Evidence map›Paper›PMID 25629232›Full record

ArticleInternational journal of molecular sciences2015

Binding mode analysis of zerumbone to key signal proteins in the tumor necrosis factor pathway.

Ayesha Fatima, Ahmad Bustamam Hj Abdul, Rasedee Abdullah, Roghayeh Abedi Karjiban, Vannajan Sanghiran Lee

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 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
3.2field-weighted citation impact, top 10% 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, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Molecules (Basel, Switzerland) · 2023
    Article
  4. Review
  5. Protective Effects of Zerumbone on Colonic Tumorigenesis in EnterotoxigenicInternational journal of molecular sciences · 2020
    Article
  6. Zerumbone Suppresses EnterotoxigenicInternational journal of molecular sciences · 2019
    Article
  7. Review
  8. Article
  9. Review
  10. Article
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 2 institutions in 1 country.

Ayesha FatimaUPM-MAKNA Cancer Research Laboratory, Institute of Biosciences, University Putra Malaysia, 43400 Serdang, Malaysia. ayeshafatima.69@gmail.com.
Ahmad Bustamam Hj AbdulUPM-MAKNA Cancer Research Laboratory, Institute of Biosciences, University Putra Malaysia, 43400 Serdang, Malaysia. ahmadbstmm@yahoo.com.
Rasedee AbdullahUPM-MAKNA Cancer Research Laboratory, Institute of Biosciences, University Putra Malaysia, 43400 Serdang, Malaysia. rasedee@gmail.com.
Roghayeh Abedi KarjibanDepartment of Chemistry, Faculty of Science, University Putra Malaysia, 43400 Serdang, Malaysia. rosa.abedi@gmail.com.
Vannajan Sanghiran LeeDepartment of Chemistry, Faculty of Science, University Malaya, Petaling Jaya, 50603 Selangor, Malaysia. vannajan@gmail.com.
Universiti Putra Malaysia · MYUniversity of Malaya · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Breast cancer is the second most common cancer among women worldwide. Several signaling pathways have been implicated as causative and progression agents. The tumor necrosis factor (TNF) α protein plays a dual role in promoting and inhibiting cancer depending largely on the pathway initiated by the binding of the protein to its receptor. Zerumbone, an active constituent of Zingiber zerumbet, Smith, is known to act on the tumor necrosis factor pathway upregulating tumour necrosis factor related apoptosis inducing ligand (TRAIL) death receptors and inducing apoptosis in cancer cells. Zerumbone is a sesquiterpene that is able to penetrate into the hydrophobic pockets of proteins to exert its inhibiting activity with several proteins. We found a good binding with the tumor necrosis factor, kinase κB (IKKβ) and the Nuclear factor κB (NF-κB) component proteins along the TNF pathway. Our results suggest that zerumbone can exert its apoptotic activities by inhibiting the cytoplasmic proteins. It inhibits the IKKβ kinase that activates the NF-κB and also binds to the NF-κB complex in the TNF pathway. Blocking both proteins can lead to inhibition of cell proliferating proteins to be downregulated and possibly ultimate induction of apoptosis.

Indexed as

Amino Acid SequenceBinding SitesCatalytic DomainDatabases, ProteinI-kappa B KinaseMolecular Docking SimulationMolecular Sequence DataNF-kappa BProtein BindingSesquiterpenesTumor Necrosis Factor-alphaI-kappa B KinaseNF-kappa BSesquiterpenesTumor Necrosis Factor-alphazerumbone

Identifiers

PMID25629232
PMCPMC4346863
OpenAlexW1975923861

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.