Evidence map›Paper›PMID 26336826›Full record

ArticleOncotarget2015

A conserved RAD6-MDM2 ubiquitin ligase machinery targets histone chaperone ASF1A in tumorigenesis.

Chen Wang, Jian-Feng Chang, Hongli Yan, Da-Liang Wang, Yan Liu, Yuanya Jing, Meng Zhang, Yu-Long Men, Dongdong Lu, Xiao-Mei Yang and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024
    Review
  2. Article
  3. Epigenetics in prostate cancer treatment.Journal of translational genetics and genomics · 2021
    Article
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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

12 authors at 4 institutions in 1 country.

Chen WangResearch Center for Translational Medicine at East Hospital, Tongji University, Shanghai, 200120/200092, China.
Jian-Feng ChangResearch Center for Translational Medicine at East Hospital, Tongji University, Shanghai, 200120/200092, China.
Hongli YanDepartment of Laboratory Medicine, Changhai Hospital, The Second Military Medical University, Shanghai, 200433, China.
Da-Liang WangInstitute of Epigenetics and Cancer Research, School of Medicine, Tsinghua University, Beijing, 100084, China.
Yan LiuInstitute of Epigenetics and Cancer Research, School of Medicine, Tsinghua University, Beijing, 100084, China.
Yuanya JingSchool of Life Sciences and Technology, Tongji University, Shanghai, 200120/200092, China.
Meng ZhangSchool of Life Sciences and Technology, Tongji University, Shanghai, 200120/200092, China.
Yu-Long MenSchool of Life Sciences and Technology, Tongji University, Shanghai, 200120/200092, China.
Dongdong LuSchool of Life Sciences and Technology, Tongji University, Shanghai, 200120/200092, China.
Xiao-Mei YangSchool of Life Sciences and Technology, Tongji University, Shanghai, 200120/200092, China.
Su ChenResearch Center for Translational Medicine at East Hospital, Tongji University, Shanghai, 200120/200092, China.
Fang-Lin SunResearch Center for Translational Medicine at East Hospital, Tongji University, Shanghai, 200120/200092, China.
Tongji University · CNShanghai East Hospital · CNTsinghua University · CNChanghai Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin is a highly organized and dynamic structure in eukaryotic cells. The change of chromatin structure is essential in many cellular processes, such as gene transcription, DNA damage repair and others. Anti-silencing function 1 (ASF1) is a histone chaperone that participates in chromatin higher-order organization and is required for appropriate chromatin assembly. In this study, we identified the E2 ubiquitin-conjugating enzyme RAD6 as an evolutionary conserved interacting protein of ASF1 in D. melanogaster and H. sapiens that promotes the turnover of ASF1A by cooperating with a well-known E3 ligase, MDM2, via ubiquitin-proteasome pathway in H. sapiens. Further functional analyses indicated that the interplay between RAD6 and ASF1A associates with tumorigenesis. Together, these data suggest that the RAD6-MDM2 ubiquitin ligase machinery is critical for the degradation of chromatin-related proteins.

Indexed as

AnimalsBlotting, WesternCell Cycle ProteinsCell LineCell Line, TumorDrosophila melanogasterDrosophila ProteinsGene Expression Regulation, NeoplasticHEK293 CellsHep G2 CellsHistonesHumansLung NeoplasmsMicroscopy, ConfocalMolecular ChaperonesProto-Oncogene Proteins c-mdm2ASF1A protein, humanCell Cycle ProteinsDrosophila ProteinsHistonesMDM2 protein, humanMolecular ChaperonesProto-Oncogene Proteins c-mdm2UBE2A protein, humanUBE2B protein, humanUbiquitin-Conjugating EnzymesASF1AMDM2protein degradationRAD6tumorigenesis

Identifiers

PMID26336826
PMCPMC4745749
OpenAlexW1859487564

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.