Evidence map›Paper›PMID 39356573›Full record

ArticleJournal of the American Society for Mass Spectrometry2024

Covalent Labeling Automated Data Analysis Platform for High Throughput in R (coADAPTr): A Proteome-Wide Data Analysis Platform for Covalent Labeling Experiments.

Raquel L Shortt, Lindsay K Pino, Emily E Chea, Carolina Rojas Ramirez, Daniel A Polasky, Alexey I Nesvizhskii, Lisa M Jones

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Raquel L ShorttDepartment of Pharmaceutical Sciences, University of Maryland, Baltimore, Maryland 21201, United States.
Lindsay K PinoTalus Bio, Seattle, Washington 98122, United States.ORCID 0000-0003-1857-7222
Emily E CheaGenNext Technologies, Half Moon Bay, California 94019, United States.
Carolina Rojas RamirezDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Daniel A PolaskyDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.ORCID 0000-0002-0515-1735
Alexey I NesvizhskiiDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.ORCID 0000-0002-2806-7819
Lisa M JonesDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093, United States.ORCID 0000-0001-8825-060X

Funding

COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
Michigan Center for Translational Cancer Proteogenomics-Diversity SupplementU24CA271037 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Saravana Mohan Dhanasekaran, Alexey I Nesvizhskii · 2022 to 2026
$4.4M
Protein Footprinting Coupled to Mass Spectrometry for the Study of Protein Higher Order Structure in Complex Model SystemsR35GM144324 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Lisa M Jones · 2022 to 2026
$3.0M
NCI NIH HHS U24 CA271037NIGMS NIH HHS R01 GM094231NIGMS NIH HHS R35 GM144324
6 · The paper itself

Abstract

Covalent labeling methods coupled to mass spectrometry have emerged in recent years for studying the higher order structure of proteins. Quantifying the extent of modification of proteins in multiple states (i.e., ligand free vs ligand-bound) can provide information on protein interaction sites and regions of conformational change. Though there are several software platforms that are used to quantify the extent of modification, the process can still be time-consuming, particularly for proteome-wide studies. Here, we present an open-source software for quantitation called Covalent labeling Automated Data Analysis Platform for high Throughput in R (coADAPTr). coADAPTr tackles the need for more efficient data analysis in covalent labeling mass spectrometry for techniques such as hydroxyl radical protein footprinting (HRPF). Traditional methods like Excel's Power Pivot (PP) are cumbersome and time-intensive, posing challenges for large-scale analyses. coADAPTr simplifies analysis by mimicking the functions used in the previous quantitation platform using PowerPivot in Microsoft Excel but with fewer steps, offering proteome-wide insights with enhanced graphical interpretations. Several features have been added to improve the fidelity and throughput compared to those of PowerPivot. These include filters to remove any duplicate data and the use of the arithmetic mean rather than the geometric mean for quantitation of the extent of modification. Validation studies confirm coADAPTr's accuracy and efficiency while processing data up to 200 times faster than conventional methods. Its open-source design and user-friendly interface make it accessible for researchers exploring intricate biological phenomena via HRPF and other covalent labeling MS methods. coADAPTr marks a significant leap in structural proteomics, providing a versatile and efficient platform for data interpretation. Its potential to transform the field lies in its seamless handling of proteome-wide data analyses, empowering researchers with a robust tool for deciphering complex structural biology data.

Indexed as

ProteomeProteomicsSoftwareData AnalysisHigh-Throughput Screening AssaysMass SpectrometryProtein FootprintingProteinsProteinsProteome

Identifiers

PMID39356573
PMCPMC11622367

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.