Evidence map›Paper›PMID 30131519›Full record

ArticleScientific reports2018

A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes.

Diletta Ami, Paolo Mereghetti, Manuela Leri, Sofia Giorgetti, Antonino Natalello, Silvia Maria Doglia, Massimo Stefani, Monica Bucciantini

Open access · goldAbstract readComparative Study
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Effects ofAnimals : an open access journal from MDPI · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. AnAnnals of medicine · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2020
    Review
  19. A convenient protein library for spectroscopic calibrations.Computational and structural biotechnology journal · 2020
    Article
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 4 institutions in 1 country.

Diletta AmiDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy. diletta.ami@unimib.it.
Paolo MereghettiDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy.
Manuela LeriDepartment of Neuroscience, Psychology, Area of Medicine and Health of the Child of the University of Florence, Viale Pieraccini, 6, 50139, Florence, Italy.
Sofia GiorgettiDepartment of Molecular Medicine, Unit of Biochemistry, University of Pavia, Viale Taramelli 3/B, 27100, Pavia, Italy.
Antonino NatalelloDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy.ORCID 0000-0002-1489-272X
Silvia Maria DogliaDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy.
Massimo StefaniDepartment of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, 50134, Florence, Italy.
Monica BucciantiniDepartment of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, 50134, Florence, Italy. monica.bucciantini@unifi.it.
University of Milano-Bicocca · ITUniversity of Florence · ITConsorzio Interuniversitario Nazionale per l'Informatica · ITUniversity of Pavia · IT

Funding

Università degli Studi di Milano-Bicocca (University of Milano-Bicocca) 2016-ATE-0385
6 · The paper itself

Abstract

Protein misfolding and aggregation are associated with a number of human degenerative diseases. In spite of the enormous research efforts to develop effective strategies aimed at interfering with the pathogenic cascades induced by misfolded/aggregated peptides/proteins, the necessary detailed understanding of the molecular bases of amyloid formation and toxicity is still lacking. To this aim, approaches able to provide a global insight in amyloid-mediated physiological alterations are of importance. In this study, we exploited Fourier transform infrared microspectroscopy, supported by multivariate analysis, to investigate in situ the spectral changes occurring in cultured intact HL-1 cardiomyocytes exposed to wild type (WT) or mutant (L55P) transthyretin (TTR) in native, or amyloid conformation. The presence of extracellular deposits of amyloid aggregates of WT or L55P TTR, respectively, is a key hallmark of two pathological conditions, known as senile systemic amyloidosis and familial amyloid polyneuropathy. We found that the major effects, associated with modifications in lipid properties and in the cell metabolic/phosphorylation status, were observed when natively folded WT or L55P TTR was administered to the cells. The effects induced by aggregates of TTR were milder and in some cases displayed a different timing compared to those elicited by the natively folded protein.

Indexed as

MutationAmyloidCalciumCells, CulturedCell SurvivalHumansMembrane LipidsMultivariate AnalysisMyocytes, CardiacPhosphorylationPrealbuminProtein AggregatesProtein FoldingReactive Oxygen SpeciesSpectroscopy, Fourier Transform InfraredAmyloidCalciumMembrane LipidsPrealbuminProtein AggregatesReactive Oxygen SpeciesTTR protein, human

Identifiers

PMID30131519
PMCPMC6104026
OpenAlexW2887364413

What OpenQuestion holds

Textmetadata
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.