Evidence map›Paper›PMID 26399161›Full record

ArticleAnalytical chemistry2015

Over 2300 phosphorylated peptide identifications with single-shot capillary zone electrophoresis-tandem mass spectrometry in a 100 min separation.

Katelyn R Ludwig, Liangliang Sun, Guijie Zhu, Norman J Dovichi, Amanda B Hummon

Abstract read
In one paragraph

Article in Analytical chemistry, 2015. 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
5.1field-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, 56 citations in OpenAlex.

  1. Article
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  5. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
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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.

Katelyn R LudwigDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Liangliang SunDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Guijie ZhuDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Norman J DovichiDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Amanda B HummonDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
University of Notre Dame · US

Funding

Spatial SILAC: Examining the Proteome in 3D Cell CulturesR01GM110406 · NIGMS · UNIVERSITY OF NOTRE DAME · PI HUMMON, AMANDA B. · 2014 to 2022
$3.0M
Technology for single cell proteomics and its application to the analysis of single Xenopus blastomeresR01GM096767 · NIGMS · UNIVERSITY OF NOTRE DAME · PI DOVICHI, NORMAN J · 2011 to 2019
$2.5M
NIGMS NIH HHS R01 GM096767NIGMS NIH HHS R01GM096767NIGMS NIH HHS R01 GM110406NIGMS NIH HHS R01GM110406
6 · The paper itself

Abstract

Ultraperformance liquid chromatography (UPLC)-electrospray ionization (ESI)-tandem mass spectrometry (MS/MS) is typically employed for phosphoproteome analysis. Alternatively, capillary zone electrophoresis (CZE)-ESI-MS/MS has great potential for phosphoproteome analysis due to the significantly different migration times of phosphorylated and unphosphorylated forms of peptides. In this work, we systematically compared UPLC-MS/MS and CZE-MS/MS for phosphorylated peptide identifications (IDs) using an enriched phosphoproteome from the MCF-10A cell line. When the sample loading amount of UPLC was 10 times higher than that of CZE (2 μg vs 200 ng), UPLC generated more phosphorylated peptide IDs than CZE (3313 vs 1783). However, when the same sample loading amounts were used for CZE and UPLC (2-200 ng), CZE-MS/MS consistently and significantly outperformed UPLC-MS/MS in terms of phosphorylated peptide and total peptide IDs. This superior performance is most likely due to the higher peptide intensity generated by CZE-MS/MS. More importantly, compared with UPLC data from a 2 μg sample, CZE-MS/MS can identify over 500 unique phosphorylated peptides from a 200 ng sample, suggesting that CZE and UPLC are complementary for phosphorylated peptide IDs. With further improved loading capacity via a dynamic pH junction method, 2313 phosphorylated peptides were identified with single-shot CZE-MS/MS in a 100 min analysis. This number of phosphorylated peptide IDs is over 1 order of magnitude higher than the number of phosphorylated peptide IDs previously reported by single-shot CZE-MS/MS.

Indexed as

Tandem Mass SpectrometryCell Line, TumorChromatography, High Pressure LiquidElectrophoresis, CapillaryHumansPeptidesPhosphorylationPeptides

Identifiers

PMID26399161
PMCPMC4605816
OpenAlexW2298101292

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.