Evidence map›Paper›PMID 33535641›Full record

ReviewCells2021

The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?

Vítor Ennes-Vidal, Marta Helena Branquinha, André Luis Souza Dos Santos, Claudia Masini d'Avila-Levy

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Susceptibility ofTropical medicine and infectious disease · 2024
    Article
  3. Deciphering Host-Parasite Interplay inACS infectious diseases · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. ACurrent research in insect science · 2024
    Article
  8. LeishIF3d is a non-canonical cap-binding protein inFrontiers in molecular biosciences · 2023
    Article
  9. Review
  10. Article
  11. 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 2 institutions in 1 country.

Vítor Ennes-VidalLaboratório de Estudos Integrados em Protozoologia, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz (FIOCRUZ), 21040-360 Rio de Janeiro, Brazil.ORCID 0000-0001-6122-1956
Marta Helena BranquinhaLaboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro (UFRJ), 21941-901 Rio de Janeiro, Brazil.ORCID 0000-0002-9752-8148
André Luis Souza Dos SantosLaboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro (UFRJ), 21941-901 Rio de Janeiro, Brazil.ORCID 0000-0003-0821-8592
Claudia Masini d'Avila-LevyLaboratório de Estudos Integrados em Protozoologia, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz (FIOCRUZ), 21040-360 Rio de Janeiro, Brazil.ORCID 0000-0001-8042-4695
Fundação Oswaldo Cruz · BRUniversidade Federal do Rio de Janeiro · BR

Funding

Lacrimal Gland Repair Using Progenitor CellsR01EY026202 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI MAKARENKOVA, HELEN P. · 2016 to 2025
$5.2M
Conselho Nacional de Desenvolvimento Científico e Tecnológico 442589Coordenação de Aperfeiçoamento de Pessoal de Nível Superior 001Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/202. 807/2018
6 · The paper itself

Abstract

Calpains are calcium-dependent cysteine peptidases that were originally described in mammals and, thereafter, their homologues were identified in almost all known living organisms. The deregulated activity of these peptidases is associated with several pathologies and, consequently, huge efforts have been made to identify selective inhibitors. Trypanosomatids, responsible for life-threatening human diseases, possess a large and diverse family of calpain sequences in their genomes. Considering that the current therapy to treat trypanosomatid diseases is limited to a handful of drugs that suffer from unacceptable toxicity, tough administration routes, like parenteral, and increasing treatment failures, a repurposed approach with calpain inhibitors could be a shortcut to successful chemotherapy. However, there is a general lack of knowledge about calpain functions in these parasites and, currently, the proteolytic activity of these proteins is still an open question. Here, we highlight the current research and perspectives on trypanosomatid calpains, overview calpain description in these organisms, and explore the potential of targeting the calpain system as a therapeutic strategy. This review gathers the current knowledge about this fascinating family of peptidases as well as insights into the puzzle: are we unable to measure calpain activity in trypanosomatids, or are the functions of these proteins devoid of proteolytic activity in these parasites?

Indexed as

AnimalsCalpainGene ExpressionHumansProteinsProteolysisTrypanosomatinaCalpainProteinschemotherapycysteine peptidaseLeishmaniaTrypanosoma

Identifiers

PMID33535641
PMCPMC7912814
OpenAlexW3127820117

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.