[HTML][HTML] Pore-forming protein toxins: from structure to function

MW Parker, SC Feil - Progress in biophysics and molecular biology, 2005 - Elsevier
Pore-forming protein toxins (PFTs) are one of Nature's most potent biological weapons. An
essential feature of their toxicity is the remarkable property that PFTs can exist either in a …

Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)

G Anderluh, P Maček - toxicon, 2002 - Elsevier
More than 32 species of sea anemones have been reported to produce lethal cytolytic
peptides and proteins. Based on their primary structure and functional properties, cytolysins …

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

FH Niesen, H Berglund, M Vedadi - Nature protocols, 2007 - nature.com
Differential scanning fluorimetry (DSF) is a rapid and inexpensive screening method to
identify low-molecular-weight ligands that bind and stabilize purified proteins. The …

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

M Vedadi, FH Niesen… - Proceedings of the …, 2006 - National Acad Sciences
The 3D structures of human therapeutic targets are enabling for drug discovery. However,
their purification and crystallization remain rate determining. In individual cases, ligands …

Role of the molten globule state in protein folding

M Arai, K Kuwajima - Advances in protein chemistry, 2000 - Elsevier
Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …

A three-stage biophysical screening cascade for fragment-based drug discovery

EH Mashalidis, P Śledź, S Lang, C Abell - Nature protocols, 2013 - nature.com
This protocol describes the screening of a library of low-molecular-weight compounds
(fragments) using a series of biophysical ligand-binding assays. Fragment-based drug …

[HTML][HTML] Pore formation by actinoporins, cytolysins from sea anemones

N Rojko, M Dalla Serra, P Maček, G Anderluh - Biochimica et Biophysica …, 2016 - Elsevier
Actinoporins (APs) from sea anemones are~ 20 kDa pore forming toxins with a β-sandwich
structure flanked by two α-helices. The molecular mechanism of APs pore formation is …

Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation

MG Hinds, W Zhang, G Anderluh, PE Hansen… - Journal of molecular …, 2002 - Elsevier
Sea anemones produce a family of 18–20 kDa proteins, the actinoporins, that lyse cells by
forming pores in cell membranes. Sphingomyelin plays an important role in their lytic activity …

The assembly dynamics of the cytolytic pore toxin ClyA

S Benke, D Roderer, B Wunderlich, D Nettels… - Nature …, 2015 - nature.com
Pore-forming toxins are protein assemblies used by many organisms to disrupt the
membranes of target cells. They are expressed as soluble monomers that assemble …

Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56

J Lisboa, C Pereira, RD Pinto, IS Rodrigues… - Nature …, 2023 - nature.com
Bacterial AB toxins are secreted key virulence factors that are internalized by target cells
through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol …