Evidence map›Paper›PMID 42615306›Full record

ReviewScience progress

RFWD3: A pivotal E3 ubiquitin ligase in DNA damage response, non-neoplastic disorders and multi-system tumorigenesis.

Yue Ding, Mingyue Zhu, Jiaping Shu, Guxin Zhou, Rong Jin, Min Chen, Ru Zhang, Fangyuan Chang

Abstract readReview
In one paragraph

Review in Science progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Yue DingSchool of Nursing and Midwifery, Jiangsu College of Nursing, Huai'an, China.
Mingyue ZhuDepartment of Obstetrics and Gynecology, Affiliated Dongtai Hospital of Nantong University, Dongtai, China.
Jiaping ShuSchool of Nursing, Jiangsu Health Vocational College, Nanjing, China.
Guxin ZhouDepartment of Obstetrics and Gynecology, Affiliated Dongtai Hospital of Nantong University, Dongtai, China.
Rong JinDepartment of Obstetrics and Gynecology, Affiliated Dongtai Hospital of Nantong University, Dongtai, China.
Min ChenDepartment of Obstetrics and Gynecology, Affiliated Dongtai Hospital of Nantong University, Dongtai, China.
Ru ZhangSchool of Nursing and Midwifery, Jiangsu College of Nursing, Huai'an, China.
Fangyuan ChangDepartment of Obstetrics and Gynecology, Affiliated Dongtai Hospital of Nantong University, Dongtai, China.ORCID 0009-0007-1057-8745

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RFWD3 is a multifunctional RING-type E3 ubiquitin ligase and a central hub in the DNA damage response (DDR) network. It regulates replication fork stability, homologous recombination repair, and cell cycle checkpoints through K63-linked ubiquitination of critical DDR effectors, thereby safeguarding genomic integrity. Germline RFWD3 dysfunction disrupts genomic homeostasis, leading to hereditary non-neoplastic disorders, including Fanconi anemia and premature ovarian insufficiency, while somatic aberrations drive tumorigenesis across multiple organ systems. This narrative review summarizes the molecular mechanisms underlying RFWD3 function in the DDR network, then examines its roles in non-neoplastic disorders and tumorigenesis, and finally integrates recent advances from molecular genetics to translational medicine. Additionally, this review highlights the context-dependent oncogenic and tumor-suppressive functions of RFWD3 in different disease settings and provides a theoretical framework for the precision diagnosis, prognostic stratification, and targeted intervention of RFWD3-associated disorders.

Indexed as

CarcinogenesisDNA DamageUbiquitin-Protein LigasesAnimalsDNA RepairFanconi AnemiaFemaleHumansPrimary Ovarian InsufficiencyRFWD3 protein, humanUbiquitin-Protein LigasesDNA damage responsegenetic diseasesmolecular targeted therapyneoplasmsRFWD3ubiquitin-protein ligases

Identifiers

PMID42615306
PMCPMC13490819

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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.