Evidence map›Paper›PMID 30755483›Full record

ArticleThe Journal of biological chemistry2019

Methionine oxidation in α-synuclein inhibits its propensity for ordered secondary structure.

Erika Ponzini, Antonella De Palma, Lucilla Cerboni, Antonino Natalello, Rossana Rossi, Rani Moons, Albert Konijnenberg, Joanna Narkiewicz, Giuseppe Legname, Frank Sobott and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. 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
3.9field-weighted citation impact, top 6% 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, 41 citations in OpenAlex.

  1. Article
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  8. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Metal ions shape α-synuclein.Scientific reports · 2020
    Article
  17. Article
  18. Dietary Antioxidants and Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2020
    Review
  19. One- and Two-Electron Oxidations of β-AmyloidMolecules (Basel, Switzerland) · 2020
    Article
  20. Autophagy and Redox Homeostasis in Parkinson's: A Crucial Balancing Act.Oxidative medicine and cellular longevity · 2020
    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

13 authors at 5 institutions in 3 countries.

Erika PonziniFrom the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy.
Antonella De Palmathe Institute of Biomedical Technologies, National Research Council of Italy, Segrate, 20090 Milan, Italy.ORCID 0000-0001-5937-8604
Lucilla CerboniFrom the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy.
Antonino NatalelloFrom the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy.ORCID 0000-0002-1489-272X
Rossana Rossithe Institute of Biomedical Technologies, National Research Council of Italy, Segrate, 20090 Milan, Italy.ORCID 0000-0002-0313-7083
Rani Moonsthe Biomolecular and Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.
Albert Konijnenbergthe Biomolecular and Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.
Joanna Narkiewiczthe Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA) and ELETTRA-Sincrotrone Trieste S.C.p.A, 34136 Trieste, Italy.
Giuseppe Legnamethe Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA) and ELETTRA-Sincrotrone Trieste S.C.p.A, 34136 Trieste, Italy.ORCID 0000-0003-0716-4393
Frank Sobottthe Biomolecular and Analytical Mass Spectrometry, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.ORCID 0000-0001-9029-1865
PierLuigi Maurithe Institute of Biomedical Technologies, National Research Council of Italy, Segrate, 20090 Milan, Italy.ORCID 0000-0003-4364-0393
Carlo SantambrogioFrom the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy, carlo.santambrogio@unimib.it.
Rita GrandoriFrom the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy, rita.grandori@unimib.it.
University of Milano-Bicocca · ITInstitute of Biomedical Technologies · ITScuola Internazionale Superiore di Studi Avanzati · ITUniversity of Antwerp · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (AS) is an intrinsically disordered protein highly expressed in dopaminergic neurons. Its amyloid aggregates are the major component of Lewy bodies, a hallmark of Parkinson's disease (PD). AS is particularly exposed to oxidation of its methionine residues, both

Indexed as

Protein AggregatesProtein Foldingalpha-SynucleinCatechinHumansLewy BodiesMethionineOxidation-ReductionParkinson DiseaseProtein Structure, SecondaryProtein Structure, Tertiaryalpha-SynucleinCatechinepigallocatechin gallateMethionineProtein AggregatesSNCA protein, humanamyloidcircular dichroism (CD)dopamineepigallocatechin-3-gallateFourier transform IR (FTIR)ion mobility (IM)mass spectrometry (MS)methionine oxidationneurodegenerative diseaseα-synuclein (α-synuclein)

Identifiers

PMID30755483
PMCPMC6462524
OpenAlexW2912002356

What OpenQuestion holds

Textmetadata
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.