Evidence map›Paper›PMID 32031398›Full record

ArticleJournal of the American Society for Mass Spectrometry2020

Comparative Analysis of Mass-Spectrometry-Based Proteomic Methods for Protein Target Discovery Using a One-Pot Approach.

Aurora Cabrera, Nancy Wiebelhaus, Baiyi Quan, Renze Ma, He Meng, Michael C Fitzgerald

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026
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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

6 authors at 1 institution in 1 country.

Aurora CabreraDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Nancy WiebelhausDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Baiyi QuanDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Renze MaDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
He MengDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.
Michael C FitzgeraldDepartment of Chemistry , Duke University , Durham , North Carolina 27708 , United States.ORCID http://orcid.org/0000-0002-6719-4722
Duke University · US

Funding

Anti-Malarial Drug Target Discovery using Energetics-Based Proteomics MethodsR21AI130406 · NIAID · DUKE UNIVERSITY · PI FITZGERALD, MICHAEL C · 2018 to 2019
$420k
NIAID NIH HHS R21 AI130406
6 · The paper itself

Abstract

Recently, several mass-spectrometry- and protein-denaturation-based proteomic methods have been developed to facilitate protein target discovery efforts in drug mode-of-action studies. These methods, which include the stability of proteins from rates of oxidation (SPROX), pulse proteolysis (PP), chemical denaturation and protein precipitation (CPP), and thermal proteome profiling (TPP) techniques, have been used in an increasing number of applications in recent years. However, while the advantages and disadvantages to using these different techniques have been reviewed, the analytical characteristics of these methods have not been directly compared. Reported here is such a direct comparison using the well-studied immunosuppressive drug, cyclosporine A (CsA), and the proteins in a yeast cell lysate. Also described is a one-pot strategy that can be utilized with each technique to streamline data acquisition and analysis. We find that there are benefits to utilizing all four strategies for protein target discovery including increased proteomic coverage and reduced false positive rates that approach 0%. Moreover, the one-pot strategy described here makes such an experiment feasible, because of the 10-fold reduction in reagent costs and instrument time it affords.

Indexed as

CyclosporineDrug DevelopmentFungal ProteinsMass SpectrometryOxidation-ReductionProtein DenaturationProtein StabilityProteolysisProteomeProteomicsCyclosporineFungal ProteinsProteomechemical denaturationmode-of-actionprotein foldingthermal denaturationthermodynamics

Identifiers

PMID32031398
PMCPMC7441748
OpenAlexW2990725998

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.