Evidence map›Paper›PMID 39460922›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

LC-MS/MS Analysis to Study the Ubiquitin-Modified Proteome of Recombinant Chinese Hamster Ovary Cells.

Karuppuchamy Selvaprakash, Michael Henry, David Ryan, Paula Meleady

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Karuppuchamy SelvaprakashNational Institute for Cellular Biotechnology, Dublin City University, Dublin, Ireland.
Michael HenryNational Institute for Cellular Biotechnology, Dublin City University, Dublin, Ireland.
David RyanNational Institute for Cellular Biotechnology, Dublin City University, Dublin, Ireland.
Paula MeleadyNational Institute for Cellular Biotechnology, Dublin City University, Dublin, Ireland. paula.meleady@dcu.ie.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is one of the most important post-translational modifications (PTMs) and involves the covalent attachment of ubiquitin to a lysine residue on a target protein. Despite ubiquitination playing a crucial role in regulating cellular processes, the ubiquitinated proteome has not been studied extensively in recombinant Chinese hamster ovary (CHO) cells. Moreover, ubiquitination modification in CHO cells is likely to have an impact on protein function related to the efficient productivity of biopharmaceuticals. In this chapter, we describe a comprehensive protocol for ubiquitin di-Glycine (diGly) peptide enrichment using an immunoprecipitation method from recombinant CHO cell proteins followed by Liquid chromatography-Mass spectrometry (LC-MS) analysis of the ubiquitinated proteome. The methods described are also applicable to differential ubiquitinated proteomic studies.

Indexed as

CricetulusProteomeProteomicsRecombinant ProteinsTandem Mass SpectrometryUbiquitinUbiquitinationAnimalsCHO CellsChromatography, LiquidCricetinaeImmunoprecipitationLiquid Chromatography-Mass SpectrometryProtein Processing, Post-TranslationalProteomeRecombinant ProteinsUbiquitinChinese hamster ovary cellsdiGly peptidesImmunoprecipitationMass spectrometryProteomicsUbiquitin

Identifiers

PMID39460922

What OpenQuestion holds

Textmetadata
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.