Evidence map›Paper›PMID 30226781›Full record

ArticleJournal of proteome research2018

Increasing the Separation Capacity of Intact Histone Proteoforms Chromatography Coupling Online Weak Cation Exchange-HILIC to Reversed Phase LC UVPD-HRMS.

Andrea F G Gargano, Jared B Shaw, Mowei Zhou, Christopher S Wilkins, Thomas L Fillmore, Ronald J Moore, Govert W Somsen, Ljiljana Paša-Tolić

Abstract read
In one paragraph

Article in Journal of proteome research, 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023
    Article
  8. Article
  9. Article
  10. Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

8 authors.

Andrea F G GarganoCenter for Analytical Sciences Amsterdam , Science Park 904 , 1098 XH Amsterdam , The Netherlands.ORCID 0000-0003-3361-7341
Jared B ShawEnvironmental Molecular Sciences Laboratory , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.ORCID 0000-0002-1130-1728
Mowei ZhouEnvironmental Molecular Sciences Laboratory , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.ORCID 0000-0003-3575-3224
Christopher S WilkinsBiological Sciences Division , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.
Thomas L FillmoreBiological Sciences Division , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.
Ronald J MooreBiological Sciences Division , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.
Govert W SomsenCenter for Analytical Sciences Amsterdam , Science Park 904 , 1098 XH Amsterdam , The Netherlands.
Ljiljana Paša-TolićEnvironmental Molecular Sciences Laboratory , Pacific Northwest National Laboratory , P.O. Box 999, Richland , Washington 99352 , United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Top-down proteomics is an emerging analytical strategy to characterize combinatorial protein post-translational modifications (PTMs). However, sample complexity and small mass differences between chemically closely related proteoforms often limit the resolution attainable by separations employing a single liquid chromatographic (LC) principle. In particular, for ultramodified proteins like histones, extensive and time-consuming fractionation is needed to achieve deep proteoform coverage. Herein, we present the first online nanoflow comprehensive two-dimensional liquid chromatography (nLC×LC) platform top-down mass spectrometry analysis of histone proteoforms. The described two-dimensional LC system combines weak cation exchange chromatography under hydrophilic interaction LC conditions (i.e., charge- and hydrophilicity-based separation) with reversed phase liquid chromatography (i.e., hydrophobicity-based separation). The two independent chemical selectivities were run at nanoflows (300 nL/min) and coupled online with high-resolution mass spectrometry employing ultraviolet photodissociation (UVPD-HRMS). The nLC×LC workflow increased the number of intact protein masses observable relative to one-dimensional approaches and allowed characterization of hundreds of proteoforms starting from limited sample quantities (∼1.5 μg).

Indexed as

Protein Processing, Post-TranslationalChromatography, Ion ExchangeChromatography, Reverse-PhaseComplex MixturesHeLa CellsHistonesHumansHydrophobic and Hydrophilic InteractionsProteomicsSpectrophotometry, UltravioletStatic ElectricityTandem Mass SpectrometryComplex MixturesHistoneshistonesonline comprehensive two-dimensional liquid chromatographypost-translational modificationstop-down mass spectrometryultraviolet photodissociation

Identifiers

PMID30226781
PMCPMC6220366

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.