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equinatoxin II

National Institutes of Health

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equinatoxin

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Highly Cited
2011
Highly Cited
2011
Oligomerization and Pore Formation by Equinatoxin II Inhibit Endocytosis and Lead to Plasma Membrane Reorganization*
Pore-forming toxins have evolved to induce membrane injury by formation of pores in the target cell that alter ion homeostasis… 
Highly Cited
2011
Highly Cited
2011
The behavior of sea anemone actinoporins at the water-membrane interface.
Highly Cited
2008
Highly Cited
2008
Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence.
Equinatoxin II is a pore-forming protein of the actinoporin family. After membrane binding, it inserts its N-terminal alpha-helix… 
Highly Cited
2003
Highly Cited
2003
Pore Formation by Equinatoxin II, a Eukaryotic Protein Toxin, Occurs by Induction of Nonlamellar Lipid Structures*
Pore formation in the target cell membranes is a common mechanism used by many toxins in order to kill cells. Among various… 
Highly Cited
2002
Highly Cited
2002
Two-step Membrane Binding by Equinatoxin II, a Pore-forming Toxin from the Sea Anemone, Involves an Exposed Aromatic Cluster and a Flexible Helix*
Equinatoxin II (EqtII) belongs to a unique family of 20-kDa pore-forming toxins from sea anemones. These toxins preferentially… 
Highly Cited
2001
Highly Cited
2001
Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina.
Highly Cited
1997
Highly Cited
1997
pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence.
Thermal denaturation of equinatoxin II (EqTxII) in glycine buffer solutions (pH 1.1, 2.0, 3.0, and 3.5) and in triple distilled… 
Highly Cited
1996
Highly Cited
1996
Cloning, sequencing, and expression of equinatoxin II.
Equinatoxin II (EqtII), a basic protein of 179 amino acids lacking cysteine residues, is the most abundant cytolysin isolated… 
Highly Cited
1995
Highly Cited
1995
Intrinsic tryptophan fluorescence of equinatoxin II, a pore-forming polypeptide from the sea anemone Actinia equina L, monitors its interaction with lipid membranes.
Equinatoxin II is a cytolytic polypeptide from the sea anemone Actinia equina L. which forms pores in natural and artificial… 
Highly Cited
1994
Highly Cited
1994
Primary and secondary structure of a pore-forming toxin from the sea anemone, Actinia equina L., and its association with lipid vesicles.
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