Evidence map›Paper›PMID 41811792›Full record

ArticleJournal of the American Society for Mass Spectrometry2026

Data-Independent Acquisition (DIA) Strategy for Measuring Protein Stability Using Stability of Proteins from Rates of Oxidation (SPROX).

Natalie M Labbe, Meghan K Virani, Michael C Fitzgerald

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Natalie M LabbeDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.ORCID 0000-0002-7798-5712
Meghan K ViraniDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.
Michael C FitzgeraldDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.ORCID 0000-0002-6719-4722

Funding

Chemical Biology Strategies to Resolve Plasmodium Heat Shock Protein FunctionR01AI173295 · NIAID · DUKE UNIVERSITY · PI Emily R Derbyshire · 2023 to 2026
$2.1M
NIAID NIH HHS R01 AI173295
6 · The paper itself

Abstract

The stability of proteins from the rates of oxidation (SPROX) technique is a mass spectrometry-based approach for making protein folding stability measurements on the proteomic scale. The development and application of SPROX, to date, have primarily relied on the use of quantitative bottom-up proteomics and data-dependent acquisition (DDA) strategies using isobaric mass tags. Use of isobaric mass tags is attractive, as it enables the mass spectrometry readout in SPROX to be highly multiplexed. However, the use of such isobaric mass tags is restricted to DDA strategies, which can be limited in their proteomic coverage compared with data-independent acquisition (DIA) strategies. Reported here is a new "one-pot" SPROX workflow that employs a DIA readout and a label-free quantification strategy. Analysis of the proteins in an

Indexed as

Mass SpectrometryProteinsProteomicsCyclosporineEscherichia coliEscherichia coli ProteinsOxidation-ReductionProtein StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCyclosporineEscherichia coli ProteinsProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID41811792
PMCPMC13047670

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Registered trials

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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.