Evidence map›Paper›PMID 24968279›Full record

ArticleAnalytical chemistry2014

Effective protein separation by coupling hydrophobic interaction and reverse phase chromatography for top-down proteomics.

Lichen Xiu, Santosh G Valeja, Andrew J Alpert, Song Jin, Ying Ge

Abstract read
In one paragraph

Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.8field-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

32 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  7. Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023
    Article
  8. Review
  9. Article
  10. Review
  11. RPLC-RPLC-MS/MS for Proteoform Identification.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018
    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

5 authors at 1 institution in 1 country.

Lichen XiuDepartment of Chemistry, University of Wisconsin-Madison , Madison 53706, Wisconsin, United States.
Santosh G Valeja
Andrew J Alpert
Song Jin
Ying Ge
University of Wisconsin–Madison · US

Funding

Deciphering Myofilament Modifications in Ischemic CardiomyopathyR01HL109810 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2013 to 2024
$3.5M
Top Down Proteomics Of Myofilaments In Heart FailureR01HL096971 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2011 to 2021
$3.3M
Nanotechnology Enabled Top-Down PhosphoproteomicsR21EB013847 · NIBIB · UNIVERSITY OF WISCONSIN-MADISON · PI JIN, SONG · 2012 to 2013
$393k
NHLBI NIH HHS R01 HL096971NHLBI NIH HHS R01HL096971NHLBI NIH HHS R01 HL109810NHLBI NIH HHS R01HL109810NIBIB NIH HHS R21 EB013847NIBIB NIH HHS R21EB013847
6 · The paper itself

Abstract

One of the challenges in proteomics is the proteome's complexity, which necessitates the fractionation of proteins prior to the mass spectrometry (MS) analysis. Despite recent advances in top-down proteomics, separation of intact proteins remains challenging. Hydrophobic interaction chromatography (HIC) appears to be a promising method that provides high-resolution separation of intact proteins, but unfortunately the salts conventionally used for HIC are incompatible with MS. In this study, we have identified ammonium tartrate as a MS-compatible salt for HIC with comparable separation performance as the conventionally used ammonium sulfate. Furthermore, we found that the selectivity obtained with ammonium tartrate in the HIC mobile phases is orthogonal to that of reverse phase chromatography (RPC). By coupling HIC and RPC as a novel two-dimensional chromatographic method, we have achieved effective high-resolution intact protein separation as demonstrated with standard protein mixtures and a complex cell lysate. Subsequently, the separated intact proteins were identified by high-resolution top-down MS. For the first time, these results have shown the high potential of HIC as a high-resolution protein separation method for top-down proteomics.

Indexed as

ProteomicsAmino Acid SequenceChromatography, Reverse-PhaseHydrophobic and Hydrophilic InteractionsMass SpectrometryMolecular Sequence DataProteinsProteins

Identifiers

PMID24968279
PMCPMC4144745
OpenAlexW2331244870

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.