Evidence map›Paper›PMID 40719761›Full record

ArticleAnalytical chemistry2025

AUTO-SP: Automated Sample Preparation for Analyzing Proteins and Protein Modifications.

T Mamie Lih, Liyuan Jiao, Lijun Chen, Jongmin Woo, Yuefan Wang, Hui Zhang

Abstract read
In one paragraph

Article in Analytical chemistry, 2025. 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
  2. Article
  3. 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

6 authors.

T Mamie LihDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0003-0317-2660
Liyuan JiaoDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Lijun ChenDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Jongmin WooDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Yuefan WangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0001-5731-6143
Hui ZhangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0001-8726-7098

Funding

Proteogenomic Characterization of Tumor Tissues and Preclinical Models with High PrecisionU24CA271079 · NCI · JOHNS HOPKINS UNIVERSITY · PI DANIEL Wanyui CHAN, Hui Zhang · 2022 to 2026
$6.6M
Biomarker Reference LaboratoryU2CCA271895 · NCI · JOHNS HOPKINS UNIVERSITY · PI DANIEL Wanyui CHAN · 2023 to 2026
$4.6M
Development of a panel of multiplex biomarkers for the early detection of pancreatic ductal adenocarcinoma and high-risk lesionsU01CA274514 · NCI · JOHNS HOPKINS UNIVERSITY · PI Randall Brand, DANIEL Wanyui CHAN · 2023 to 2026
$3.2M
NCI NIH HHS U01 CA274514NCI NIH HHS U24 CA271079NCI NIH HHS U2C CA271895
6 · The paper itself

Abstract

Liquid chromatography (LC) tandem mass spectrometry (MS/MS) is one of the widely used proteomic techniques to study the alterations occurring at the protein level as well as post-translational modifications (PTMs) of proteins that are relevant to different physiological or pathological statuses. The mass spectrometric analysis of peptides digested from proteins (bottom-up proteomics) has emerged as one of the major approaches for proteomics. In this approach, proteins are first cleaved by one or more proteases into peptides for MS analysis, and peptides with PTMs are further enriched, followed by the LC-MS/MS analysis. To achieve a reproducible and quantitative proteomic characterization, a well-established protease digestion and PTM peptide enrichment protocol is critical. In this study, we developed AUTO-SP, a sample preparation platform providing automated protocols for BCA analysis, protein digestion, and PTM enrichment for protein and PTM analyses. We utilized patient-derived xenograft (PDX) breast cancer tumor tissues (basal-like and luminal subtypes) to demonstrate the efficacy of AUTO-SP. The protein amount was quantified, and proteins were further digested by using AUTO-SP for each PDX sample. Based on the data-independent acquisition (DIA)-MS data, we observed that samples of the same breast cancer subtypes were highly correlated (≥0.98). Additionally, >25,000 phosphopeptides and >14,000 ubiquitinated peptides were identified in the PDX samples when using AUTO-SP for PTM enrichment, while unique pathways were enriched from the differentially expressed ubiquitinated peptides of basal-like and luminal subtypes. AUTO-SP demonstrated its efficacy to provide a reliable and reproducible sample preparation procedure for MS-based proteomic and PTM analyses.

Indexed as

Breast NeoplasmsProteinsProteomicsAnimalsAutomationChromatography, LiquidFemaleHumansMicePeptidesProtein Processing, Post-TranslationalTandem Mass SpectrometryPeptidesProteins

Identifiers

PMID40719761
PMCPMC12355475

What Socratic 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 Socratic graph.