Evidence map›Paper›PMID 34639138›Full record

ArticleInternational journal of molecular sciences2021

Oligomeric Structural Transition of HspB1 from Chinese Hamster.

Nina Kurokawa, Rio Midorikawa, Manami Nakamura, Keiichi Noguchi, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Masafumi Yohda

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 55% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. A new perspective on iron-dependent cell death: PRDX-1-mediated ferroptosis in tumor cells.Apoptosis : an international journal on programmed cell death · 2025
    Review
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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

8 authors at 2 institutions in 1 country.

Nina KurokawaDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
Rio MidorikawaDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
Manami NakamuraDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
Keiichi NoguchiInstrumentation Analysis Center, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.
Ken MorishimaInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.ORCID 0000-0003-1091-3850
Rintaro InoueInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
Masaaki SugiyamaInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka 590-0494, Japan.
Masafumi YohdaDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.ORCID 0000-0001-8307-9671
Tokyo University of Agriculture and Technology · JPKyoto University · JP

Funding

Japan Society for the Promotion of Science 18H03681Japan Society for the Promotion of Science 18H04690Japan Society for the Promotion of Science 18H05229Japan Society for the Promotion of Science 19K16088Japan Society for the Promotion of Science 19KK0071Japan Society for the Promotion of Science 20H02532Japan Society for the Promotion of Science 20K06579Japan Society for the Promotion of Science 21K15051
6 · The paper itself

Abstract

HspB1 is a mammalian sHsp that is ubiquitously expressed in almost all tissues and involved in regulating many vital functions. Although the recent crystal structure of human HspB1 showed that 24 monomers form the oligomeric complex of human HspB1 in a spherical configuration, the molecular architecture of HspB1 is still controversial. In this study, we examined the oligomeric structural change of CgHspB1 by sedimentation velocity analytical ultracentrifugation. At the low temperature of 4 °C, CgHspB1 exists as an 18-mer, probably a trimeric complex of hexamers. It is relatively unstable and partially dissociates into small oligomers, hexamers, and dodecamers. At elevated temperatures, the 24-mer was more stable than the 18-mer. The 24-mer is also in dynamic equilibrium with the dissociated oligomers in the hexameric unit. The hexamer further dissociates to dimers. The disulfide bond between conserved cysteine residues seems to be partly responsible for the stabilization of hexamers. The N-terminal domain is involved in the assembly of dimers and the interaction between hexamers. It is plausible that CgHspB1 expresses a chaperone function in the 24-mer structure.

Indexed as

Protein ConformationProtein MultimerizationAnimalsCHO CellsCricetinaeCricetulusHeat-Shock ProteinsHumansMolecular ChaperonesProtein DomainsHeat-Shock ProteinsHSPB1 protein, humanMolecular Chaperonesanalytical ultracentrifugationchaperoneChinese hamsterfoldingsmall heat shock protein

Identifiers

PMID34639138
PMCPMC8509488
OpenAlexW3203320427

What OpenQuestion holds

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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.