Evidence map›Paper›PMID 29254231›Full record

ArticleOncotarget2017

Proteomic analysis of affinity-purified extracellular proteasomes reveals exclusively 20S complexes.

Valentina A Kulichkova, Tatiana O Artamonova, Olga G Lyublinskaya, Mikhail A Khodorkovskii, Alexey N Tomilin, Anna S Tsimokha

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Functional 20S Proteasomes in Retroviruses: Evidence in Favor.International journal of molecular sciences · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Exosomal Protease Cargo as Prognostic Biomarker in Colorectal Cancer.Asian Pacific journal of cancer prevention : APJCP · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Review
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

6 authors at 2 institutions in 1 country.

Valentina A KulichkovaInstitute of Cytology, Russian Academy of Sciences, St-Petersburg 194064, Russia.
Tatiana O ArtamonovaInstitute of Nanobiotechnologies, Peter the Great St-Petersburg Polytechnic University, St-Petersburg 195251, Russia.
Olga G LyublinskayaInstitute of Cytology, Russian Academy of Sciences, St-Petersburg 194064, Russia.
Mikhail A KhodorkovskiiInstitute of Nanobiotechnologies, Peter the Great St-Petersburg Polytechnic University, St-Petersburg 195251, Russia.
Alexey N TomilinInstitute of Cytology, Russian Academy of Sciences, St-Petersburg 194064, Russia.
Anna S TsimokhaInstitute of Cytology, Russian Academy of Sciences, St-Petersburg 194064, Russia.
Institute of Cytology · RUPeter the Great St. Petersburg Polytechnic University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasome-mediated proteolysis is important for many basic cellular processes. In addition to their functions in the cell, proteasomes have been found in physiological fluids of both healthy and diseased humans including cancer patients. Higher levels of these proteasomes are associated with higher cancer burden and stage. The etiology and functions of these proteasomes, referred to as circulating, plasmatic, or extracellular proteasomes (ex-PSs), are unclear. Here we show that human cancer cell lines, as well as human endometrium-derived mesenchymal stem cells (hMESCs), release proteasome complexes into culture medium (CM). To define ex-PS composition, we have affinity purified them from CM conditioned by human leukemia cell line K562. Using matrix-assisted laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS), we have identified core 20S proteasome subunits and a set of 15 proteasome-interacting proteins (PIPs), all previously described as exosome cargo proteins. Three of them, PPIase A, aldolase A, and transferrin, have never been reported as PIPs. The study provides compelling arguments that ex-PSs do not contain 19S or PA200 regulatory particles and are represented exclusively by the 20S complex.

Indexed as

affinity purificationextracellular proteasomehuman leukemia K562 cellsmass spectrometryproteasome interacting protein (PIP)

Identifiers

PMID29254231
PMCPMC5731941
OpenAlexW2767132232

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.