Evidence map›Paper›PMID 31637449›Full record

ReviewCellular and molecular life sciences : CMLS2020

The role of E3 ubiquitin ligase HECTD3 in cancer and beyond.

Qiuyun Jiang, Fubing Li, Zhuo Cheng, Yanjie Kong, Ceshi Chen

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Portrait of WWP1: the current state in human cancer.Frontiers in cell and developmental biology · 2024
    Review
  10. Article
  11. Genes · 2023
    Article
  12. Article
  13. Regulation of apoptosis by ubiquitination in liver cancer.American journal of cancer research · 2023
    Review
  14. Article
  15. Targeting HECTD3-IKKα axis inhibits inflammation-related metastasis.Signal transduction and targeted therapy · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

5 authors at 4 institutions in 1 country.

Qiuyun JiangKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences and Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, 650223, China.
Fubing LiAffiliated Cancer Hospital and Institute of Guangzhou Medical University, Guangzhou, 510095, China.
Zhuo ChengKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences and Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, 650223, China.
Yanjie KongInstitute of Translation Medicine, Shenzhen Second People's Hospital, The First Affiliated Hospital of Shenzhen University, Shenzhen, 518035, China.
Ceshi ChenKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences and Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, 650223, China. chenc@mail.kiz.ac.cn.
Chinese Academy of Sciences · CNGuangzhou Medical University · CNKunming Institute of Zoology · CNShenzhen Second People's Hospital · CN

Funding

Key Technologies Research and Development Program (CN) 2018YFC2000400National Natural Science Foundation of China 31771516National Natural Science Foundation of China 81773149National Natural Science Foundation of China 81830087National Natural Science Foundation of China U1602221
6 · The paper itself

Abstract

Ubiquitin modification plays significant roles in protein fate determination, signaling transduction, and cellular processes. Over the past 2 decades, the number of studies on ubiquitination has demonstrated explosive growth. E3 ubiquitin ligases are the key enzymes that determine the substrate specificity and are involved in cancer. Several recent studies shed light on the functions and mechanisms of HECTD3 E3 ubiquitin ligase. This review describes the progress in the recent studies of HECTD3 in cancer and other diseases. We propose that HECTD3 is a potential biomarker and a therapeutic target, and discuss the future directions for HECTD3 investigations.

Indexed as

AnimalsBiomarkers, TumorEnzyme InhibitorsHumansMolecular Targeted TherapyNeoplasmsUbiquitinationUbiquitin-Protein LigasesBiomarkers, TumorEnzyme InhibitorsHECTD3 protein, humanUbiquitin-Protein LigasesCancerHECTD3InhibitorsUbiquitination

Identifiers

PMID31637449
PMCPMC11105068
OpenAlexW2982254651

What OpenQuestion holds

Textmetadata
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.