Evidence map›Paper›PMID 38534381›Full record

ReviewCells2024

Protein Stability Regulation in Osteosarcoma: The Ubiquitin-like Modifications and Glycosylation as Mediators of Tumor Growth and as Targets for Therapy.

Jacopo Di Gregorio, Laura Di Giuseppe, Sara Terreri, Michela Rossi, Giulia Battafarano, Olivia Pagliarosi, Vincenzo Flati, Andrea Del Fattore

Abstract readReview
In one paragraph

Review in Cells, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. 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

8 authors.

Jacopo Di GregorioDepartment of Biotechnological and Applied Clinical Sciences, University of L'Aquila, 67100 L'Aquila, Italy.ORCID 0000-0001-8865-2967
Laura Di GiuseppeDepartment of Clinical, Internal, Anaesthesiological and Cardiovascular Sciences, Sapienza University, 00185 Rome, Italy.
Sara TerreriBone Physiopathology Research Unit, Translational Pediatrics and Clinical Genetics Research Division, Bambino Gesù Children's Hospital, IRCCS, 00146 Rome, Italy.
Michela RossiBone Physiopathology Research Unit, Translational Pediatrics and Clinical Genetics Research Division, Bambino Gesù Children's Hospital, IRCCS, 00146 Rome, Italy.ORCID 0000-0002-6844-6469
Giulia BattafaranoBone Physiopathology Research Unit, Translational Pediatrics and Clinical Genetics Research Division, Bambino Gesù Children's Hospital, IRCCS, 00146 Rome, Italy.ORCID 0000-0002-9297-5184
Olivia PagliarosiBone Physiopathology Research Unit, Translational Pediatrics and Clinical Genetics Research Division, Bambino Gesù Children's Hospital, IRCCS, 00146 Rome, Italy.
Vincenzo FlatiDepartment of Biotechnological and Applied Clinical Sciences, University of L'Aquila, 67100 L'Aquila, Italy.ORCID 0000-0003-1014-297X
Andrea Del FattoreBone Physiopathology Research Unit, Translational Pediatrics and Clinical Genetics Research Division, Bambino Gesù Children's Hospital, IRCCS, 00146 Rome, Italy.ORCID 0000-0003-3848-412X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of new therapeutic targets and the development of innovative therapeutic approaches are the most important challenges for osteosarcoma treatment. In fact, despite being relatively rare, recurrence and metastatic potential, particularly to the lungs, make osteosarcoma a deadly form of cancer. In fact, although current treatments, including surgery and chemotherapy, have improved survival rates, the disease's recurrence and metastasis are still unresolved complications. Insights for analyzing the still unclear molecular mechanisms of osteosarcoma development, and for finding new therapeutic targets, may arise from the study of post-translational protein modifications. Indeed, they can influence and alter protein structure, stability and function, and cellular interactions. Among all the post-translational modifications, ubiquitin-like modifications (ubiquitination, deubiquitination, SUMOylation, and NEDDylation), as well as glycosylation, are the most important for regulating protein stability, which is frequently altered in cancers including osteosarcoma. This review summarizes the relevance of ubiquitin-like modifications and glycosylation in osteosarcoma progression, providing an overview of protein stability regulation, as well as highlighting the molecular mediators of these processes in the context of osteosarcoma and their possible targeting for much-needed novel therapy.

Indexed as

Bone NeoplasmsOsteosarcomaGlycosylationHumansProtein StabilityUbiquitinUbiquitincancerglycosylationNEDDylationosteosarcomapost-translational modificationsSUMOylationubiquitination

Identifiers

PMID38534381
PMCPMC10969184

What OpenQuestion holds

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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.