Evidence map›Paper›PMID 34932327›Full record

ArticleAnalytical chemistry2022

Epitope Mapping with Diethylpyrocarbonate Covalent Labeling-Mass Spectrometry.

Catherine Y Tremblay, Zachary J Kirsch, Richard W Vachet

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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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.
Zachary J KirschDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, United States.
Richard W VachetDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, United States.ORCID 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
Chemistry-Biology Interface Predoctoral Training GrantT32GM139789 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ERIC Robert STRIETER · 2021 to 2026
$3.4M
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 GM008515NIGMS NIH HHS T32 GM139789NIH HHS S10 OD010645
6 · The paper itself

Abstract

Antigen-antibody epitope mapping is essential for understanding binding mechanisms and developing new protein therapeutics. In this study, we investigate diethylpyrocarbonate (DEPC) covalent labeling-mass spectrometry as a means of analyzing antigen-antibody interactions using the well-characterized model system of TNFα in complex with three different antibodies. Results show that residues buried in the epitope undergo substantial decreases in labeling, as expected. Interestingly, serine, threonine, and tyrosine residues at the edges of the epitope undergo unexpected increases in labeling. The increased labeling of these weakly nucleophilic residues is caused by the formation of hydrophobic pockets upon antibody binding that presumably increase local DEPC concentrations. Residues that are distant from the epitope generally do not undergo changes in labeling extent; however, some that do change experience variations in their local microenvironment due to side-chain reorganization or stabilization of the TNFα trimer that occurs upon binding. Overall, DEPC labeling of antigen-antibody complexes is found to depend on both changes in solvent exposure and changes to the residue microenvironment.

Indexed as

ThreonineTyrosineDiethyl PyrocarbonateEpitope MappingMass SpectrometryDiethyl PyrocarbonateThreonineTyrosine

Identifiers

PMID34932327
PMCPMC8785103
OpenAlexW4200577513

What OpenQuestion holds

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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.