ZnO for performance enhancement of surface plasmon resonance biosensor: a review

GS Mei, PS Menon, G Hegde - Materials Research Express, 2020 - iopscience.iop.org
This paper reviews Kretschmann-based SPR sensor utilizing ZnO thin films and
nanostructures for performance enhancement. The advancement in surface plasmon …

Beyond pore formation: Reorganization of the plasma membrane induced by pore-forming proteins

M Kulma, G Anderluh - Cellular and Molecular Life Sciences, 2021 - Springer
Pore-forming proteins (PFPs) are a heterogeneous group of proteins that are expressed and
secreted by a wide range of organisms. PFPs are produced as soluble monomers that bind …

[HTML][HTML] Pore-forming proteins from cnidarians and arachnids as potential biotechnological tools

E Rivera-de-Torre, J Palacios-Ortega, JG Gavilanes… - Toxins, 2019 - mdpi.com
Animal venoms are complex mixtures of highly specialized toxic molecules. Cnidarians and
arachnids produce pore-forming proteins (PFPs) directed against the plasma membrane of …

[HTML][HTML] Structural foundations of sticholysin functionality

J Palacios-Ortega, S García-Linares… - … et Biophysica Acta (BBA …, 2021 - Elsevier
Actinoporins constitute a family of α pore-forming toxins produced by sea anemones. The
soluble fold of these proteins consists of a β-sandwich flanked by two α-helices. Actinoporins …

A two‐step mechanism for the binding of the HIV‐1 MPER epitope by the 10 E 8 antibody onto biosensor‐supported lipid bilayers

M García‐Porras, J Torralba, S Insausti, J Valle… - FEBS …, 2024 - Wiley Online Library
HIV‐1 antibodies targeting the carboxy‐terminal area of the membrane‐proximal external
region (ctMPER) are close to exerting viral pan‐neutralization. Here, we reconstituted the …

Sticholysin recognition of ceramide-phosphoethanolamine

C García-Montoya, D Heras-Márquez… - Archives of Biochemistry …, 2023 - Elsevier
Actinoporins are pore-forming toxins produced by sea anemones. They exert their activity by
binding to the membranes of target cells. There, they oligomerize, forming cation-selective …

Decoupling immunomodulatory properties from lipid binding in the α-pore-forming toxin Sticholysin II

AL Rivero-Hernández, YP Hervis… - International Journal of …, 2024 - Elsevier
Sticholysin II (StII), a pore-forming toxin from the marine anemone Stichodactyla helianthus,
enhances an antigen-specific cytotoxic T lymphocyte (CTL) response when co-encapsulated …

[HTML][HTML] Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus

E Rivera-de-Torre, J Palacios-Ortega, JP Slotte… - International Journal of …, 2020 - mdpi.com
Venoms constitute complex mixtures of many different molecules arising from evolution in
processes driven by continuous prey–predator interactions. One of the most common …

Sticholysin, sphingomyelin, and cholesterol: A closer look at a tripartite interaction

J Palacios-Ortega, S García-Linares… - Biophysical …, 2019 - cell.com
Actinoporins are a group of soluble toxic proteins that bind to membranes containing
sphingomyelin (SM) and oligomerize to form pores. Sticholysin II (StnII) is a member of the …

Determination of the boundary lipids of sticholysins using tryptophan quenching

J Palacios-Ortega, R Amigot-Sánchez… - Scientific reports, 2022 - nature.com
Sticholysins are α-pore-forming toxins produced by the sea-anemone Stichodactyla
helianthus. These toxins exert their activity by forming pores on sphingomyelin-containing …