Evidence map›Paper›PMID 29208924›Full record

ArticleScientific reports2017

HSP60 possesses a GTPase activity and mediates protein folding with HSP10.

Tomoya Okamoto, Hiroshi Yamamoto, Ikuru Kudo, Kazuya Matsumoto, Masafumi Odaka, Ewa Grave, Hideaki Itoh

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
–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

28 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  7. A conservedMicrobiology (Reading, England) · 2025
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  13. Mizoribine Promotes Molecular Chaperone HSP60/HSP10 Complex Formation.International journal of molecular sciences · 2024
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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

7 authors.

Tomoya OkamotoDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Hiroshi YamamotoDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Ikuru KudoDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Kazuya MatsumotoDepartment of Applied Chemistry, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Masafumi OdakaDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Ewa GraveDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan.
Hideaki ItohDepartment of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita, 010-8502, Japan. itohh@gipc.akita-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.

Indexed as

Adenosine TriphosphateAllosteric RegulationAnimalsBinding SitesChaperonin 10Chaperonin 60Computer SimulationGreen Fluorescent ProteinsGTP PhosphohydrolasesGuanosine TriphosphateModels, MolecularMolecular ChaperonesProtein FoldingProtein MultimerizationSus scrofaThiosulfate SulfurtransferaseAdenosine TriphosphateChaperonin 10Chaperonin 60Green Fluorescent ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMolecular ChaperonesThiosulfate Sulfurtransferase

Identifiers

PMID29208924
PMCPMC5717063

What OpenQuestion holds

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Registered trials

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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.