Evidence map›Paper›PMID 29951842›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein.

Piriya Wongkongkathep, Jong Yoon Han, Tae Su Choi, Sheng Yin, Hugh I Kim, Joseph A Loo

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Removal of Toxic Metabolites-Chelation: Manganese Disorders.Journal of inherited metabolic disease · 2025
    Review
  7. ZnJournal of the American Chemical Society · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. Three-repeat and four-repeat tau isoforms form different oligomers.Protein science : a publication of the Protein Society · 2022
    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

6 authors at 2 institutions in 3 countries.

Piriya WongkongkathepDepartment of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, CA, 90095, USA.
Jong Yoon HanDepartment of Chemistry, Korea University, Seoul, Republic of Korea.
Tae Su ChoiDepartment of Chemistry, Korea University, Seoul, Republic of Korea.
Sheng YinDepartment of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, CA, 90095, USA.
Hugh I KimDepartment of Chemistry, Korea University, Seoul, Republic of Korea.
Joseph A LooDepartment of Chemistry and Biochemistry, University of California-Los Angeles, Los Angeles, CA, 90095, USA. JLoo@chem.ucla.edu.ORCID 0000-0001-9989-1437
Korea University · KRUniversity of California, Los Angeles · US

Funding

UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
Ultra-High Resolution Mass Spectrometer for Biomedical ResearchS10RR028893 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2010 to 2010
$2.7M
High-Resolution Ion Mobility Mass SpectrometerS10OD018504 · OD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2014 to 2014
$915k
NCRR NIH HHS S10 RR028893NIGMS NIH HHS R01 GM103479NIGMS NIH HHS R01GM103479NIH HHS S10 OD018504
6 · The paper itself

Abstract

Structural characterization of intrinsically disordered proteins (IDPs) has been a major challenge in the field of protein science due to limited capabilities to obtain full-length high-resolution structures. Native ESI-MS with top-down MS was utilized to obtain structural features of protein-ligand binding for the Parkinson's disease-related protein, α-synuclein (αSyn), which is natively unstructured. Binding of heavy metals has been implicated in the accelerated formation of αSyn aggregation. Using high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry, native top-down MS with various fragmentation methods, including electron capture dissociation (ECD), collisional activated dissociation (CAD), and multistage tandem MS (MS

Indexed as

alpha-SynucleinCobaltIntrinsically Disordered ProteinsManganeseModels, MolecularSpectrometry, Mass, Electrospray IonizationTandem Mass Spectrometryalpha-SynucleinCobaltIntrinsically Disordered ProteinsManganeseElectron capture dissociationElectrospray ionizationMetal bindingNative mass spectrometryProtein-ligand complexTop-down mass spectrometryα-Synuclein

Identifiers

PMID29951842
PMCPMC6087494
OpenAlexW2809702123

What OpenQuestion holds

Textmetadata
LicenceTDM
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.