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HaDeX: an R Package and Web-server for Analysis of Data from Hydrogen-deuterium Exchange Mass Spectrometry Experiments

Overview
Journal Bioinformatics
Specialty Biology
Date 2020 Jun 25
PMID 32579220
Citations 11
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Abstract

Motivation: Hydrogen-deuterium mass spectrometry (HDX-MS) is a rapidly developing technique for monitoring dynamics and interactions of proteins. The development of new devices has to be followed with new software suites addressing emerging standards in data analysis.

Results: We propose HaDeX, a novel tool for processing, analysis and visualization of HDX-MS experiments. HaDeX supports a reproducible analytical process, including data exploration, quality control and generation of publication-quality figures.

Availability And Implementation: HaDeX is available primarily as a web-server (http://mslab-ibb.pl/shiny/HaDeX/), but its all functionalities are also accessible as the R package (https://CRAN.R-project.org/package=HaDeX) and standalone software (https://sourceforge.net/projects/HaDeX/).

Supplementary Information: Supplementary data are available at Bioinformatics online.

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References
1.
Woods Jr V, Hamuro Y . High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: utility in pharmaceutical design. J Cell Biochem Suppl. 2002; Suppl 37:89-98. DOI: 10.1002/jcb.10069. View

2.
Houde D, Berkowitz S, Engen J . The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J Pharm Sci. 2011; 100(6):2071-86. PMC: 3164548. DOI: 10.1002/jps.22432. View

3.
Konermann L, Pan J, Liu Y . Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev. 2010; 40(3):1224-34. DOI: 10.1039/c0cs00113a. View

4.
Lau A, Ahdash Z, Martens C, Politis A . Deuteros: software for rapid analysis and visualization of data from differential hydrogen deuterium exchange-mass spectrometry. Bioinformatics. 2019; 35(17):3171-3173. PMC: 6736138. DOI: 10.1093/bioinformatics/btz022. View

5.
Claesen J, Burzykowski T . Computational methods and challenges in hydrogen/deuterium exchange mass spectrometry. Mass Spectrom Rev. 2016; 36(5):649-667. DOI: 10.1002/mas.21519. View