Evidence map›Paper›PMID 32442437›Full record

SynthesisPharmacology & therapeutics2020

The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.

G R Tundo, D Sbardella, A M Santoro, A Coletta, F Oddone, G Grasso, D Milardi, P M Lacal, S Marini, R Purrello and 2 more

Open access · greenAbstract readSystematic Review
In one paragraph

Synthesis in Pharmacology & therapeutics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Review
  3. An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026
    Article
  4. Review
  5. Article
  6. [Interferon-α induces disulfidptosis occurrence in human liver cancer cells].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2026
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Investigation of Anticancer Peptides Derived fromMolecules (Basel, Switzerland) · 2025
    Article

6 more citing papers are in PubMed but not listed here.

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

12 authors at 7 institutions in 2 countries.

G R TundoDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Rome, Italy. Electronic address: grazia.tundo@libero.it.
D SbardellaIRCCS-Fondazione Bietti, Rome, Italy.
A M SantoroCNR, Institute of Crystallography, Catania, Italy.
A ColettaDepartment of Chemistry, University of Aarhus, Aarhus, Denmark.
F OddoneIRCCS-Fondazione Bietti, Rome, Italy.
G GrassoDepartment of Chemical Sciences, University of Catania, Catania, Italy.
D MilardiCNR, Institute of Crystallography, Catania, Italy.
P M LacalLaboratory of Molecular Oncology, IDI-IRCCS, Rome, Italy.
S MariniDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Rome, Italy.
R PurrelloDepartment of Chemical Sciences, University of Catania, Catania, Italy.
G GrazianiDepartment of Systems Medicine, University of Rome Tor Vergata, Rome, Italy. Electronic address: graziani@uniroma2.it.
M ColettaDepartment of Clinical Sciences and Translational Medicine, University of Rome Tor Vergata, Rome, Italy. Electronic address: coletta@med.uniroma2.it.
University of Rome Tor Vergata · ITInstitute of Crystallography · ITUniversity of Catania · ITAarhus University · DKFondazione G.B. Bietti · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITIstituto Dermopatico dell'Immacolata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin Proteasome System (UPS) is an adaptable and finely tuned system that sustains proteostasis network under a large variety of physiopathological conditions. Its dysregulation is often associated with the onset and progression of human diseases; hence, UPS modulation has emerged as a promising new avenue for the development of treatments of several relevant pathologies, such as cancer and neurodegeneration. The clinical interest in proteasome inhibition has considerably increased after the FDA approval in 2003 of bortezomib for relapsed/refractory multiple myeloma, which is now used in the front-line setting. Thereafter, two other proteasome inhibitors (carfilzomib and ixazomib), designed to overcome resistance to bortezomib, have been approved for treatment-experienced patients, and a variety of novel inhibitors are currently under preclinical and clinical investigation not only for haematological malignancies but also for solid tumours. However, since UPS collapse leads to toxic misfolded proteins accumulation, proteasome is attracting even more interest as a target for the care of neurodegenerative diseases, which are sustained by UPS impairment. Thus, conceptually, proteasome activation represents an innovative and largely unexplored target for drug development. According to a multidisciplinary approach, spanning from chemistry, biochemistry, molecular biology to pharmacology, this review will summarize the most recent available literature regarding different aspects of proteasome biology, focusing on structure, function and regulation of proteasome in physiological and pathological processes, mostly cancer and neurodegenerative diseases, connecting biochemical features and clinical studies of proteasome targeting drugs.

Indexed as

Cyclin-Dependent KinasesDrug ResistanceE2F4 Transcription FactorHoloenzymesHumansLipid DropletsMolecular ChaperonesMuscle ProteinsNeoplasmsNeurodegenerative DiseasesNF-kappa BProteasome Endopeptidase ComplexProteasome InhibitorsProteostasisTumor Suppressor Protein p53UbiquitinATP dependent 26S proteaseCyclin-Dependent KinasesE2F4 Transcription FactorHoloenzymesMolecular ChaperonesMuscle ProteinsNF-kappa BProteasome Endopeptidase ComplexProteasome Inhibitorsproteasome maturation proteinPSME1 protein, humanTumor Suppressor Protein p53UbiquitinCancerNeurodegenerationProteasomeProteasome inhibitorsSARS-Cov-2

Identifiers

PMID32442437
PMCPMC7236745
OpenAlexW3028262458

What OpenQuestion holds

Textmetadata
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.