Evidence map›Paper›PMID 35019278›Full record

ArticleAnalytical chemistry2022

Benzoyl Transfer for Footprinting Alcohol-Containing Residues in Higher Order Structural Applications of Mass-Spectrometry-Based Proteomics.

Austin B Moyle, Ming Cheng, Nicole D Wagner, Michael L Gross

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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023
    Article
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  7. Article
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

4 authors at 1 institution in 1 country.

Austin B MoyleDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States.
Ming ChengDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0002-1581-6382
Nicole D WagnerDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0003-3980-4893
Michael L GrossDepartment of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States.ORCID 0000-0003-1159-4636
Washington University in St. Louis · US

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
NEW CHEMICAL PROBES ENABLE MASS SPECTROMETRY-BASED FOOTPRINTING OF HUMAN PROTEIN STRUCTURE IN LIPID MEMBRANES AND CELLSR01GM131008 · NIGMS · WASHINGTON UNIVERSITY · PI MICHAEL L GROSS, Weikai Li · 2019 to 2026
$3.8M
A Biomedical Mass Spectrometry Resource: Ongoing Driving Biomedical ProjectsR24GM136766 · NIGMS · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2020 to 2022
$2.3M
NIGMS NIH HHS P41 GM103422NIGMS NIH HHS R01 GM131008NIGMS NIH HHS R24 GM136766
6 · The paper itself

Abstract

Protein footprinting mass spectrometry (MS), an emerging approach to elucidate higher-order structure (HOS) and binding, benefits from the iterative development of reaction strategies to expand the covalent labeling toolbox. Herein, we introduce a footprinting reagent for nucleophiles and demonstrate its efficacy for differential covalent labeling MS analysis. Benzoyl fluoride (BF), although reactive with water, is more practical for modifying nucleophilic functional groups than other acid halides and serves as an acyl-transfer reagent for proteins. BF is 10 times more reactive with phenolic Tyr than the current generation nucleophile footprinter. BF modifies, in addition to Tyr, Lys, His, and the N-terminus, weak nucleophiles Ser and Thr, for which few footprinters exist, imparting broad applicability with a range of nucleophiles. We applied benzoylation to a model Ser- and Thr-rich protein-ligand binding system without perturbing the protein HOS. This efficacious footprinting method expands the toolbox of reagents and provides promise for future reaction strategies including possibly membrane proteins.

Indexed as

Protein FootprintingProteomicsIndicators and ReagentsMass SpectrometryMembrane ProteinsIndicators and ReagentsMembrane Proteins

Identifiers

PMID35019278
PMCPMC10483880
OpenAlexW4206425820

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.