Evidence map›Paper›PMID 32103020›Full record

ArticleScientific data2020

Comprehensive draft of the mouse embryonic fibroblast lysosomal proteome by mass spectrometry based proteomics.

Srigayatri Ponnaiyan, Fatema Akter, Jasjot Singh, Dominic Winter

Open access · goldAbstract readDataset
In one paragraph

Article in Scientific data, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 30 citations in OpenAlex.

  1. Mass Spectrometry-Based Proteomic Analysis of Lysosome-Enriched Fractions.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Proteomic analysis links truncated tau to lysosome motility, autophagy, and endo-lysosomal dysfunction.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. 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 at 1 institution in 2 countries.

Srigayatri Ponnaiyan *Institute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, 53115, Germany.
Fatema Akter *Institute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, 53115, Germany.
Jasjot SinghInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, 53115, Germany.
Dominic WinterInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, 53115, Germany. dominic.winter@uni-bonn.de.ORCID http://orcid.org/0000-0001-6788-6641
University of Bonn · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) FOR2625
6 · The paper itself

Abstract

Lysosomes are the main degradative organelles of cells and involved in a variety of processes including the recycling of macromolecules, storage of compounds, and metabolic signaling. Despite an increasing interest in the proteomic analysis of lysosomes, no systematic study of sample preparation protocols for lysosome enriched fractions has been performed to date. In the current study, we used samples enriched for lysosomes by paramagnetic nanoparticles and systematically evaluated experimental parameters for the analysis of the lysosomal proteome. This includes different approaches for the concentration of lysosome-containing fractions; desalting of samples by solid phase extraction; fractionation of peptide samples; and different gradient lengths for LC-MS/MS analyses of unfractionated samples by data dependent and data independent acquisition. Furthermore, we evaluated four different digestion methods including filter aided sample preparation (FASP), in-gel digestion, and in-solution digestion using either RapiGest or urea. Using the combined data, we generated a benchmark lysosomal proteome data set for mouse embryonic fibroblasts as well as a spectral library for the analysis of lysosomes by data independent acquisition.

Indexed as

AnimalsChromatography, LiquidEmbryo, MammalianFibroblastsLysosomesMiceProteomeProteomicsTandem Mass SpectrometryProteome

Identifiers

PMID32103020
PMCPMC7044164
OpenAlexW3008491580

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.