ArticleFrontiers in molecular neuroscience2012
Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity.
Article in Frontiers in molecular neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Human stefin B: from its structure, folding, and aggregation to its function in health and disease.Frontiers in molecular neuroscience · 2022Review
- Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation.Frontiers in molecular neuroscience · 2021Article
- Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B.ACS chemical neuroscience · 2019Article
- Inhibition of Protein Aggregation by Several Antioxidants.Oxidative medicine and cellular longevity · 2018Article
- Pore-Forming Proteins as Mediators of Novel Epigenetic Mechanism of Epilepsy.Frontiers in neurology · 2017Article
- Article
- The role of initial oligomers in amyloid fibril formation by human stefin B.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is well documented that amyloid forming peptides and proteins interact with membranes and that this correlates with cytotoxicity. To introduce the theme we give a brief description of some amyloidogenic proteins and note their similarities with pore forming toxins (PFTs) and cell penetrating peptides. Human stefin B, a member of the family of cystatins, is an amyloidogenic protein in vitro. This review describes our studies of the interaction of stefin B oligomers and prefibrillar aggregates with model membranes leading to pore formation. We have studied the interaction between human stefin B and artificial membranes of various compositions. We also have prepared distinct sizes and morphologies of stefin B prefibrillar states and assessed their toxicity. Furthermore, we have measured electrical currents through pores formed by stefin B prefibrillar oligomers in a planar lipid bilayer setup. We finally discuss the possible functional and pathological significance of such pores formed by human stefin B.
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