Evidence map›Paper›PMID 41410420›Full record

ArticleProteomics2026

In-Cell Proteomics Enables High-Resolution Temporal Profiling of Cell Cycle Progression and DNA Damage Response in Saccharomyces cerevisiae.

Henry Nwaora, Yanbao Yu, Zhihao Zhuang

Abstract read
In one paragraph

Article in Proteomics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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.

Henry NwaoraDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.
Yanbao YuDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.
Zhihao ZhuangDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.

Funding

Predictive Modeling & Optimal Control Framework for Model-Based Epidemic Response in DelawareP20GM103446 · NIGMS · UNIVERSITY OF DELAWARE · PI Shawn W Polson · 2012 to 2026
$67.2M
This renovation project will create over 1455 sq. ft. of state- of-the-art reseaP20GM104316 · NIGMS · UNIVERSITY OF DELAWARE · PI FOX, JOSEPH M · 2014 to 2024
$26.8M
NIH ADMINISTRATIVE SUPPLEMENT AUTOMATED PEPTIDE SYNTHESIZER ZHUANGR01GM129468 · NIGMS · UNIVERSITY OF DELAWARE · PI ZHUANG, ZHIHAO · 2019 to 2022
$1.3M
Deciphering protein ubiquitination with chemical biology toolsR35GM152011 · NIGMS · UNIVERSITY OF DELAWARE · PI Zhihao Zhuang · 2024 to 2026
$1.2M
National Institute of Health's National Institute of General Medical Sciences P20GM103446National Institutes of Health (NIH) R01GM129468National Institutes of Health (NIH) R35GM152011NIGMS NIH HHS P20 GM103446NIGMS NIH HHS P20 GM104316NIGMS NIH HHS P20GM104316NIGMS NIH HHS R01 GM129468NIGMS NIH HHS R35 GM152011
6 · The paper itself

Abstract

Yeast is a widely used model organism in biological and proteomics research. Conventional bottom-up proteomic analysis of yeast cells requires disruption of the rigid cell wall to extract proteins, which is often associated with lengthy procedures, significant technical variations, and noticeable sample loss. Here, we present an "in-cell proteomics" approach that eliminates cell lysis and digests proteins directly in the yeast cells after a rapid methanol fixation. The approach integrates all the sample processing into a single filter device, offering a simple yet highly effective and sensitive approach for yeast proteomics analysis. We applied this approach to characterize proteome dynamics in the budding yeast Saccharomyces cerevisiae during cell cycle progression and following DNA damage. With single-shot LC-MS, we were able to detect and quantify around 3500 yeast proteins from the in-cell digests. Our study introduces a novel in-cell approach for yeast proteomics analysis and presents a quantitative proteome map of yeast cell-cycle progression with high temporal resolution for cell division cycle (Cdc) proteins. It also provides a comprehensive, time-resolved view of proteome-wide dynamics and remodeling throughout the yeast cell cycle in response to methyl methanesulfonate (MMS)-induced DNA damage. SUMMARY: Yeast proteomics studies often require detergent-based and/or mechanical disruption procedures for cell lysis and protein digestion. We reported an "in-cell proteomics" approach that eliminates cell lysis and digests proteins directly in the yeast cells after a simple methanol fixation. The approach integrates all the sample processing into a single filter device, offering a rapid yet highly effective and sensitive approach for yeast proteomics analysis. Using this method, we were able to characterize proteome dynamics in the budding yeast Saccharomyces cerevisiae during cell cycle progression and following DNA damage.

Indexed as

Cell CycleDNA DamageProteomeProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChromatography, LiquidMethyl MethanesulfonateMethyl MethanesulfonateProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID41410420
PMCPMC13155863

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Registered trials

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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.