ArticleJournal of molecular evolution2005
Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites.
Article in Journal of molecular evolution, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Identification of a conserved gene family with an essential role inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A dual-aptazyme system for genetic complementation reveals stage-specific roles for themSphere · 2026Article
- An inclusive assessment of apoptosis mechanisms inCurrent research in parasitology & vector-borne diseases · 2025Review
- Identification of novel compounds againstComputational and structural biotechnology journal · 2025Article
- Susceptibility ofTropical medicine and infectious disease · 2024Article
- Discovery of essential kinetoplastid-insect adhesion proteins and their function in Leishmania-sand fly interactions.Nature communications · 2024Article
- Differential expression of peptidases in Strigomonas culicis wild-type and aposymbiotic strains: from proteomic data to proteolytic activity.Memorias do Instituto Oswaldo Cruz · 2024Article
- Domain Architecture Based Methods for Comparative Functional Genomics Toward Therapeutic Drug Target Discovery.Journal of molecular evolution · 2023Review
- Evaluation of calpain T-cell epitopes as vaccine candidates against experimental Leishmania major infection: a pilot study.Parasitology research · 2022Article
- Global distribution of treatment resistance gene markers for leishmaniasis.Journal of clinical laboratory analysis · 2022Review
- Antileishmanial Efficacy of the Calpain Inhibitor MDL28170 in Combination with Amphotericin B.Tropical medicine and infectious disease · 2022Article
- The Use of AlphaFold forFrontiers in cellular and infection microbiology · 2022Article
- The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?Cells · 2021Review
- Expression and cellular localisation of Trypanosoma cruzi calpains.Memorias do Instituto Oswaldo Cruz · 2020Article
- Article
- Cell death in Leishmania.Parasite (Paris, France) · 2019Review
- Calpains of Leishmania braziliensis: genome analysis, differential expression, and functional analysis.Memorias do Instituto Oswaldo Cruz · 2019Article
- Susceptibility of promastigotes and intracellular amastigotes from distinct Leishmania species to the calpain inhibitor MDL28170.Parasitology research · 2018Article
- Why calpain inhibitors are interesting leading compounds to search for new therapeutic options to treat leishmaniasis?Parasitology · 2017Review
- Susceptibility of Phytomonas serpens to calpain inhibitors in vitro: interference on the proliferation, ultrastructure, cysteine peptidase expression and interaction with the invertebrate host.Memorias do Instituto Oswaldo Cruz · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Employing whole-genome analysis we have characterized a large family of genes coding for calpain-related proteins in three kinetoplastid parasites. We have defined a total of 18 calpain-like sequences in Trypanosoma brucei, 27 in Leishmania major, and 24 in Trypanosoma cruzi. Sequence characterization revealed a well-conserved protease domain in most proteins, although residues critical for catalytic activity were frequently altered. Many of the proteins contain a novel N-terminal sequence motif unique to kinetoplastids. Furthermore, 24 of the sequences contain N-terminal fatty acid acylation motifs indicating association of these proteins with intracellular membranes. This extended family of proteins also includes a group of sequences that completely lack a protease domain but is specifically related to other kinetoplastid calpain-related proteins by a highly conserved N-terminal domain and by genomic organization. All sequences lack the C-terminal calmodulin-related calcium-binding domain typical of most mammalian calpains. Our analysis emphasizes the highly modular structure of calpains and calpain-like proteins, suggesting that they are involved in diverse cellular functions. The discovery of this surprisingly large family of calpain-like proteins in lower eukaryotes that combines novel and conserved sequence modules contributes to our understanding of the evolution of this abundant protein family.
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