Evidence map›Paper›PMID 36923932›Full record

ArticleInternational journal of biological sciences2023

Phosphorylation by IKKβ Promotes the Degradation of HMGCL via NEDD4 in Lung Cancer.

Chenxi Zhong, Guosheng Xiong, Haitang Yang, Xiaohua Du, Jiankui Du, Feng Yao, Wentao Fang, Yuezhen Deng

Open access · goldFull text read
In one paragraph

Article in International journal of biological sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
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  4. Review
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  8. Review
  9. Article
  10. Advances of E3 ligases in lung cancer.Biochemistry and biophysics reports · 2024
    Review
  11. Article
  12. 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

8 authors at 2 institutions in 1 country.

Chenxi ZhongDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Guosheng XiongDepartment of Thoracic Surgery, The First Affiliated Hospital of Kunming Medical University, Kunming, 650032, Yunnan, China.
Haitang YangDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Xiaohua DuDepartment of Respiratory and Critical Care Medicine. The First Affiliated Hospital of Kunming Medical University, Kunming, 650032, Yunnan, China.
Jiankui DuDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Feng YaoDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Wentao FangDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Yuezhen DengDepartment of Thoracic Surgery, Shanghai Chest Hospital, School of Medicine, Shanghai Jiao Tong University, 200030, Shanghai, China.
Shanghai Chest Hospital · CNKunming Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inflammation and metabolic reprogramming are hallmarks of cancer. How inflammation regulates cancer metabolism remains poorly understood. In this study, we found that 3-hydroxy-3-methylglutaryl-CoA lyase (HMGCL), the enzyme that catalyzes the catabolism of leucine and promotes the synthesis of ketone bodies, was downregulated in lung cancer. Downregulation of HMGCL was associated with a larger tumor size and a shorter overall survival time. In a functional study, overexpression of HMGCL increased the content of β-hydroxybutyrate (β-HB) and inhibited the tumorigenicity of lung cancer cells, and deletion of HMGCL promoted de novo tumorigenesis in KP (Kras

Indexed as

Lung NeoplasmsLyasesAnimalsI-kappa B KinaseInflammationMiceNedd4 Ubiquitin Protein LigasesOxo-Acid-LyasesPhosphorylationProtein Serine-Threonine KinasesTumor Necrosis Factor-alphaUbiquitinationUbiquitin-Protein Ligases3-hydroxy-3-methylglutaryl-coenzyme A lyaseI-kappa B KinaseLyasesNedd4 protein, mouseNedd4 Ubiquitin Protein LigasesOxo-Acid-LyasesProtein Serine-Threonine KinasesTumor Necrosis Factor-alphaUbiquitin-Protein LigasesHMGCLIKKβKetone bodyLung cancerNEDD4

Identifiers

PMID36923932
PMCPMC10008690
OpenAlexW4324009399

What OpenQuestion holds

Textfull text, public
LicenceCC BY
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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.