Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Katja Ota"'
Autor:
Matej Skočaj, Nataša Resnik, Maja Grundner, Katja Ota, Nejc Rojko, Vesna Hodnik, Gregor Anderluh, Andrzej Sobota, Peter Maček, Peter Veranič, Kristina Sepčić
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e92783 (2014)
Ostreolysin A (OlyA) is an ∼15-kDa protein that has been shown to bind selectively to membranes rich in cholesterol and sphingomyelin. In this study, we investigated whether OlyA fluorescently tagged at the C-terminal with mCherry (OlyA-mCherry) la
Externí odkaz:
https://doaj.org/article/ba3cbb4164a54b8a9f0081467e9860a3
Autor:
Markus Aebi, Adrijana Leonardi, Katja Ota, Markus Künzler, Mojca Narat, Gregor Anderluh, Miha Mikelj, Therese Wohlschlager, Kristina Sepčić, Matej Skočaj, Peter Maček, Igor Križaj
Publikováno v:
Biochimie. 95:1855-1864
The mushroom Pleurotus ostreatus has been reported to produce the hemolytic proteins ostreolysin (OlyA), pleurotolysin A (PlyA) and pleurotolysin B (PlyB). The present study of the native and recombinant proteins dissects out their lipid-binding char
Autor:
Katja Ota, Magda Tušek-Žnidarič, Peter Maček, Simona Sitar, Valerija Vezočnik, Katja Rebolj, Kristina Sepčić, David Pahovnik, Ema Žagar, Jasna Štrus
Publikováno v:
Journal of chromatography. A. 1418
Asymmetric-flow field-flow fractionation technique coupled to a multi-angle light-scattering detector (AF4-MALS) was used together with dynamic light-scattering (DLS) in batch mode and transmission electron microscopy (TEM) to study the size characte
Autor:
Katja, Ota, Matej, Butala, Gabriella, Viero, Mauro, Dalla Serra, Kristina, Sepčić, Peter, Maček
Publikováno v:
Sub-cellular biochemistry. 80
Proteins with membrane-attack complex/perforin (MACPF) domains are found in almost all kingdoms of life, and they have a variety of biological roles, including defence and attack, organism development, and cell adhesion and signalling. The distributi
Autor:
Andrzej Sobota, Maja Grundner, Katja Ota, Vesna Hodnik, Peter Veranič, Matej Skočaj, Kristina Sepčić, Peter Maček, Gregor Anderluh, Nataša Resnik, Nejc Rojko
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 3, p e92783 (2014)
PLoS ONE, Vol 9, Iss 3, p e92783 (2014)
Ostreolysin A (OlyA) is an ∼15-kDa protein that has been shown to bind selectively to membranes rich in cholesterol and sphingomyelin. In this study, we investigated whether OlyA fluorescently tagged at the C-terminal with mCherry (OlyA-mCherry) la
Publikováno v:
MACPF/CDC Proteins-Agents of Defence, Attack and Invasion ISBN: 9789401788809
Proteins with membrane-attack complex/perforin (MACPF) domains are found in almost all kingdoms of life, and they have a variety of biological roles, including defence and attack, organism development, and cell adhesion and signalling. The distributi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8bfc88774ec5ccc6503b78c8a9bf9499
https://doi.org/10.1007/978-94-017-8881-6_14
https://doi.org/10.1007/978-94-017-8881-6_14
Publikováno v:
Biochimica et biophysica acta. 1834(8)
article i nfo Proteins with hemopexin repeats are widespread in viruses, prokaryotes and eukaryotes. We report here for the first time the existence of a protein in fungi with the four-bladed β-propeller fold that is typical for hemopexin- like prot
Autor:
Katja Rebolj, a Biserka Bakrac, a Maja Garvas, b Katja Ota, a Marjeta Sentjurc, b Cristina Potrich, c,d Manuela Coraiola, c,d Rossella Tomazzolli, c,d Mauro Dalla Serra, c,d Peter Macek, a Kristina Sepcic, a,?
Publikováno v:
Biochemical journal (Lond., 1984) 1798 (2010): 891–902. doi:10.1016/j.bbamem.2010.01.016
info:cnr-pdr/source/autori:Katja Rebolj;a Biserka Bakrac;a Maja Garvas;b Katja Ota;a Marjeta Sentjurc;b Cristina Potrich;c,d Manuela Coraiola;c,d Rossella Tomazzolli;c,d Mauro Dalla Serra;c,d Peter Macek;a Kristina Sepcic;a,?/titolo:EPR and FTIR studies reveal the importance of highly ordered sterol-enriched membrane domains for ostreolysin activity./doi:10.1016%2Fj.bbamem.2010.01.016/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:891/pagina_a:902/intervallo_pagine:891–902/volume:1798
info:cnr-pdr/source/autori:Katja Rebolj;a Biserka Bakrac;a Maja Garvas;b Katja Ota;a Marjeta Sentjurc;b Cristina Potrich;c,d Manuela Coraiola;c,d Rossella Tomazzolli;c,d Mauro Dalla Serra;c,d Peter Macek;a Kristina Sepcic;a,?/titolo:EPR and FTIR studies reveal the importance of highly ordered sterol-enriched membrane domains for ostreolysin activity./doi:10.1016%2Fj.bbamem.2010.01.016/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:891/pagina_a:902/intervallo_pagine:891–902/volume:1798
Ostreolysin is a cytolytic protein from the edible oyster mushroom (Pleurotus ostreatus), which recognizes specifically and binds to raft-like sterol-enriched membrane domains that exist in the liquid-ordered phase. Its binding can be abolished by mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89da5d1434525a3ef8ef3cc61c37cc54
http://www.cnr.it/prodotto/i/9830
http://www.cnr.it/prodotto/i/9830