Evidence map›Paper›PMID 26633535›Full record

ReviewBiomolecules2015

A Novel Aspect of Tumorigenesis-BMI1 Functions in Regulating DNA Damage Response.

Xiaozeng Lin, Diane Ojo, Fengxiang Wei, Nicholas Wong, Yan Gu, Damu Tang

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Dual-Targeting CSC Therapy: Acid-Responsive Cisplatin/CaCOPharmaceuticals (Basel, Switzerland) · 2025
    Article
  8. Molecular regulation and therapeutic targeting ofFrontiers in cell and developmental biology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022
    Review
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Xiaozeng LinDepartment of Medicine, Division of Nephrology, McMaster University, Hamilton, ON L8S 4L8, Canada. linx36@mcmaster.ca.
Diane OjoDepartment of Medicine, Division of Nephrology, McMaster University, Hamilton, ON L8S 4L8, Canada. ojod@mcmaster.ca.
Fengxiang WeiThe Genetics Laboratory, Longgang District Maternity and Child Healthcare Hospital, Longgang District, Shenzhen 518000, China. haowei727499@163.com.
Nicholas WongDepartment of Medicine, Division of Nephrology, McMaster University, Hamilton, ON L8S 4L8, Canada. wongnyh@gmail.com.
Yan GuDepartment of Medicine, Division of Nephrology, McMaster University, Hamilton, ON L8S 4L8, Canada. yangu@hotmail.ca.
Damu TangDepartment of Medicine, Division of Nephrology, McMaster University, Hamilton, ON L8S 4L8, Canada. damut@mcmaster.ca.
St. Joseph's Hospital · CAShenzhen Maternity and Child Healthcare Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BMI1 plays critical roles in maintaining the self-renewal of hematopoietic, neural, intestinal stem cells, and cancer stem cells (CSCs) for a variety of cancer types. BMI1 promotes cell proliferative life span and epithelial to mesenchymal transition (EMT). Upregulation of BMI1 occurs in multiple cancer types and is associated with poor prognosis. Mechanistically, BMI1 is a subunit of the Polycomb repressive complex 1 (PRC1), and binds the catalytic RING2/RING1b subunit to form a functional E3 ubiquitin ligase. Through mono-ubiquitination of histone H2A at lysine 119 (H2A-K119Ub), BMI1 represses multiple gene loci; among these, the INK4A/ARF locus has been most thoroughly investigated. The locus encodes the p16INK4A and p14/p19ARF tumor suppressors that function in the pRb and p53 pathways, respectively. Its repression contributes to BMI1-derived tumorigenesis. BMI1 also possesses other oncogenic functions, specifically its regulative role in DNA damage response (DDR). In this process, BMI1 ubiquitinates histone H2A and γH2AX, thereby facilitating the repair of double-stranded DNA breaks (DSBs) through stimulating homologous recombination and non-homologous end joining. Additionally, BMI1 compromises DSB-induced checkpoint activation independent of its-associated E3 ubiquitin ligase activity. We review the emerging role of BMI1 in DDR regulation and discuss its impact on BMI1-derived tumorigenesis.

Indexed as

DNA DamageAnimalsCarcinogenesisDNA RepairHumansMitogen-Activated Protein Kinase 7MAPK7 protein, humanMitogen-Activated Protein Kinase 7ATMBMI1checkpoint activationDNA damage response (DDR)H2Ahistone ubiquitinationrepair of double-stranded DNA breaksγH2AX

Identifiers

PMID26633535
PMCPMC4693283
OpenAlexW2185968630

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.