Evidence mapPaperPMID 37705738Full record

ReviewInternational journal of biological sciences2023

IκB kinase β (IKKβ): Structure, transduction mechanism, biological function, and discovery of its inhibitors.

Juan Zhang, Rui Zhang, Wei Li, Xiao-Chi Ma, Feng Qiu, Cheng-Peng Sun

Abstract readReview
In one paragraph

Review 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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Review
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  12. Computational Analysis andCurrent medicinal chemistry · 2026
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  13. Review
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  15. Article
  16. Review
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  18. Targeting PBK with small-molecule 1-Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

6 authors.

Juan ZhangSchool of Chinese Materia Medica, State Key Laboratory of Component-Based Chinese Medicine, Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China.
Rui ZhangSchool of Chinese Materia Medica, State Key Laboratory of Component-Based Chinese Medicine, Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China.
Wei LiSchool of Chinese Materia Medica, State Key Laboratory of Component-Based Chinese Medicine, Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China.
Xiao-Chi MaCollege of Pharmacy, Second Affiliated Hospital, Dalian Medical University, Dalian 116044, China.
Feng QiuSchool of Chinese Materia Medica, State Key Laboratory of Component-Based Chinese Medicine, Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China.
Cheng-Peng SunSchool of Chinese Materia Medica, State Key Laboratory of Component-Based Chinese Medicine, Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 301617, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effective approach to discover innovative drugs will ask natural products for answers because of their complex and changeable structures and multiple biological activities. Inhibitory kappa B kinase beta (IKKβ), known as IKK2, is a key regulatory kinase responsible for the activation of NF-κB through its phosphorylation at Ser177 and Ser181 to promote the phosphorylation of inhibitors of kappa B (IκBs), triggering their ubiquitination and degradation to active the nuclear factor kappa-B (NF-κB) cascade. Chemical inhibition of IKKβ or its genetic knockout has become an effective method to block NF-κB-mediated proliferation and migration of tumor cells and inflammatory response. In this review, we summarized the structural feature and transduction mechanism of IKKβ and the discovery of inhibitors from natural resources (e.g. sesquiterpenoids, diterpenoids, triterpenoids, flavonoids, and alkaloids) and chemical synthesis (e.g. pyrimidines, pyridines, pyrazines, quinoxalines, thiophenes, and thiazolidines). In addition, the biosynthetic pathway of novel natural IKKβ inhibitors and their biological potentials were discussed. This review will provide inspiration for the structural modification of IKKβ inhibitors based on the skeleton of natural products or chemical synthesis and further phytochemistry investigations.

Indexed as

Biological ProductsI-kappa B KinaseNF-kappa BPhosphorylationProtein Serine-Threonine KinasesBiological ProductsI-kappa B KinaseNF-kappa BProtein Serine-Threonine KinasesBioactivitychemical synthesisIKKβInhibitorNatural products

Identifiers

PMID37705738
PMCPMC10496512

What Socratic holds

Textmetadata
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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 Socratic graph.