Evidence map›Paper›PMID 26745641›Full record

ArticleEndocrinology2016

SNaPP: Simplified Nanoproteomics Platform for Reproducible Global Proteomic Analysis of Nanogram Protein Quantities.

Eric L Huang, Paul D Piehowski, Daniel J Orton, Ronald J Moore, Wei-Jun Qian, Cameron P Casey, Xiaofei Sun, Sudhansu K Dey, Kristin E Burnum-Johnson, Richard D Smith

Open access · bronzeAbstract read
In one paragraph

Article in Endocrinology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.5field-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

33 citing papers in PubMed, 49 citations in OpenAlex.

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  12. Single-cell Proteomics: Progress and Prospects.Molecular & cellular proteomics : MCP · 2020
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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

10 authors at 2 institutions in 1 country.

Eric L HuangPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Paul D PiehowskiPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Daniel J OrtonPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Ronald J MoorePacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Wei-Jun QianPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Cameron P CaseyPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Xiaofei SunPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Sudhansu K DeyPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Kristin E Burnum-JohnsonPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Richard D SmithPacific Northwest National Laboratory (E.L.H., P.D.P., D.J.O., R.J.M., W.-J.Q., C.P.C., K.E.B.-J., R.D.S.), Richland, Washington 99352; and Cincinnati Children's Hospital Medical Center (X.S., S.K.D.), Cincinnati, Ohio 45229.
Pacific Northwest National Laboratory · USCincinnati Children's Hospital Medical Center · 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
Molecular signaling in uterine receptivity to implantationR01HD068524 · NICHD · CINCINNATI CHILDRENS HOSP MED CTR · PI Xiaofei Sun · 2011 to 2026
$5.3M
NICHD NIH HHS R01 HD068524NICHD NIH HHS R01HD068524NIGMS NIH HHS P41 GM103493NIGMS NIH HHS P41GM103493
6 · The paper itself

Abstract

Global proteomic analyses of complex protein samples in nanogram quantities require a fastidious approach to achieve in-depth protein coverage and quantitative reproducibility. Biological samples are often severely mass limited and can preclude the application of more robust bulk sample processing workflows. In this study, we present a system that minimizes sample handling by using online immobilized trypsin digestion and solid phase extraction to create a simple, sensitive, robust, and reproducible platform for the analysis of nanogram-size proteomic samples. To demonstrate the effectiveness of our simplified nanoproteomics platform, we used the system to analyze preimplantation blastocysts collected on day 4 of pregnancy by flushing the uterine horns with saline. For each of our three sample groups, blastocysts were pooled from three mice resulting in 22, 22, and 25 blastocysts, respectively. The resulting proteomic data provide novel insight into mouse blastocyst protein expression on day 4 of normal pregnancy because we characterized 348 proteins that were identified in at least two sample groups, including 59 enzymes and blastocyst specific proteins (eg, zona pellucida proteins). This technology represents an important advance in which future studies could perform global proteomic analyses of blastocysts obtained from an individual mouse, thereby enabling researchers to investigate interindividual variation as well as increase the statistical power without increasing animal numbers. This approach is also easily adaptable to other mass-limited sample types.

Indexed as

AnimalsBlastocystEnzymes, ImmobilizedFemaleMass SpectrometryMiceNanotechnologyPregnancyProteinsProteomicsReproducibility of ResultsTandem Mass SpectrometryEnzymes, ImmobilizedProteins

Identifiers

PMID26745641
PMCPMC4769369
OpenAlexW2229366407

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.