Evidence map›Paper›PMID 30796622›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

Top-Down Analysis of Proteins in Low Charge States.

Aarti Bashyal, James D Sanders, Dustin D Holden, Jennifer S Brodbelt

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  2. Article
  3. AsymmetricJournal of the American Chemical Society · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Mesh Fragmentation Improves Dissociation Efficiency in Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Aarti BashyalDepartment of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA.
James D SandersDepartment of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA.
Dustin D HoldenDepartment of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA.
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA. jbrodbelt@cm.utexas.edu.ORCID http://orcid.org/0000-0003-3207-0217
The University of Texas at Austin · US

Funding

UVPD Mass Spectrometry of Protein ComplexesR01GM121714 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2017 to 2020
$1.4M
National Institutes of Health GM121714NIGMS NIH HHS R01 GM121714Welch Foundation F-1155
6 · The paper itself

Abstract

The impact of charging methods on the dissociation behavior of intact proteins in low charge states is investigated using HCD and 193 nm UVPD. Low charge states are produced for seven different proteins using the following four different methods: (1) proton transfer reactions of ions in high charge states generated from conventional denaturing solutions; (2) ESI of proteins in solutions of high ionic strength to enhance retention of folded native-like conformations; (3) ESI of proteins in high pH solutions to limit protonation; and (4) ESI of carbamylated proteins. Comparison of sequence coverages, degree of preferential cleavages, and types and distribution of fragment ions reveals a number of differences in the fragmentation patterns depending on the method used to generate the ions. More notable differences in these metrics are observed upon HCD than upon UVPD. The fragmentation caused by HCD is influenced more significantly by the presence/absence of mobile protons, a factor that modulates the degree of preferential cleavages and net sequence coverages. Carbamylation of the lysines and the N-terminus of the proteins alters the proton mobility by reducing the number of proton-sequestering, highly basic sites as evidenced by decreased preferential fragmentation C-terminal to Asp or N-terminal to Pro upon HCD. UVPD is less dependent on the method used to generate the low charge states and favors non-specific fragmentation, an outcome which is important for obtaining high sequence coverage of intact proteins.

Indexed as

AnimalsCattleHorsesHumansHydrogen-Ion ConcentrationIonsModels, MolecularOsmolar ConcentrationPhotolysisProtein CarbamylationProtein ConformationProtein DenaturationProtein FoldingProteinsProtonsSpectrometry, Mass, Electrospray IonizationIonsProteinsProtonsLow charge stateProteinTop-downUltraviolet photodissociation

Identifiers

PMID30796622
PMCPMC6447437
OpenAlexW2915560282

What OpenQuestion holds

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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.