Evidence map›Paper›PMID 31695102›Full record

ArticleScientific reports2019

Structural analysis of human SEPHS2 protein, a selenocysteine machinery component, over-expressed in triple negative breast cancer.

Carmine Nunziata, Andrea Polo, Angela Sorice, Francesca Capone, Marina Accardo, Eliana Guerriero, Federica Zito Marino, Michele Orditura, Alfredo Budillon, Susan Costantini

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05817227 (Selenoproteins as Prognostic Markers and Therapeutic Targets in Breast Cancer.), which is not on this map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 15% 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.

NCT05817227 recruitingnot on this mapstarted 2022, after this paper: background citation

Selenoproteins as Prognostic Markers and Therapeutic Targets in Breast Cancer.

TypeobservationalSponsorNational Cancer Institute, NaplesRan2022 to 2027Enrolled300ConditionsBreast Cancer
3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 46 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

10 authors at 2 institutions in 1 country.

Carmine NunziataExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia.
Andrea PoloExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia.
Angela SoriceExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia.
Francesca CaponeExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia.
Marina AccardoDepartment of Mental and Physical Health and Preventive Medicine, Università degli Studi della Campania "Luigi Vanvitelli", Pathology Unit, Napoli, Italia.
Eliana GuerrieroIstituto Tecnico Industriale (ITIS) "Guido Dorso", Avellino, Italia.
Federica Zito MarinoDepartment of Mental and Physical Health and Preventive Medicine, Università degli Studi della Campania "Luigi Vanvitelli", Pathology Unit, Napoli, Italia.
Michele OrdituraDivision of Medical Oncology, Department of Precision Medicine, School of Medicine, Università degli Studi della Campania "Luigi Vanvitelli", Napoli, Italia.
Alfredo BudillonExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia. a.budillon@istitutotumori.na.it.
Susan CostantiniExperimental Pharmacology Unit, Laboratori di Mercogliano, Istituto Nazionale Tumori - IRCCS - Fondazione G. Pascale, Napoli, Italia. s.costantini@istitutotumori.na.it.
Istituto Nazionale Tumori IRCCS "Fondazione G. Pascale" · ITUniversity of Campania "Luigi Vanvitelli" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selenophosphate synthetase 2 (SEPHS2) synthesizes selenide and ATP into selenophosphate, the selenium donor for selenocysteine (Sec), which is cotranslationally incorporated into selenoproteins. The action and regulatory mechanisms of SEPHS2 as well as its role in carcinogenesis (especially breast cancer) remain ambiguous and need further clarification. Therefore, lacking an experimentally determined structure for SEPHS2, we first analyzed the physicochemical properties of its sequence, modeled its three-dimensional structure and studied its conformational behavior to identify the key residues (named HUB nodes) responsible for protein stability and to clarify the molecular mechanisms by which it induced its function. Bioinformatics analysis evidenced higher amplification frequencies of SEPHS2 in breast cancer than in other cancer types. Therefore, because triple negative breast cancer (TNBC) is biologically the most aggressive breast cancer subtype and its treatment represents a challenge due to the absence of well-defined molecular targets, we evaluated SEPHS2 expression in two TNBC cell lines and patient samples. We demonstrated mRNA and protein overexpression to be correlated with aggressiveness and malignant tumor grade, suggesting that this protein could potentially be considered a prognostic marker and/or therapeutic target for TNBC.

Indexed as

Amino Acid SequenceFemaleGene AmplificationHumansPhosphotransferasesProtein StabilitySelenocysteineTriple Negative Breast NeoplasmsPhosphotransferasesSelenocysteineselenophosphate synthetase 2, human

Identifiers

PMID31695102
PMCPMC6834634
OpenAlexW2983058656

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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.