Evidence map›Paper›PMID 39481095›Full record

ReviewChemical reviews2024

Computational Tools for Hydrogen-Deuterium Exchange Mass Spectrometry Data Analysis.

Michele Stofella, Antonio Grimaldi, Jochem H Smit, Jürgen Claesen, Emanuele Paci, Frank Sobott

Abstract readReview
In one paragraph

Review in Chemical reviews, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Intrinsic Hydrogen-Deuterium Exchange Rates in HThe journal of physical chemistry. B · 2026
    Article
  8. Article
  9. Review
  10. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  11. Article
  12. A framework for automated multimodal HDX-MS analysis.bioRxiv : the preprint server for biology · 2025
    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

6 authors.

Michele StofellaSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0002-4533-1319
Antonio GrimaldiDipartimento di Fisica e Astronomia, Universita' di Bologna, 40127 Bologna, Italy.
Jochem H SmitDepartment of Microbiology and Immunology, Rega Institute for Medical Research, Laboratory of Molecular Bacteriology, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0002-3597-9429
Jürgen ClaesenEpidemiology and Data Science, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands.ORCID 0000-0001-7615-5322
Emanuele PaciDipartimento di Fisica e Astronomia, Universita' di Bologna, 40127 Bologna, Italy.ORCID 0000-0002-4891-2768
Frank SobottSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0001-9029-1865

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrogen-deuterium exchange (HDX) has become a pivotal method for investigating the structural and dynamic properties of proteins. The versatility and sensitivity of mass spectrometry (MS) made the technique the ideal companion for HDX, and today HDX-MS is addressing a growing number of applications in both academic research and industrial settings. The prolific generation of experimental data has spurred the concurrent development of numerous computational tools, designed to automate parts of the workflow while employing different strategies to achieve common objectives. Various computational methods are available to perform automated peptide searches and identification; different statistical tests have been implemented to quantify differences in the exchange pattern between two or more experimental conditions; alternative strategies have been developed to deconvolve and analyze peptides showing multimodal behavior; and different algorithms have been proposed to computationally increase the resolution of HDX-MS data, with the ultimate aim to provide information at the level of the single residue. This review delves into a comprehensive examination of the merits and drawbacks associated with the diverse strategies implemented by software tools for the analysis of HDX-MS data.

Indexed as

Hydrogen Deuterium Exchange-Mass SpectrometryAlgorithmsData AnalysisDeuterium Exchange MeasurementMass SpectrometryPeptidesProteinsSoftwarePeptidesProteins

Identifiers

PMID39481095
PMCPMC11565574

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.