Evidence map›Paper›PMID 21698116›Full record

ArticlePloS one2011

Analysis of proteasomal proteolysis during the in vitro metacyclogenesis of Trypanosoma cruzi.

Josiane Cardoso, Carla De Paula Lima, Tiago Leal, Daniela F Gradia, Stênio P Fragoso, Samuel Goldenberg, Renata Guerra De Sá, Marco A Krieger

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Stage-specific MCM protein expression inFrontiers in cellular and infection microbiology · 2025
    Article
  2. Article
  3. Metacyclogenesis as the Starting Point of Chagas Disease.International journal of molecular sciences · 2023
    Review
  4. Review
  5. Adaptation of the Tumor Antigen Presentation Machinery to Ionizing Radiation.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Redox Balance Keepers and Possible Cell Functions Managed by Redox Homeostasis inFrontiers in cellular and infection microbiology · 2019
    Review
  11. Identification ofFrontiers in endocrinology · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. 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

8 authors at 3 institutions in 1 country.

Josiane CardosoInstituto Carlos Chagas/FIOCRUZ, Curitiba, Parana, Brazil.
Carla De Paula Lima
Tiago Leal
Daniela F Gradia
Stênio P Fragoso
Samuel Goldenberg
Renata Guerra De Sá
Marco A Krieger
Fundação Oswaldo Cruz · BRFundação Carlos Chagas · BRUniversidade Federal de Ouro Preto · BR

Funding

Functional genomics of metacyclogenesis in T.cruziR01AI050196 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI BUCK, GREGORY ALLEN · 2002 to 2006
$2.6M
NIAID NIH HHS 5R01AI050196-02NIAID NIH HHS R01 AI050196
6 · The paper itself

Abstract

Proteasomes are large protein complexes, whose main function is to degrade unnecessary or damaged proteins. The inhibition of proteasome activity in Trypanosoma cruzi blocks parasite replication and cellular differentiation. We demonstrate that proteasome-dependent proteolysis occurs during the cellular differentiation of T. cruzi from replicative non-infectious epimastigotes to non-replicative and infectious trypomastigotes (metacyclogenesis). No peaks of ubiquitin-mediated degradation were observed and the profile of ubiquitinated conjugates was similar at all stages of differentiation. However, an analysis of carbonylated proteins showed significant variation in oxidized protein levels at the various stages of differentiation and the proteasome inhibition also increased oxidized protein levels. Our data suggest that different proteasome complexes coexist during metacyclogenesis. The 20S proteasome may be free or linked to regulatory particles (PA700, PA26 and PA200), at specific cell sites and the coordinated action of these complexes would make it possible for proteolysis of ubiquitin-tagged proteins and oxidized proteins, to coexist in the cell.

Indexed as

AnimalsBlotting, WesternHydrolysisProteasome Endopeptidase ComplexTrypanosoma cruziUbiquitinationProteasome Endopeptidase Complex

Identifiers

PMID21698116
PMCPMC3117861
OpenAlexW2005953424

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.