Evidence map›Paper›PMID 21103004›Full record

ArticleGenes & cancer2010

Small RING Finger Proteins RBX1 and RBX2 of SCF E3 Ubiquitin Ligases: The Role in Cancer and as Cancer Targets.

Dongping Wei, Yi Sun

Open access · bronzeAbstract read
In one paragraph

Article in Genes & cancer, 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
1.9field-weighted citation impact, top 15% 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, 103 citations in OpenAlex.

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  9. The Cullin-RING Ligase Family in Immune Regulation.Advances in experimental medicine and biology · 2024
    Review
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  11. FBXW7 in breast cancer: mechanism of action and therapeutic potential.Journal of experimental & clinical cancer research : CR · 2023
    Review
  12. Review
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  19. Review
  20. Review

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 2 institutions in 1 country.

Dongping WeiDivision of Radiation and Cancer Biology, Department of Radiation Oncology, University of Michigan Comprehensive Cancer Center, Ann Arbor, MI, USA.
Yi Sun
Radiation Oncology Associates · USUniversity of Michigan–Ann Arbor · US

Funding

SAG E3 ubiquitin ligase in regulation of transformation and carcinogenesisR01CA118762 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2006 to 2015
$2.6M
SAG E3 ubiquitin ligase in angiogenesis & carcinogenesisR01CA111554 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2005 to 2010
$1.8M
NCI NIH HHS R01 CA111554NCI NIH HHS R01 CA118762
6 · The paper itself

Abstract

The SCF (Skp1-cullin-F-box proteins), also known as CRL (cullin-based RING ligase), is the largest family of E3 ubiquitin ligases that mediate approximately 20% ubiquitinated protein substrates for 26S proteasome degradation. Through promoting timely degradation of many key regulatory proteins, SCF E3 ligase controls numerous cellular processes; its dysfunction contributes to a number of human diseases, including cancer. The RING component of SCF complex consists of 2 family members, RBX1 (RING box protein 1), also known as ROC1 (regulator of cullins), and RBX2/ROC2 (also known as SAG [sensitive to apoptosis gene]), both of which are essential for the catalytic activity of SCF. RBX1 and RBX2 are evolutionarily conserved from yeast to humans and play an essential role during mouse embryonic development. Moreover, RBX1 and RBX2 are both overexpressed in multiple human cancer tissues and required for the growth and survival of cancer cells. In this review, we will discuss the similarities and differences between 2 RING family members, their regulation of SCF E3 ligase activity, and their role in development, cancer cell survival, and skin carcinogenesis, along with a brief discussion of RBX-SCF E3 ligases as the cancer targets and a recently discovered small molecule inhibitor of SCF E3 ligases as a novel class of anticancer drugs.

Indexed as

anticancer targetsneddylationprotein degradationRING box proteinsSCF E3 ubiquitin ligasesubiquitin-proteasome system

Identifiers

PMID21103004
PMCPMC2983490
OpenAlexW2145861536

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.