Evidence map›Paper›PMID 33442901›Full record

ArticleChembiochem : a European journal of chemical biology2021

SP3-FAIMS Chemoproteomics for High-Coverage Profiling of the Human Cysteinome*.

Tianyang Yan, Heta S Desai, Lisa M Boatner, Stephanie L Yen, Jian Cao, Maria F Palafox, Yasaman Jami-Alahmadi, Keriann M Backus

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 87 citations in OpenAlex.

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  19. Size-Dependent Target Engagement of Covalent Probes.Journal of medicinal chemistry · 2025
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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

8 authors at 1 institution in 1 country.

Tianyang YanDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.ORCID 0000-0002-4941-9828
Heta S DesaiDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
Lisa M BoatnerDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
Stephanie L YenDepartment of Chemistry and Biochemistry, UCLA, Los Angeles, CA 90095, USA.
Jian CaoDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
Maria F PalafoxDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
Yasaman Jami-AlahmadiDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
Keriann M BackusDepartment of Biological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.ORCID 0000-0001-8541-1404
University of California, Los Angeles · US

Funding

CHEMISTRY BIOLOGY INTERFACE TRAINING PROGRAMT32GM008496 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 1993 to 2019
$6.3M
Systems in Integrative BiologyT32GM008185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHOU, TOM · 1987 to 2022
$4.6M
Beckman Young Investigator AwardNIGMS NIH HHS T32 GM008185NIGMS NIH HHS T32 GM008496NIGMS System and Integrative Biology 5T32GM008185-33Scholar Award V2019-017TRDRP T31DT1800
6 · The paper itself

Abstract

Chemoproteomics has enabled the rapid and proteome-wide discovery of functional, redox-sensitive, and ligandable cysteine residues. Despite widespread adoption and considerable advances in both sample-preparation workflows and MS instrumentation, chemoproteomics experiments still typically only identify a small fraction of all cysteines encoded by the human genome. Here, we develop an optimized sample-preparation workflow that combines enhanced peptide labeling with single-pot, solid-phase-enhanced sample-preparation (SP3) to improve the recovery of biotinylated peptides, even from small sample sizes. By combining this improved workflow with on-line high-field asymmetric waveform ion mobility spectrometry (FAIMS) separation of labeled peptides, we achieve unprecedented coverage of >14000 unique cysteines in a single-shot 70 min experiment. Showcasing the wide utility of the SP3-FAIMS chemoproteomic method, we find that it is also compatible with competitive small-molecule screening by isotopic tandem orthogonal proteolysis-activity-based protein profiling (isoTOP-ABPP). In aggregate, our analysis of 18 samples from seven cell lines identified 34225 unique cysteines using only ∼28 h of instrument time. The comprehensive spectral library and improved coverage provided by the SP3-FAIMS chemoproteomics method will provide the technical foundation for future studies aimed at deciphering the functions and druggability of the human cysteineome.

Indexed as

BiotinCycloaddition ReactionCysteineHEK293 CellsHumansIodoacetamideIon Mobility SpectrometryPeptidesProteomicsSolid-Phase Synthesis TechniquesBiotinCysteineIodoacetamidePeptideschemoproteomicscysteinehigh-field asymmetric waveform ion mobility spectrometry (FAIMS)LC-MS/MSsingle-pot, solid-phase-enhanced sample-preparation (SP3)

Identifiers

PMID33442901
PMCPMC8942723
OpenAlexW3118452131

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.