Evidence map›Paper›PMID 26186340›Full record

ArticlePloS one2015

Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution.

Diego Sbardella, Grazia Raffaella Tundo, Francesca Sciandra, Manuela Bozzi, Magda Gioia, Chiara Ciaccio, Umberto Tarantino, Andrea Brancaccio, Massimo Coletta, Stefano Marini

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.1field-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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.

  1. Pooled it
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  16. Targeting Insulin-Degrading Enzyme to Treat Type 2 Diabetes Mellitus.Trends in endocrinology and metabolism: TEM · 2016
    Review
  17. Novel Platinum(II) compounds modulate insulin-degrading enzyme activity and induce cell death in neuroblastoma cells.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
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 3 institutions in 2 countries.

Diego SbardellaDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Grazia Raffaella TundoDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Francesca SciandraIstituto di Chimica del Riconoscimento Molecolare (CNR), Università Cattolica del Sacro Cuore, Largo F. Vito 1, I-00168, Rome, Italy.
Manuela BozziIstituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Largo F. Vito 1, I-00168, Rome, Italy.
Magda GioiaDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Chiara CiaccioDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Umberto TarantinoDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Andrea BrancaccioIstituto di Chimica del Riconoscimento Molecolare (CNR), Università Cattolica del Sacro Cuore, Largo F. Vito 1, I-00168, Rome, Italy; School of Biochemistry, Medical Sciences Building, University Walk, Bristol, B581TD, United Kingdom.
Massimo ColettaDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
Stefano MariniDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Via Montpellier 1, I-00133, Rome, Italy; Center for Space Biomedicine, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy.
University of Rome Tor Vergata · ITUniversità Cattolica del Sacro Cuore · ITUniversity of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.

Indexed as

Blotting, WesternCell Line, TumorComplex MixturesEndoplasmic ReticulumGene SilencingHeat-Shock ResponseHumansInsulysinNeuroblastomaProteasome Endopeptidase ComplexProtein BindingStress, PhysiologicalSubcellular FractionsTime FactorsATP dependent 26S proteaseComplex MixturesInsulysinProteasome Endopeptidase Complex

Identifiers

PMID26186340
PMCPMC4506093
OpenAlexW1413753939

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.