Evidence map›Paper›PMID 26307715›Full record

ArticleEuropean journal of mass spectrometry (Chichester, England)2015

Integration of electrochemistry with ultra-performance liquid chromatography/mass spectrometry.

Yi Cai, Qiuling Zheng, Yong Liu, Roy Helmy, Joseph A Loo, Hao Chen

Open access · greenAbstract read
In one paragraph

Article in European journal of mass spectrometry (Chichester, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Electrochemical andJournal of pharmaceutical analysis · 2020
    Article
  3. Article
  4. Article
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

6 authors at 3 institutions in 1 country.

Yi CaiCenter for Intelligent Chemical Instrumentation, Department of Chemistry and Biochemistry, Edison Biotechnology Institute, Ohio University, Athens, OH, 45701 USA. yc816211@ohio.edu.
Qiuling ZhengCenter for Intelligent Chemical Instrumentation, Department of Chemistry and Biochemistry, Edison Biotechnology Institute, Ohio University, Athens, OH, 45701 USA. qz320511@ohio.edu.
Yong LiuDepartment of Analytical Chemistry, Merck Research Laboratories, Merck & Co., Inc., Rahway, NJ 07065, USA. yong_liu2@merck.com.
Roy HelmyDepartment of Analytical Chemistry, Merck Research Laboratories, Merck & Co., Inc., Rahway, NJ 07065, USA. roy_helmy@merck.com.
Joseph A LooDep artment of Chemistry and Biochemistry, Department of Biological Chemistry, David Geffen School of Medicine at UCLA, and UCLA/DOE Institute for Genomics and Proteomics, University of California-Los Angeles, Los Angeles, CA 90095, USA. roger.giles@srlab.co.uk.
Hao ChenCenter for Intelligent Chemical Instrumentation, Department of Chemistry and Biochemistry, Edison Biotechnology Institute, Ohio University, Athens, OH, 45701 USA. chenh2@ohio.edu.
Ohio University · USMerck & Co., Inc., Rahway, NJ, USA (United States) · USUniversity of California, Los Angeles · US

Funding

UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
NIGMS NIH HHS R01 GM103479NIGMS NIH HHS R01GM103479
6 · The paper itself

Abstract

This study presents the development of ultra-performance liquid chromatography (UPLC) mass spectrometry (MS) combined with electrochemistry (EC) for the first time and its application for the structural analysis of proteins/peptides that contain disulfide bonds. In our approach, a protein/peptide mixture sample undergoes a fast UPLC separation and subsequent electrochemical reduction in an electrochemical flow cell followed by online MS and tandem mass spectrometry (MS/MS) analyses. The electrochemical cell is coupled to the mass spectrometer using our recently developed desorption electrospray ionization (DESI) interface. Using this UPLC/EC/DESI-MS method, peptides that contain disulfide bonds can be differentiated from those without disulfide bonds, as the former are electroactive and reducible. MS/MS analysis of the disulfide-reduced peptide ions provides increased information on the sequence and disulfide-linkage pattern. In a reactive DESI- MS detection experiment in which a supercharging reagent was used to dope the DESI spray solvent, increased charging was obtained for the UPLC-separated proteins. Strikingly, upon online electrolytic reduction, supercharged proteins (e.g., α-lactalbumin) showed even higher charging, which will be useful in top- down protein structure MS analysis as increased charges are known to promote protein ion dissociation. Also, the separation speed and sensitivity are enhanced by approximately 1(~)2 orders of magnitude by using UPLC for the liquid chromatography (LC)/EC/MS platform, in comparison to the previously used high- performance liquid chromatography (HPLC). This UPLC/EC/DESI-MS method combines the power of fast UPLC separation, fast electrochemical conversion, and online MS structural analysis for a potentially valuable tool for proteomics research and bioanalysis.

Indexed as

Chromatography, High Pressure LiquidElectrochemistryEquipment DesignEquipment Failure AnalysisProteinsReproducibility of ResultsSensitivity and SpecificitySpectrometry, Mass, Electrospray IonizationSystems IntegrationProteins

Identifiers

PMID26307715
PMCPMC4552337
OpenAlexW1947038424

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.