ArticleBiochemistry2014
Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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Who cites it
5 citing papers in PubMed.
- Rare Earth Element-Induced Condensation of the Block V of the Repeats-in-Toxin Domain from CyaA fromLangmuir : the ACS journal of surfaces and colloids · 2025Article
- Ion-selective conformational stabilization of a disordered repeats-in-toxin protein domain.Biophysical journal · 2025Article
- Genetic Functionalization of Protein-Based Biomaterials via Protein Fusions.Biomacromolecules · 2024Review
- Bactericidal Effect ofFrontiers in microbiology · 2021Article
- Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens.PloS one · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Self-assembling proteins represent potential scaffolds for the organization of enzymatic activities. The alkaline protease repeats-in-toxin (RTX) domain from Pseudomonas aeruginosa undergoes multiple structural transitions in the presence and absence of calcium, a native structural cofactor. In the absence of calcium, this domain is capable of spontaneous, ordered polymerization, producing amyloid-like fibrils and large two-dimensional protein sheets. This polymerization occurs under near-physiological conditions, is rapid, and can be controlled by regulating calcium in solution. Fusion of the RTX domain to a soluble protein results in the incorporation of engineered protein function into these macromolecular assemblies. Applications of this protein sequence in bacterial adherence and colonization and the generation of biomaterials are discussed.
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