Evidence map›Paper›PMID 27876348›Full record

ArticleJournal of chromatography. A2016

Characterization of an immobilized enzyme reactor for on-line protein digestion.

Stephanie Moore, Stephanie Hess, James Jorgenson

Abstract read
In one paragraph

Article in Journal of chromatography. A, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 33 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

3 authors at 1 institution in 1 country.

Stephanie MooreChemistry Department, University of North Carolina at Chapel Hill, NC 27599, United States.
Stephanie HessChemistry Department, University of North Carolina at Chapel Hill, NC 27599, United States.
James JorgensonChemistry Department, University of North Carolina at Chapel Hill, NC 27599, United States. Electronic address: jj@unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Statistics and Bioinformatics Core - WangU24DK097153 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BURANT, CHARLES F · 2012 to 2017
$10.1M
High Resolution MetabolomicsR01DK101473 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KENNEDY, ROBERT T · 2015 to 2018
$1000k
NIDDK NIH HHS R01 DK101473NIDDK NIH HHS U24 DK097153
6 · The paper itself

Abstract

Despite the developments for faster liquid chromatographic and mass spectral detection techniques, the standard in-solution protein digestion for proteomic analyses has remained relatively unchanged. The typical in-solution trypsin protein digestion is usually the slowest part of the workflow, albeit one of the most important. The development of a highly efficient immobilized enzyme reactor (IMER) with rapid performance for on-line protein digestion would greatly decrease the analysis time involved in a proteomic workflow. Presented here is the development of a silica based IMER for on-line protein digestion, which produced rapid digestions in the presence of organic mobile phase for both model proteins and a complex sample consisting of the insoluble portion of a yeast cell lysate. Protein sequence coverage and identifications evaluated between the IMER and in-solution digestions were comparable. Overall, for a yeast cell lysate with only a 10s volumetric residence time on-column, the IMER identified 507 proteins while the in-solution digestion identified 490. There were no significant differences observed based on identified protein's molecular weight or isoelectric point between the two digestion methods. Implementation of the IMER into the proteomic workflow provided similar protein identification results, automation for sample analysis, and reduced the analysis time by 15h.

Indexed as

Enzymes, ImmobilizedProteolysisTrypsinChromatography, High Pressure LiquidMass SpectrometryProteomicsSaccharomyces cerevisiae ProteinsSequence Analysis, ProteinEnzymes, ImmobilizedSaccharomyces cerevisiae ProteinsTrypsinDigestionIMERImmobilized enzymeMembrane proteinsTrypsin

Identifiers

PMID27876348
PMCPMC5136339
OpenAlexW2550575357

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.