Evidence map›Paper›PMID 20491623›Full record

ReviewCurrent protein & peptide science2010

The ubiquitin-proteasome system as a prospective molecular target for cancer treatment and prevention.

Di Chen, Q Ping Dou

Open access · greenAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

62 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The cross talk of ubiquitination and chemotherapy tolerance in colorectal cancer.Journal of cancer research and clinical oncology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Differential expression ofFrontiers in molecular neuroscience · 2023
    Article
  10. F-box only protein 9 and its role in cancer.Molecular biology reports · 2022
    Review
  11. Article
  12. The roles of KLHL family members in human cancers.American journal of cancer research · 2022
    Review
  13. Osteosarcoma in Children: Not Only Chemotherapy.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

2 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

2 authors at 1 institution in 1 country.

Di ChenThe Prevention Program, Barbara Ann Karmanos Cancer Institute, and Departments of Oncology and Pathology, School of Medicine, Wayne State University, Detroit, Michigan, USA.
Q Ping Dou
The Barbara Ann Karmanos Cancer Institute · US

Funding

Roles of polymorphic COMT, tea polyphenols and proteasome in cancer preventionR01CA120009 · NCI · WAYNE STATE UNIVERSITY · PI DOU, QING PING · 2006 to 2010
$1.5M
High resolution spectroscopy for in vivo copper speciation in prostate and breastR21CA139386 · NCI · ILLINOIS INSTITUTE OF TECHNOLOGY · PI BARREA, RAUL ALBERTO · 2009 to 2010
$334k
NCI NIH HHS 1R01CA120009NCI NIH HHS 1R21CA139386-01NCI NIH HHS 3R01CA120009-04S1NCI NIH HHS R01 CA120009NCI NIH HHS R21 CA139386
6 · The paper itself

Abstract

Proteasomes are large multicatalytic proteinase complexes located in the cytosol and the nucleus of eukaryotic cells. The ubiquitin-proteasome system is responsible for the degradation of most intracellular proteins and therefore plays an essential regulatory role in critical cellular processes including cell cycle progression, proliferation, differentiation, angiogenesis and apoptosis. Besides involving in normal cellular functions and homeostasis, the alteration of proteasomal activity contributes to the pathological states of several clinical disorders including inflammation, neurodegeneration and cancer. It has been reported that human cancer cells possess elevated level of proteasome activity and are more sensitive to proteasome inhibitors than normal cells, indicating that the inhibition of the ubiquitin-proteasome system could be used as a novel approach for cancer therapy. In this review we summarize several specific aspects of research for the proteasome complex, including the structure and catalytic activities of the proteasome, properties and mechanisms of action of various proteasome inhibitors, and finally the clinical development of proteasome inhibitors as novel anticancer agents.

Indexed as

Antineoplastic AgentsApoptosisCell ProliferationCysteine Proteinase InhibitorsHumansModels, BiologicalNeoplasmsProteasome Endopeptidase ComplexProteasome InhibitorsSignal TransductionUbiquitinAntineoplastic AgentsCysteine Proteinase InhibitorsProteasome Endopeptidase ComplexProteasome InhibitorsUbiquitin

Identifiers

PMID20491623
PMCPMC3306609
OpenAlexW2156440292

What OpenQuestion holds

Textmetadata
LicenceTDM
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.