Evidence map›Paper›PMID 33530589›Full record

ArticleProteomes2021

Targeted Quantification of the Lysosomal Proteome in Complex Samples.

Peter Mosen, Anne Sanner, Jasjot Singh, Dominic Winter

Open access · goldAbstract read
In one paragraph

Article in Proteomes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Mass Spectrometry-Based Proteomic Analysis of Lysosome-Enriched Fractions.Methods in molecular biology (Clifton, N.J.) · 2026
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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

4 authors at 1 institution in 1 country.

Peter MosenInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115 Bonn, Germany.
Anne SannerInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115 Bonn, Germany.
Jasjot SinghInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115 Bonn, Germany.
Dominic WinterInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, 53115 Bonn, Germany.ORCID 0000-0001-6788-6641
University of Bonn · DE

Funding

Deutsche Forschungsgemeinschaft FOR2625Studienstiftung des Deutschen Volkes n/a
6 · The paper itself

Abstract

In eukaryotic cells, lysosomes play a crucial role in the breakdown of a variety of components ranging from small molecules to complex structures, ascertaining the continuous turnover of cellular building blocks. Furthermore, they act as a regulatory hub for metabolism, being crucially involved in the regulation of major signaling pathways. Currently, ~450 lysosomal proteins can be reproducibly identified in a single cell line by mass spectrometry, most of which are low-abundant, restricting their unbiased proteomic analysis to lysosome-enriched fractions. In the current study, we applied two strategies for the targeted investigation of the lysosomal proteome in complex samples: data-independent acquisition (DIA) and parallel reaction monitoring (PRM). Using a lysosome-enriched fraction, mouse embryonic fibroblast whole cell lysate, and mouse liver whole tissue lysate, we investigated the capabilities of DIA and PRM to investigate the lysosomal proteome. While both approaches identified and quantified lysosomal proteins in all sample types, and their data largely correlated, DIA identified on average more proteins, especially for lower complex samples and longer chromatographic gradients. For the highly complex tissue sample and shorter gradients, however, PRM delivered a better performance regarding both identification and quantification of lysosomal proteins. All data are available via ProteomeXchange with identifier PXDD023278.

Indexed as

data-independent acquisitionlabel-free quantificationlysosomesparallel reaction monitoringtargeted proteomics

Identifiers

PMID33530589
PMCPMC7931001
OpenAlexW3123087441

What OpenQuestion holds

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LicenceCC BY
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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.