Evidence map›Paper›PMID 41746267›Full record

ArticleJournal of the American Society for Mass Spectrometry2026

Exploring the Potential of Ultrafast Arylation for Capping Cysteine Residues with Fixed Charge Modifications.

Toma Chowdhury, Thomas A Shoff, Colomba Sanchez-Marsetti, W Hill Harman, Ryan R Julian

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Toma ChowdhuryDepartment of Chemistry, University of California, Riverside, California 92521, United States.
Thomas A ShoffDepartment of Chemistry, University of California, Riverside, California 92521, United States.
Colomba Sanchez-MarsettiDepartment of Chemistry, University of California, Riverside, California 92521, United States.ORCID 0009-0008-5368-2056
W Hill HarmanDepartment of Chemistry, University of California, Riverside, California 92521, United States.ORCID 0000-0003-0400-2890
Ryan R JulianDepartment of Chemistry, University of California, Riverside, California 92521, United States.ORCID 0000-0003-1580-8355

Funding

Connecting long-lived protein isomerization to lysosomal failure in Alzheimer's diseaseR01AG066626 · NIA · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI JULIAN, RYAN ROY · 2020 to 2024
$2.8M
NIA NIH HHS R01 AG066626
6 · The paper itself

Abstract

Reduction of disulfide bonds in proteins followed by selective modification of Cysteine (Cys) residues is a common practice in proteomics experiments to facilitate digestion into peptides and ultimately identification by mass spectrometry (MS). Due to its high nucleophilicity, a variety of reaction pathways can be used to block Cys; however, arylation is not often employed. Recently, Lipka and co-workers reported an electrophilic Cys arylation reagent,

Indexed as

CysteinePyridinium CompoundsAmino Acid SequenceMass SpectrometryProteomicsTandem Mass SpectrometryCysteinePyridinium Compoundsclick reactionepimerfragmentationisomerphotodissociation

Identifiers

PMID41746267
PMCPMC13047680

What OpenQuestion holds

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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.