Evidence map›Paper›PMID 32430400›Full record

ArticleThe Journal of biological chemistry2020

The prohibitin-binding compound fluorizoline affects multiple components of the translational machinery and inhibits protein synthesis.

Xin Jin, Jianling Xie, Michael Zabolocki, Xuemin Wang, Tao Jiang, Dong Wang, Laurent Désaubry, Cedric Bardy, Christopher G Proud

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Prohibitins: A Key Link between Mitochondria and Nervous System Diseases.Oxidative medicine and cellular longevity · 2022
    Review
  7. Article
  8. Article
  9. SFPH proteins as therapeutic targets for a myriad of diseases.Bioorganic & medicinal chemistry letters · 2020
    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

9 authors at 5 institutions in 3 countries.

Xin JinLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia.
Jianling XieLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia.ORCID 0000-0002-0588-8016
Michael ZabolockiLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia.
Xuemin WangLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia.
Tao JiangLaboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology and School of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Dong WangSino-French Joint Lab of Food Nutrition/Safety and Medicinal Chemistry, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
Laurent DésaubrySino-French Joint Lab of Food Nutrition/Safety and Medicinal Chemistry, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.ORCID 0000-0002-1192-2970
Cedric BardyLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia.
Christopher G ProudLifelong Health Theme, South Australian Health & Medical Research Institute, Adelaide, Australia Christopher.Proud@sahmri.com.
South Australian Health and Medical Research Institute · AUFlinders University · AUQingdao National Laboratory for Marine Science and Technology · CNCentre National de la Recherche Scientifique · FRTianjin University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorizoline (FLZ) binds to prohibitin-1 and -2 (PHB1/2), which are pleiotropic scaffold proteins known to affect signaling pathways involved in several intracellular processes. However, it is not yet clear how FLZ exerts its effect. Here, we show that exposure of three different human cancer cell lines to FLZ increases the phosphorylation of key translation factors, particularly of initiation factor 2 (eIF2) and elongation factor 2 (eEF2), modifications that inhibit their activities. FLZ also impaired signaling through mTOR complex 1, which also regulates the translational machinery,

Indexed as

A549 CellsCalciumEndoplasmic Reticulum StressEukaryotic Initiation Factor-2HEK293 CellsHeLa CellsHumansNeoplasm ProteinsNeoplasmsPeptide Elongation Factor 2PhosphorylationProhibitinsProtein BiosynthesisProtein Synthesis InhibitorsRepressor ProteinsCalciumEukaryotic Initiation Factor-2Neoplasm ProteinsPeptide Elongation Factor 2PHB protein, humanProhibitinsProtein Synthesis InhibitorsRepressor Proteinscalciumcancercell deatheEF2eIF2elongationendoplasmic reticulum stress (ER stress)eukaryotic initiation factor 2 (eIF2)eukaryotic translation initiationinitiationprohibitinprotein synthesistranslation elongation factor

Identifiers

PMID32430400
PMCPMC7380185
OpenAlexW3026210083

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.