Evidence map›Paper›PMID 19193609›Full record

ArticleMolecular & cellular proteomics : MCP2009

Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins.

Marie-Pierre Bousquet-Dubouch, Emilie Baudelet, Frédéric Guérin, Mariette Matondo, Sandrine Uttenweiler-Joseph, Odile Burlet-Schiltz, Bernard Monsarrat

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 73 citations in OpenAlex.

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  9. Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  15. A Conserved Requirement forFrontiers in physiology · 2019
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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.

Marie-Pierre Bousquet-DubouchCNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, F-31077 Toulouse, France.
Emilie Baudelet
Frédéric Guérin
Mariette Matondo
Sandrine Uttenweiler-Joseph
Odile Burlet-Schiltz
Bernard Monsarrat
Institut de Pharmacologie et de Biologie Structurale · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An affinity purification strategy was developed to characterize human proteasome complexes diversity as well as endogenous proteasome-interacting proteins (PIPs). This single step procedure, initially used for 20 S proteasome purification, was adapted to purify all existing physiological proteasome complexes associated to their various regulatory complexes and to their interacting partners. The method was applied to the purification of proteasome complexes and their PIPs from human erythrocytes but can be used to purify proteasomes from any human sample as starting material. The benefit of in vivo formaldehyde cross-linking as a stabilizer of protein-protein interactions was studied by comparing the status of purified proteasomes and the identified proteins in both protocols (with or without formaldehyde cross-linking). Subsequent proteomics analyses identified all proteasomal subunits, known regulators, and recently assigned partners. Moreover other proteins implicated at different levels of the ubiquitin-proteasome system were also identified for the first time as PIPs. One of them, the ubiquitin-specific protease USP7, also known as HAUSP, is an important player in the p53-HDM2 pathway. The specificity of the interaction was further confirmed using a complementary approach that consisted of the reverse immunoprecipitation with HAUSP as a bait. Altogether we provide a valuable tool that should contribute, through the identification of partners likely to affect proteasomal function, to a better understanding of this complex proteolytic machinery in any living human cell and/or organ/tissue and in different cell physiological states.

Indexed as

AnimalsAntibodiesChromatography, AffinityCross-Linking ReagentsElectrophoresis, Polyacrylamide GelErythrocytesFormaldehydeHumansImmunoprecipitationMiceProteasome Endopeptidase ComplexProtein BindingProtein SubunitsProteomicsRatsReproducibility of ResultsAntibodiesCross-Linking ReagentsFormaldehydeProteasome Endopeptidase ComplexProtein SubunitsUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, human

Identifiers

PMID19193609
PMCPMC2689779
OpenAlexW2159090260

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.