Evidence map›Paper›PMID 31664819›Full record

ArticleAnalytical chemistry2019

Synergistic Structural Information from Covalent Labeling and Hydrogen-Deuterium Exchange Mass Spectrometry for Protein-Ligand Interactions.

Tianying Liu, Patanachai Limpikirati, Richard W Vachet

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Diethylpyrocarbonate Footprints a Membrane Protein in Micelles.Journal of the American Society for Mass Spectrometry · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 1 institution in 1 country.

Tianying LiuDepartment of Chemistry , University of Massachusetts , Amherst , Massachusetts 01003 , United States.
Patanachai LimpikiratiDepartment of Chemistry , University of Massachusetts , Amherst , Massachusetts 01003 , United States.ORCID 0000-0001-7708-4415
Richard W VachetDepartment of Chemistry , University of Massachusetts , Amherst , Massachusetts 01003 , United States.ORCID 0000-0003-4514-0210
University of Massachusetts Amherst · US

Funding

Copper-Induced Amyloidosis Studied by Mass SpectrometryR01GM075092 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI VACHET, RICHARD W · 2005 to 2020
$4.0M
Acquisition of an Orbitrap MSS10OD010645 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI EYLES, STEPHEN J. · 2013 to 2013
$600k
NIGMS NIH HHS R01 GM075092NIH HHS S10 OD010645
6 · The paper itself

Abstract

Hydrogen-deuterium exchange (HDX) mass spectrometry (MS) and covalent labeling (CL) MS are typically considered to be complementary methods for protein structural analysis, because one probes the protein backbone, while the other probes side chains. For protein-ligand interactions, we demonstrate in this work that the two labeling techniques can provide synergistic structural information about protein-ligand binding when reagents like diethylpyrocarbonate (DEPC) are used for CL because of the differences in the reaction rates of DEPC and HDX. Using three model protein-ligand systems, we show that the slower time scale for DEPC labeling makes it only sensitive to changes in solvent accessibility and insensitive to changes in protein structural fluctuations, whereas HDX is sensitive to changes in both solvent accessibility and structural fluctuations. When used together, the two methods more clearly reveal binding sites and ligand-induced changes to structural fluctuations that are distant from the binding site, which is more comprehensive information than either technique alone can provide. We predict that these two methods will find widespread usage together for more deeply understanding protein-ligand interactions.

Indexed as

Hydrogen Deuterium Exchange-Mass SpectrometryDiethyl PyrocarbonateLigandsModels, MolecularProteinsDiethyl PyrocarbonateLigandsProteins

Identifiers

PMID31664819
PMCPMC6891134
OpenAlexW2982584626

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.