Evidence map›Paper›PMID 36973006›Full record

ArticleLife science alliance2023

Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation.

Meng-Cheng Lai, Hao-Yu Cheng, Sin-Hong Lew, Yu-An Chen, Chien-Hung Yu, Han-You Lin, Shih-Ming Lin

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Meng-Cheng LaiDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Hao-Yu ChengDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.ORCID https://orcid.org/0000-0001-9504-9066
Sin-Hong LewDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Yu-An ChenDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Chien-Hung YuDepartment of Biochemistry and Molecular Biology, National Cheng Kung University, Tainan, Taiwan.
Han-You LinDepartment of Veterinary Medicine, School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan.
Shih-Ming LinDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan smlin@mail.ncku.edu.tw.ORCID https://orcid.org/0000-0002-9672-8316

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial Hsp60 (mtHsp60) plays a crucial role in maintaining the proper folding of proteins in the mitochondria. mtHsp60 self-assembles into a ring-shaped heptamer, which can further form a double-ring tetradecamer in the presence of ATP and mtHsp10. However, mtHsp60 tends to dissociate in vitro, unlike its prokaryotic homologue, GroEL. The molecular structure of dissociated mtHsp60 and the mechanism behind its dissociation remain unclear. In this study, we demonstrated that

Indexed as

ChaperoninsEscherichia coliAdenosine TriphosphateMitochondriaAdenosine TriphosphateChaperonins

Identifiers

PMID36973006
PMCPMC10053435

What OpenQuestion holds

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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.