Evidence map›Paper›PMID 34493042›Full record

ReviewChemical reviews2022

Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.

Ellie I James, Taylor A Murphree, Clint Vorauer, John R Engen, Miklos Guttman

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
21.5field-weighted citation impact, top 1% 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

150 citing papers in PubMed, 291 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  15. Intrinsic Hydrogen-Deuterium Exchange Rates in HThe journal of physical chemistry. B · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  20. Article

90 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Ellie I JamesDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.
Taylor A MurphreeDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.
Clint VorauerDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.
John R EngenDepartment of Chemistry & Chemical Biology, Northeastern University, Boston, Massachusetts 02115, United States.
Miklos GuttmanDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.ORCID 0000-0003-2419-1334
University of Washington · USNortheastern University · US

Funding

Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Conformational Regulation and Therapeutic Targeting of Oncogenic KRASR01CA233978 · NCI · NORTHEASTERN UNIVERSITY · PI WALENSKY, LOREN DAVID, WALES, THOMAS EDWARD · 2020 to 2024
$2.4M
Mechanisms of IgM mediated activation of the complement systemR01AI153191 · NIAID · UNIVERSITY OF WASHINGTON · PI GUTTMAN, MIKLOS · 2021 to 2025
$2.4M
Hybrid structural mass spectrometry for rapid site-specific glycan structural elucidationR01GM127579 · NIGMS · UNIVERSITY OF WASHINGTON · PI GUTTMAN, MIKLOS · 2018 to 2021
$1.7M
NCI NIH HHS R01 CA233978NIAID NIH HHS R01 AI153191NIGMS NIH HHS R01 GM127579NIGMS NIH HHS T32 GM007750
6 · The paper itself

Abstract

Solution-phase hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) is a widespread tool for structural analysis across academia and the biopharmaceutical industry. By monitoring the exchangeability of backbone amide protons, HDX-MS can reveal information about higher-order structure and dynamics throughout a protein, can track protein folding pathways, map interaction sites, and assess conformational states of protein samples. The combination of the versatility of the hydrogen/deuterium exchange reaction with the sensitivity of mass spectrometry has enabled the study of extremely challenging protein systems, some of which cannot be suitably studied using other techniques. Improvements over the past three decades have continually increased throughput, robustness, and expanded the limits of what is feasible for HDX-MS investigations. To provide an overview for researchers seeking to utilize and derive the most from HDX-MS for protein structural analysis, we summarize the fundamental principles, basic methodology, strengths and weaknesses, and the established applications of HDX-MS while highlighting new developments and applications.

Indexed as

Deuterium Exchange MeasurementHydrogen Deuterium Exchange-Mass SpectrometryDeuteriumHydrogenMass SpectrometryProteinsDeuteriumHydrogenProteins

Identifiers

PMID34493042
PMCPMC9053315
OpenAlexW3197273087

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.