Evidence map›Paper›PMID 24830947›Full record

ArticlePloS one2014

Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations.

Silvia Vilasi, Rita Carrotta, Maria Rosalia Mangione, Claudia Campanella, Fabio Librizzi, Loredana Randazzo, Vincenzo Martorana, Antonella Marino Gammazza, Maria Grazia Ortore, Annalisa Vilasi and 10 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 59 citations in OpenAlex.

  1. Biomolecular NMR assignments · 2025
    Article
  2. Article
  3. Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Heat Shock Proteins as Immunomodulants.Molecules (Basel, Switzerland) · 2018
    Review
  13. Heat Shock Proteins in Alzheimer's Disease: Role and Targeting.International journal of molecular sciences · 2018
    Review
  14. Article
  15. Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

20 authors at 6 institutions in 2 countries.

Silvia VilasiInstitute of Biophysics, National Research Council, Palermo, Italy.
Rita CarrottaInstitute of Biophysics, National Research Council, Palermo, Italy.
Maria Rosalia MangioneInstitute of Biophysics, National Research Council, Palermo, Italy.
Claudia CampanellaDepartment of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
Fabio LibrizziInstitute of Biophysics, National Research Council, Palermo, Italy.
Loredana RandazzoInstitute of Biophysics, National Research Council, Palermo, Italy.
Vincenzo MartoranaInstitute of Biophysics, National Research Council, Palermo, Italy.
Antonella Marino GammazzaDepartment of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
Maria Grazia OrtoreDepartment of Life and Environmental Sciences and National Interuniversity Consortium for the Physical Sciences of Matter, Marche Polytechnic University, Ancona, Italy.
Annalisa VilasiInstitute of Biosciences and Bioresources, National Research Council, Napoli, Italy.
Gabriella PocsfalviInstitute of Biosciences and Bioresources, National Research Council, Napoli, Italy.
Giosalba BurgioDepartment of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
Davide CoronaDepartment of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
Antonio Palumbo PiccionelloInstitute of Biophysics, National Research Council, Palermo, Italy; Department of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
Giovanni ZummoDepartment of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy.
Donatella BuloneInstitute of Biophysics, National Research Council, Palermo, Italy.
Everly Conway de MacarioDepartment of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and Institute of Marine and Environmental Technology, Columbus Center, Baltimore, Maryland, United States of America.
Alberto J L MacarioEuro-Mediterranean Institute of Science and Technology, Palermo, Italy; Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and Institute of Marine and Environmental Technology, Columbus Center, Baltimore, Maryland, United States of America.
Pier Luigi San BiagioInstitute of Biophysics, National Research Council, Palermo, Italy.
Francesco CappelloInstitute of Biophysics, National Research Council, Palermo, Italy; Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
National Research Council · ITUniversity of Palermo · ITUniversity of Maryland, Baltimore · USInstitute of Biosciences and Bioresources · ITIstituto Euro Mediterraneo di Scienza e Tecnologia · ITMarche Polytechnic University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naïve, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naïve cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60. We found that Naïve Hsp60 in aqueous solution is assembled in very stable heptamers and tetradecamers at all concentrations assayed, without any trace of monomer presence.

Indexed as

Adenosine TriphosphatasesCell-Free SystemChaperonin 60CytosolHumansHydrolysisInflammationMitochondriaMitochondrial ProteinsProtein BindingRecombinant ProteinsScattering, RadiationSpectrometry, FluorescenceAdenosine TriphosphatasesChaperonin 60HSPD1 protein, humanMitochondrial ProteinsRecombinant Proteins

Identifiers

PMID24830947
PMCPMC4022648
OpenAlexW1988411751

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.