Evidence map›Paper›PMID 25394868›Full record

ReviewNature reviews. Drug discovery2014

SCF ubiquitin ligase-targeted therapies.

Jeffrey R Skaar, Julia K Pagan, Michele Pagano

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Drug discovery, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 222 papers.

0numbers the graph read from it
0cells of the map it votes in
222citing papers in PubMed
13.4field-weighted citation impact, top 1% 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

222 citing papers in PubMed, 340 citations in OpenAlex.

  1. Article
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  6. Review
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  10. Review
  11. The structure and function of FBXW5 in human diseases.Biochemistry and biophysics reports · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Journal of microbiology and biotechnology · 2025
    Article
  16. Ubiquitin proteasome system in cardiac fibrosis.Journal of advanced research · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

162 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

3 authors at 1 institution in 1 country.

Jeffrey R Skaar1] Department of Pathology, Laura and Isaac Perlmutter Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA. [2].
Julia K Pagan1] Department of Pathology, Laura and Isaac Perlmutter Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA. [2].
Michele Pagano1] Department of Pathology, Laura and Isaac Perlmutter Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA. [2] Howard Hughes Medical Institute.
New York University · US

Funding

REGULATION OF THE GI PHASE BY THE UBIQUITIN PATHWAYR01GM057587 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PAGANO, MICHELE · 1998 to 2018
$7.8M
F-box proteins: deregulated cell cycle control and proteolysis in cancerR37CA076584 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PAGANO, MICHELE · 2006 to 2016
$4.7M
Howard Hughes Medical InstituteNCI NIH HHS R37 CA076584NCI NIH HHS R37CA076584 ANDNIGMS NIH HHS R01 GM057587NIGMS NIH HHS R01GM057587
6 · The paper itself

Abstract

The clinical successes of proteasome inhibitors for the treatment of cancer have highlighted the therapeutic potential of targeting this protein degradation system. However, proteasome inhibitors prevent the degradation of numerous proteins, which may cause adverse effects. Increased specificity could be achieved by inhibiting the components of the ubiquitin-proteasome system that target specific subsets of proteins for degradation. F-box proteins are the substrate-targeting subunits of SKP1-CUL1-F-box protein (SCF) ubiquitin ligase complexes. Through the degradation of a plethora of diverse substrates, SCF ubiquitin ligases control a multitude of processes at the cellular and organismal levels, and their dysregulation is implicated in many pathologies. SCF ubiquitin ligases are characterized by their high specificity for substrates, and these ligases therefore represent promising drug targets. However, the potential for therapeutic manipulation of SCF complexes remains an underdeveloped area. This Review explores and discusses potential strategies to target SCF-mediated biological processes to treat human diseases.

Indexed as

AnimalsAntineoplastic AgentsDrug Delivery SystemsF-Box ProteinsHumansNeoplasmsProtein BindingSKP Cullin F-Box Protein LigasesAntineoplastic AgentsF-Box ProteinsSKP Cullin F-Box Protein Ligases

Identifiers

PMID25394868
PMCPMC4410837
OpenAlexW2055092042

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.