Evidence map›Paper›PMID 32208662›Full record

ArticleAnalytical chemistry2020

Picoflow Liquid Chromatography-Mass Spectrometry for Ultrasensitive Bottom-Up Proteomics Using 2-μm-i.d. Open Tubular Columns.

Piliang Xiang, Ying Zhu, Yu Yang, Zhitao Zhao, Sarah M Williams, Ronald J Moore, Ryan T Kelly, Richard D Smith, Shaorong Liu

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
6.1field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  6. Review
  7. What's new in single-cell proteomics.Current opinion in biotechnology · 2024
    Review
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  16. Separation methods in single-cell proteomics: RPLC or CE?International journal of mass spectrometry · 2022
    Article
  17. Article
  18. Review
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  20. 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

9 authors at 3 institutions in 1 country.

Piliang XiangDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID 0000-0002-7742-7083
Ying ZhuEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0002-5416-0566
Yu YangDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Zhitao ZhaoDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Sarah M WilliamsEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99354, United States.
Ronald J MooreBiological Sciences Division, Pacific Northwest National Laboratory Rochester, Richland, Washington 99354, United States.ORCID 0000-0003-2806-2855
Ryan T KellyEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0002-3339-4443
Richard D SmithBiological Sciences Division, Pacific Northwest National Laboratory Rochester, Richland, Washington 99354, United States.
Shaorong LiuDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID 0000-0002-4602-0483
Pacific Northwest National Laboratory · USUniversity of Oklahoma · USBrigham Young University · US

Funding

Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
NIGMS NIH HHS P41 GM103493
6 · The paper itself

Abstract

In many areas of application, key objectives of chemical separation and analysis are to minimize the sample quantity while maximizing the chemical information obtained. Increasing measurement sensitivity is especially critical for proteomics research, especially when processing trace samples and where multiple measurements are desired. A rich collection of technologies has been developed, but the resulting sensitivity remains insufficient for achieving in-depth coverage of proteomic samples as small as single cells. Here, we combine picoliter-scale liquid chromatography (picoLC) with mass spectrometry (MS) to address this issue. The picoLC employs a 2-μm-i.d. open tubular column to reduce the sample input needed to greatly increase the sensitivity achieved using electrospray ionization (ESI) with MS. With this picoLC-MS system, we show that we can identify ∼1000 proteins reliably using only 75 pg of tryptic peptides, representing a 10-100-fold sensitivity improvement compared with the state-of-the-art liquid chromatography (LC) or capillary electrophoresis (CE)-MS methods. PicoLC-MS extends the limit of separation science and is expected to be a powerful tool for single cell proteomics.

Indexed as

ProteomicsChromatography, LiquidElectrophoresis, CapillaryHeLa CellsHumansMass SpectrometryParticle SizePeptidesSingle-Cell AnalysisSurface PropertiesPeptides

Identifiers

PMID32208662
PMCPMC7279521
OpenAlexW3013439422

What OpenQuestion holds

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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.