Evidence map›Paper›PMID 42542525›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

O- and N-Phosphoproteomic Analysis Using Online Alkaline-pH Reversed-Phase Nanoelectrospray-Tandem Mass Spectrometry.

Yuqiu Wang, Minchu Tang, Wenfan Xie

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

3 authors.

Yuqiu WangDepartment of Analytical Chemistry, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China. wangyuqiu@fudan.edu.cn.
Minchu TangDepartment of Analytical Chemistry, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Wenfan XieSchool of Chinese Materia Medica, Nanjing University of Chinese Medicine, Nanjing, 210023, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation (O-linked and N-linked) is associated with a wide range of biological processes and cell signaling pathways. Aberrant phosphorylation is often observed as a hallmark of diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Mass spectrometry (MS) is an indispensable tool for studying protein phosphorylation. This is primarily due to its high sensitivity and throughput, which allows for comprehensive identification and quantification of phosphorylation events in complex biological samples. In this chapter, we describe a detailed protocol for phosphoproteomic analysis using one-dimensional online alkaline-pH reversed-phase nanoelectrospray-tandem MS (alkaline-pH-MS/MS). It complements traditional online low-pH reversed-phase nanoelectrospray-tandem MS (low-pH-MS/MS) by modulating the charge state distribution of phosphopeptides, which may facilitate the characterization of phosphoproteins with significant biological functions.

Indexed as

Chromatography, Reverse-PhasePhosphoproteinsProteomicsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryHumansHydrogen-Ion ConcentrationNanotechnologyPhosphopeptidesPhosphorylationPhosphopeptidesPhosphoproteinsAlkaline-pH-MS/MSMass spectrometryPhosphoproteomicsPhosphorylationPosttranslational modification

Identifiers

PMID42542525

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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.