Evidence map›Paper›PMID 29552646›Full record

ArticleBiochemistry and biophysics reports2017

Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog.

Dario Spigolon, D Travis Gallagher, Adrian Velazquez-Campoy, Donatella Bulone, Jatin Narang, Pier Luigi San Biagio, Francesco Cappello, Alberto J L Macario, Everly Conway de Macario, Frank T Robb

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

Article in Biochemistry and biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 7 institutions in 3 countries.

Dario SpigolonInstitute for Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA.
D Travis GallagherInstitute for Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA.
Adrian Velazquez-CampoyInstitute of Biocomputation and Physics of Complex Systems (BIFI), Joint Units: BIFI-IQFR and GBsC-CSIC,Universidad de Zaragoza, Zaragoza, Spain.
Donatella BuloneInstitute of Biophysics, UOS Palermo, National Research Council, Italy.
Jatin NarangInstitute for Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA.
Pier Luigi San BiagioInstitute of Biophysics, UOS Palermo, National Research Council, Italy.
Francesco CappelloDepartment of Biomedicine and Clinical Neurosciences, Human Anatomy Section, University of Palermo, Palermo, Italy.
Alberto J L MacarioEuro-Mediterranean Institute of Science and Technology (IEMEST), Palermo, Italy.
Everly Conway de MacarioEuro-Mediterranean Institute of Science and Technology (IEMEST), Palermo, Italy.
Frank T RobbInstitute for Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA.
Advanced Bioscience Laboratories (United States) · USInstitute for Bioscience and Biotechnology ResearchNational Research Council · ITInstituto de Investigación Sanitaria Aragón · ESIstituto Euro Mediterraneo di Scienza e Tecnologia · ITUniversity of Maryland, Baltimore · USUniversity of Palermo · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The disassembly of the wild type complex, which is tightly coupled with subunit denaturation, was decoupled by the mutation without affecting the stability of individual subunits. Our results verify the effectiveness of the homo-hexadecameric archaeal chaperonin as a proxy to assess the impact of subtle defects in heterologous systems with mutations in a single subunit.

Indexed as

CCT5ChaperoninChaperonopathiesDLS, dynamic light scatteringDSC, differential scanning calorimetryITC, isothermal titration calorimetryNeuropathyPf-CD1, Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deletedPf, Pyrococcus furiosusProtein calorimetryPyrococcus furiosus

Identifiers

PMID29552646
PMCPMC5851525
OpenAlexW2752113200

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.