesano 49, 80131 Napoli, Italy.
Antonella PaladinoIstituto di Chimica del Riconoscimento Molecolare, CNR, Via M. Bianco 9, 20131 Milano, Italy.
Marco PersicoDipartimento di Farmacia, Università di Napoli "Federico II", Via D. Montesano 49, 80131 Napoli, Italy.
Massimo ColettaDipartimento di Scienze Cliniche e Medicina Traslazionale, Università di Roma Tor Vergata, Via Montpellier 1, 00133 Roma, Italy.
Caterina FattorussoDipartimento di Farmacia, Università di Napoli "Federico II", Via D. Montesano 49, 80131 Napoli, Italy.ORCID 0000-0003-3330-4281
Consorzio Catania Ricerche · ITConsorzio Interuniversitario Nazionale per l'Informatica · ITFondazione G.B. Bietti · ITUniversity of Catania · ITInstitute of Biostructure and Bioimaging · ITInstitute of Chemistry of Molecular Recognition · ITThe University of Texas Health Science Center at San Antonio · USUniversity of Campania "Luigi Vanvitelli" · ITUniversity of Naples Federico II · ITUniversity of Rome Tor Vergata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study provides new evidence that cationic porphyrins may be considered as tunable platforms to interfere with the structural "key code" present on the 20S proteasome α-rings and, by consequence, with its catalytic activity. Here, we describe the functional and conformational effects on the 20S proteasome induced by the cooperative binding of the tri-cationic 5-(phenyl)-10,15,20-(tri

Indexed as

Allosteric RegulationCatalysisCationsCytoplasmHumansKineticsNuclear Magnetic Resonance, BiomolecularPorphyrinsProteasome Endopeptidase ComplexProtein BindingCationsPorphyrinsProteasome Endopeptidase Complex20S proteasomeallosteric modulatorconformational/functional equilibriaintegrated interaction modelkinetic analysismolecular dynamics simulationNMR studies

Identifiers

PMID33003385
PMCPMC7582714
OpenAlexW3090280123

What OpenQuestion holds

Textmetadata
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.