Evidence map›Paper›PMID 26345206›Full record

ArticleScientific reports2015

Geranylgeranylacetone selectively binds to the HSP70 of Helicobacter pylori and alters its coccoid morphology.

Ewa Grave, Shin-ichi Yokota, Soh Yamamoto, Arisa Tamura, Takako Ohtaki-Mizoguchi, Kenji Yokota, Keiji Oguma, Kazuhiko Fujiwara, Nobuaki Ogawa, Tomoya Okamoto and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. The Role ofInternational journal of molecular sciences · 2025
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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

12 authors at 4 institutions in 1 country.

Ewa GraveDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Shin-ichi YokotaDepartment of Microbiology, Sapporo Medical University School of Medicine, Sapporo, 060-8556, Japan.
Soh YamamotoDepartment of Microbiology, Sapporo Medical University School of Medicine, Sapporo, 060-8556, Japan.
Arisa TamuraDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Takako Ohtaki-MizoguchiDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Kenji YokotaGraduate School of Health Sciences, Okayama University, Okayama 700-8558, Japan.
Keiji OgumaDepartment of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8558, Japan.
Kazuhiko FujiwaraDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Nobuaki OgawaDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Tomoya OkamotoDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Michiro OtakaDepartment of Gastroenterology, Juntendo University School of Medicine, Bunkyo-Ku, Tokyo 113-8421, Japan.
Hideaki ItohDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan.
Akita University · JPOkayama University · JPSapporo Medical University · JPJuntendo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Geranylgeranylacetone (GGA) is used to treat patients suffering from peptic ulcers and gastritis. We examined the effect of GGA on Helicobacter pylori, which is a causative factor of gastrointestinal diseases. Previously, we have reported that GGA binds specifically to the molecular chaperone HSP70. In this paper, we report that GGA bounds to H. pylori HSP70 (product of the DnaK gene) with 26-times higher affinity than to human HSP70, and induced large conformational changes as observed from surface plasmon resonance and circular dichroism. Binding of GGA suppressed the activity of the H. pylori chaperone. GGA also altered several characteristics of H. pylori cells. GGA-treated cells elicited enhanced interleukin-8 production by gastric cancer cell lines and potentiated susceptibility to complement as compared to untreated cells. GGA also caused morphological alterations in H. pylori as reflected in fewer coccoid-like cells, suggesting that GGA converts H. pylori to an actively dividing, spiral state (vegetative form) from a non-growing, coccoid state. This morphological conversion by GGA resulted in accelerated growth of H. pylori. These results suggest a model in which GGA sensitizes H. pylori to antibiotic treatment by converting the cells to an actively growing state.

Indexed as

Protein ConformationBacterial ProteinsCell Line, TumorDiterpenesHelicobacter pyloriHSP70 Heat-Shock ProteinsHumansProtein BindingRecombinant ProteinsSurface Plasmon ResonanceBacterial ProteinsDiterpenesgeranylgeranylacetoneHSP70 Heat-Shock ProteinsRecombinant Proteins

Identifiers

PMID26345206
PMCPMC4561889
OpenAlexW1423091113

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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 OpenQuestion graph.