Evidence map›Paper›PMID 33886284›Full record

ArticleJournal of the American Society for Mass Spectrometry2021

Complementary Structural Information for Stressed Antibodies from Hydrogen-Deuterium Exchange and Covalent Labeling Mass Spectrometry.

Catherine Y Tremblay, Patanachai Limpikirati, Richard W Vachet

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  3. Article
  4. Hybrid Mass Spectrometry Applied across the Production of Antibody Biotherapeutics.Journal of the American Society for Mass Spectrometry · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. 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.

Catherine Y TremblayDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, United States.
Patanachai LimpikiratiDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, United States.
Richard W VachetDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, United States.ORCID http://orcid.org/0000-0003-4514-0210
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
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
Higher Order Structure Analysis of Protein Therapeutics by Covalent Labeling MSR43GM116211 · NIGMS · RECLAIM PHARMACEUTICAL WASTE MANAGEMENT · PI GRABAN, ERIC · 2016 to 2016
$277k
NIGMS NIH HHS R01 GM075092NIGMS NIH HHS R43 GM116211NIGMS NIH HHS T32 GM008515NIH HHS S10 OD010645
6 · The paper itself

Abstract

Identifying changes in the higher-order structure (HOS) of therapeutic monoclonal antibodies upon storage, stress, or mishandling is important for ensuring efficacy and avoiding adverse effects. Here, we demonstrate diethylpyrocarbonate (DEPC)-based covalent labeling (CL) mass spectrometry (MS) and hydrogen-deuterium exchange (HDX)/MS can be used together to provide site-specific information about subtle conformational changes that are undetectable by traditional techniques. Using heat-stressed rituximab as a model protein, we demonstrate that CL/MS is more sensitive than HDX/MS to subtle HOS structural changes under low stress conditions (e.g., 45 and 55 °C for 4 h). At higher heat stress (65 °C for 4 h), we find CL/MS and HDX/MS provide complementary information, as CL/MS reports on changes in side chain orientation while HDX/MS reveals changes in backbone dynamics. More interestingly, we demonstrate that the two techniques work synergistically to identify likely aggregation sites in the heat-stressed protein. In particular, the C

Indexed as

AntibodiesDeuterium Exchange MeasurementDiethyl PyrocarbonateHot TemperatureHydrogen Deuterium Exchange-Mass SpectrometryProtein DomainsRituximabSolventsTime FactorsAntibodiesDiethyl PyrocarbonateRituximabSolventsAntibody therapeuticsCovalent labelingDiethylpyrocarbonateHydrogen/deuterium exchangeMass spectrometryProtein higher-order structureRituximab

Identifiers

PMID33886284
PMCPMC8177069
OpenAlexW3153478112

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.