Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Katarina Kristan"'
Publikováno v:
Toxicon. 56:305-312
Our study elucidates some mechanisms of contractions or relaxations of isolated porcine left anterior descending coronary artery (LAD) induced by two peptides from the honeybee venom, melittin and apamin. Contractions or relaxations were measured on
Publikováno v:
FEBS Journal. 274:539-550
Equinatoxin II is a cytolytic protein isolated from the sea anemone Actinia equina. It is a member of the actinoporins, a family of eukaryotic pore-forming toxins with a unique mechanism of pore formation. Equinatoxin II is a 20 kDa cysteineless prot
Autor:
Jeremy H. Lakey, Vesna Hojnik, Gregor Anderluh, Juan Manuel González-Mañas, Gregor Gunčar, Zdravko Podlesek, Dušan Turk, Peter Maček, Katarina Kristan, Ion Gutiérrez-Aguirre
Publikováno v:
Journal of Biological Chemistry. 279:46509-46517
Actinoporins are eukaryotic pore-forming proteins that create 2-nm pores in natural and model lipid membranes by the self-association of four monomers. The regions that undergo conformational change and form part of the transmembrane pore are current
Autor:
Gabriella Viero, Gregor Anderluh, Nejc Rojko, Peter Maček, Eva Žerovnik, Katarina Kristan, Mauro Dalla Serra
Publikováno v:
The Journal of biological chemistry
288 (2013): 23704–23715. doi:10.1074/jbc.M113.481572
info:cnr-pdr/source/autori:Rojko N1, Kristan K?, Viero G, ?erovnik E, Ma?ek P, Dalla Serra M, Anderluh G./titolo:Membrane damage by an alpha-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps/doi:10.1074%2Fjbc.M113.481572/rivista:The Journal of biological chemistry (Print)/anno:2013/pagina_da:23704/pagina_a:23715/intervallo_pagine:23704–23715/volume:288
288 (2013): 23704–23715. doi:10.1074/jbc.M113.481572
info:cnr-pdr/source/autori:Rojko N1, Kristan K?, Viero G, ?erovnik E, Ma?ek P, Dalla Serra M, Anderluh G./titolo:Membrane damage by an alpha-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps/doi:10.1074%2Fjbc.M113.481572/rivista:The Journal of biological chemistry (Print)/anno:2013/pagina_da:23704/pagina_a:23715/intervallo_pagine:23704–23715/volume:288
Actinoporin equinatoxin II (EqtII) is an archetypal example of α-helical pore-forming toxins that porate cellular membranes by the use of α-helices. Previous studies proposed several steps in the pore formation: binding of monomeric protein onto th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93fb18b6c6af7713134d66844bab39ca
Autor:
Andrew J. Miles, Bonnie A. Wallace, Raymond S. Norton, Frances Separovic, Alison Drechsler, Katarina Kristan, Gregor Anderluh
Publikováno v:
Biochimica et biophysica acta. 1778(10)
Synchrotron radiation circular dichroism (SRCD) spectroscopy studies of the eukaryotic pore-forming protein equinatoxin II (EqtII) were carried out in solution and in the presence of micelles or small unilamellar vesicles (SUV) of different lipid com
Publikováno v:
The FEBS journal. 274(2)
Equinatoxin II is a cytolytic protein isolated from the sea anemone Actinia equina. It is a member of the actinoporins, a family of eukaryotic pore-forming toxins with a unique mechanism of pore formation. Equinatoxin II is a 20 kDa cysteineless prot
Autor:
Petra Malovrh, Gregor Anderluh, Jeremy H. Lakey, Zdravko Podlesek, Qi Hong, Ariana Barlič, Peter Maček, Juan Manuel González-Mañas, Ion Gutiérrez-Aguirre, Dušan Turk, Katarina Kristan
Publikováno v:
The Journal of biological chemistry. 277(44)
Equinatoxin II (EqtII) belongs to a unique family of 20-kDa pore-forming toxins from sea anemones. These toxins preferentially bind to membranes containing sphingomyelin and create cation-selective pores by oligomerization of 3–4 monomers. In this