Evidence map›Paper›PMID 30624053›Full record

ArticleAnalytical chemistry2019

Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Large-Scale Phosphoproteomics with the Production of over 11,000 Phosphopeptides from the Colon Carcinoma HCT116 Cell Line.

Daoyang Chen, Katelyn R Ludwig, Oleg V Krokhin, Vic Spicer, Zhichang Yang, Xiaojing Shen, Amanda B Hummon, Liangliang Sun

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

Daoyang ChenDepartment of Chemistry , Michigan State University , 578 South Shaw Lane , East Lansing , Michigan 48824 , United States.
Katelyn R LudwigDepartment of Chemistry and Biochemistry , University of Notre Dame , Notre Dame , Indiana 46556 , United States.
Vic Spicer
Zhichang YangDepartment of Chemistry , Michigan State University , 578 South Shaw Lane , East Lansing , Michigan 48824 , United States.
Xiaojing ShenDepartment of Chemistry , Michigan State University , 578 South Shaw Lane , East Lansing , Michigan 48824 , United States.ORCID 0000-0003-2079-9115
Amanda B HummonDepartment of Chemistry and Biochemistry, Comprehensive Cancer Center , The Ohio State University , 414 Biomedical Research Tower , Columbus , Ohio 43201 , United States.ORCID 0000-0002-1969-9013
Liangliang SunDepartment of Chemistry , Michigan State University , 578 South Shaw Lane , East Lansing , Michigan 48824 , United States.ORCID 0000-0001-8939-5042
Michigan State University · USUniversity of Manitoba · CAThe Ohio State University · USUniversity 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
Quantitative proteomics of Zebrafish embryos and blastomeresR01GM125991 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SUN, LIANGLIANG · 2018 to 2022
$1.7M
NIGMS NIH HHS R01 GM110406NIGMS NIH HHS R01 GM125991
6 · The paper itself

Abstract

Phosphoproteomics requires better separation of phosphopeptides to boost the coverage of the phosphoproteome. We argue that an alternative separation method that produces orthogonal phosphopeptide separation to the widely used LC needs to be considered. Capillary zone electrophoresis (CZE) is one important alternative because CZE and LC are orthogonal for phosphopeptide separation and because the migration time of peptides in CZE can be accurately predicted. In this work, we coupled strong cation exchange (SCX)-reversed-phase LC (RPLC) to CZE-MS/MS for large-scale phosphoproteomics of the colon carcinoma HCT116 cell line. The CZE-MS/MS-based platform identified 11,555 phosphopeptides. The phosphopeptide data set is at least 100% larger than that from previous CZE-MS/MS studies and will be a valuable resource for building a model for predicting the migration time of phosphopeptides in CZE. Phosphopeptides migrate significantly slower than corresponding unphosphopeptides under acidic conditions of CZE separations and in a normal polarity. According to our modeling data, phosphorylation decreases peptide's charge roughly by one charge unit, resulting in dramatic decrease in electrophoretic mobility. Preliminary investigations demonstrate that electrophoretic mobility of phosphopeptides containing one phosphoryl group can be predicted with the same accuracy as for nonmodified peptides ( R

Indexed as

Amino Acid SequenceChromatography, Reverse-PhaseElectrophoresis, CapillaryHCT116 CellsHumansPhosphopeptidesProteomeProteomicsTandem Mass SpectrometryPhosphopeptidesProteome

Identifiers

PMID30624053
PMCPMC6506858
OpenAlexW2909907179

What OpenQuestion holds

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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.