ReviewCells2016
The Trypanosome Flagellar Pocket Collar and Its Ring Forming Protein-TbBILBO1.
Review in Cells, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- FAZ assembly in bloodstream formMolecular biology of the cell · 2023Article
- TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei.Parasite (Paris, France) · 2022Article
- Bhalin, an Essential Cytoskeleton-Associated Protein ofMicroorganisms · 2021Article
- Structural and functional studies of the first tripartite protein complex at the Trypanosoma brucei flagellar pocket collar.PLoS pathogens · 2021Article
- The kinesin of the flagellum attachment zone in Leishmania is required for cell morphogenesis, cell division and virulence in the mammalian host.PLoS pathogens · 2021Article
- Evaluation of the Immunoprotective Potential of Recombinant Paraflagellar Rod Proteins ofVaccines · 2020Article
- A photoactivatable crosslinking system reveals protein interactions in the Toxoplasma gondii inner membrane complex.PLoS biology · 2019Article
- The Trypanosomal Transferrin Receptor of Trypanosoma Brucei-A Review.Tropical medicine and infectious disease · 2019Review
- Transcriptome, proteome and draft genome of Euglena gracilis.BMC biology · 2019Article
- Identification of TOEFAZ1-interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis.Molecular microbiology · 2018Article
- Let's get fISSical: fast in silico synchronization as a new tool for cell division cycle analysis.Parasitology · 2018Review
- Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei.PLoS pathogens · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sub-species of Trypanosoma brucei are the causal agents of human African sleeping sickness and Nagana in domesticated livestock. These pathogens have developed an organelle-like compartment called the flagellar pocket (FP). The FP carries out endo- and exocytosis and is the only structure this parasite has evolved to do so. The FP is essential for parasite viability, making it an interesting structure to evaluate as a drug target, especially since it has an indispensible cytoskeleton component called the flagellar pocket collar (FPC). The FPC is located at the neck of the FP where the flagellum exits the cell. The FPC has a complex architecture and division cycle, but little is known concerning its organization. Recent work has focused on understanding how the FP and the FPC are formed and as a result of these studies an important calcium-binding, polymer-forming protein named TbBILBO1 was identified. Cellular biology analysis of TbBILBO1 has demonstrated its uniqueness as a FPC component and until recently, it was unknown what structural role it played in forming the FPC. This review summarizes the recent data on the polymer forming properties of TbBILBO1 and how these are correlated to the FP cytoskeleton.
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Registered trials
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.