Evidence map›Paper›PMID 25755298›Full record

ArticleMolecular & cellular proteomics : MCP2015

Quantitative proteome analysis of temporally resolved phagosomes following uptake via key phagocytic receptors.

Brian D Dill, Marek Gierlinski, Anetta Härtlova, Alba González Arandilla, Manman Guo, Rosemary G Clarke, Matthias Trost

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  6. Assessing the Phagosome Proteome by Quantitative Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Isolation of Polystyrene Bead-Induced Phagosomes for Western Blotting.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. Quantitative proteomic analysis reveals the molecular mechanism of the Yesso scallop (Computational and structural biotechnology journal · 2022
    Article
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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

7 authors at 2 institutions in 1 country.

Brian D DillFrom the ‡MRC Protein Phosphorylation and Ubiquitylation Unit.
Marek Gierlinski§Division of Computational Biology and.
Anetta HärtlovaFrom the ‡MRC Protein Phosphorylation and Ubiquitylation Unit.
Alba González ArandillaFrom the ‡MRC Protein Phosphorylation and Ubiquitylation Unit.
Manman GuoFrom the ‡MRC Protein Phosphorylation and Ubiquitylation Unit.
Rosemary G Clarke¶Division of Cell Signalling and Immunology, University of Dundee, Scotland, DD1 5EH, United Kingdom.
Matthias TrostFrom the ‡MRC Protein Phosphorylation and Ubiquitylation Unit, m.trost@dundee.ac.uk.
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Medical Research Council G1100713Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_12016/5Wellcome TrustWellcome Trust 081867/Z/06/ZWellcome Trust 097945/Z/11/Z
6 · The paper itself

Abstract

Macrophages operate at the forefront of innate immunity and their discrimination of foreign versus "self" particles is critical for a number of responses including efficient pathogen killing, antigen presentation, and cytokine induction. In order to efficiently destroy the particles and detect potential threats, macrophages express an array of receptors to sense and phagocytose prey particles. In this study, we accurately quantified a proteomic time-course of isolated phagosomes from murine bone marrow-derived macrophages induced by particles conjugated to seven different ligands representing pathogen-associated molecular patterns, immune opsonins or apoptotic cell markers. We identified a clear functional differentiation over the three timepoints and detected subtle differences between certain ligand-phagosomes, indicating that triggering of receptors through a single ligand type has mild, but distinct, effects on phagosome proteome and function. Moreover, our data shows that uptake of phosphatidylserine-coated beads induces an active repression of NF-κB immune responses upon Toll-like receptor (TLR)-activation by recruitment of anti-inflammatory regulators to the phagosome. This data shows for the first time a systematic time-course analysis of bone marrow-derived macrophages phagosomes and how phagosome fate is regulated by the receptors triggered for phagocytosis.

Indexed as

PhagocytosisAnimalsCalreticulinComplement System ProteinsImmunity, InnateImmunoglobulin GLigandsLipopolysaccharidesMacrophagesMannansMiceMicrospheresNF-kappa BOpsonin ProteinsPhagosomesPhosphatidylserinesCalreticulinComplement System ProteinsImmunoglobulin GLigandsLipopolysaccharidesMannansNF-kappa BOpsonin ProteinsPhosphatidylserinesProteomeReceptors, Cell Surface

Identifiers

PMID25755298
PMCPMC4424403
OpenAlexW2127271866

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.