Evidence map›Paper›PMID 21329427›Full record

ReviewExpert review of proteomics2011

Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions.

Michael J Chalmers, Scott A Busby, Bruce D Pascal, Graham M West, Patrick R Griffin

Open access · greenAbstract readReview
In one paragraph

Review in Expert review of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
9.2field-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

128 citing papers in PubMed, 260 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS.Protein science : a publication of the Protein Society · 2025
    Article
  9. Mechanism of allosteric activation in human mitochondrial ClpP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. MgbioRxiv : the preprint server for biology · 2024
    Article
  19. Interpretation of Hydrogen/Deuterium Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  20. Article

68 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 1 institution in 1 country.

Michael J ChalmersThe Scripps Research Molecular Screening Center, The Scripps Research Institute, Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, USA.
Scott A Busby
Bruce D Pascal
Graham M West
Patrick R Griffin
Scripps Research Institute · US

Funding

Scripps Research Institute Molecular Screen Center(RMI)U54MH074404 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI ROSEN, HUGH · 2005 to 2007
$11.6M
Development of H/D exchange technology for the study of large protein complexesR01GM084041 · NIGMS · SCRIPPS FLORIDA · PI GRIFFIN, PATRICK ROBERT · 2009 to 2012
$1.6M
Acquisition of a LTQ/Orbitrap MS to advance the study of protein dynamicsS10RR027270 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI GRIFFIN, PATRICK ROBERT · 2010 to 2010
$500k
Intramural NIH HHSNCRR NIH HHS S10 RR027270NIGMS NIH HHS R01 GM084041NIGMS NIH HHS R01-GM084041NIMH NIH HHS U54 MH074404NIMH NIH HHS U54-MH074404
6 · The paper itself

Abstract

Functional regulation of ligand-activated receptors is driven by alterations in the conformational dynamics of the protein upon ligand binding. Differential hydrogen/deuterium exchange (HDX) coupled with mass spectrometry has emerged as a rapid and sensitive approach for characterization of perturbations in conformational dynamics of proteins following ligand binding. While this technique is sensitive to detecting ligand interactions and alterations in receptor dynamics, it also can provide important mechanistic insights into ligand regulation. For example, HDX has been used to determine a novel mechanism of ligand activation of the nuclear receptor peroxisome proliferator activated receptor-γ, perform detailed analyses of binding modes of ligands within the ligand-binding pocket of two estrogen receptor isoforms, providing insight into selectivity, and helped classify different types of estrogen receptor-α ligands by correlating their pharmacology with the way they interact with the receptor based solely on hierarchical clustering of receptor HDX signatures. Beyond small-molecule-receptor interactions, this technique has also been applied to study protein-protein complexes, such as mapping antibody-antigen interactions. In this article, we summarize the current state of the differential HDX approaches and the future outlook. We summarize how HDX analysis of protein-ligand interactions has had an impact on biology and drug discovery.

Indexed as

AnimalsDeuterium Exchange MeasurementHormonesHumansHydrogenLigandsMass SpectrometryModels, MolecularProtein BindingProtein ConformationProtein KinasesProteinsProtein Structure, TertiaryReceptors, Cell SurfaceReceptors, Cytoplasmic and NuclearHormonesHydrogenLigandsProtein KinasesProteinsReceptors, Cell SurfaceReceptors, Cytoplasmic and Nuclear

Identifiers

PMID21329427
PMCPMC3113475
OpenAlexW2066736637

What OpenQuestion holds

Textmetadata
LicenceTDM
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.