Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Ilya Mikhalyov"'
Autor:
Nataliya Gretskaya, Mikhail Akimov, Dmitry Andreev, Anton Zalygin, Ekaterina Belitskaya, Galina Zinchenko, Elena Fomina-Ageeva, Ilya Mikhalyov, Elena Vodovozova, Vladimir Bezuglov
Publikováno v:
Pharmaceutics, Vol 15, Iss 4, p 1289 (2023)
Despite the wide variety of available cationic lipid platforms for the delivery of nucleic acids into cells, the optimization of their composition has not lost its relevance. The purpose of this work was to develop multi-component cationic lipid nano
Externí odkaz:
https://doaj.org/article/0c22c068ac8f49df8bafbf6a25d69749
Autor:
Alena Koukalová, Mariana Amaro, Gokcan Aydogan, Gerhard Gröbner, Philip T. F. Williamson, Ilya Mikhalyov, Martin Hof, Radek Šachl
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Abstract It is a fundamental question in cell biology and biophysics whether sphingomyelin (SM)- and cholesterol (Chol)- driven nanodomains exist in living cells and in model membranes. Biophysical studies on model membranes revealed SM and Chol driv
Externí odkaz:
https://doaj.org/article/7164659d8d9f4ac9aa6acda2fdde406c
Autor:
David Davidović, Robert Vácha, Joana C. Ricardo, Ilya Mikhalyov, Maria J. Sarmento, Michael C. Owen, Radek Šachl, Barbora Chmelová, Martin Hof, Natalia Gretskaya, Mariana Amaro
Publikováno v:
Biophys J
Gangliosides form an important class of receptor lipids containing a large oligosaccharide headgroup whose ability to self-organize within lipid membranes results in the formation of nanoscopic platforms. Despite their biological importance, the mole
Autor:
Martin Hof, Petra Riegerová, Ilya Mikhalyov, Radek Šachl, Natalia Gretskaya, Kristián Skála, Ivo S. Vinklárek, Lukas Velas
Publikováno v:
The Journal of Physical Chemistry Letters. 10:2024-2030
Plasma membranes of living cells are compartmentalized into small submicroscopic structures (nanodomains) having potentially relevant biological functions. Despite this, structural features of these nanodomains remain elusive, primarily due to the di
Publikováno v:
Angewandte Chemie (International Ed. in English)
β‐Amyloid (Aβ) oligomers are neurotoxic and implicated in Alzheimer's disease. Neuronal plasma membranes may mediate formation of Aβ oligomers in vivo. Membrane components sphingomyelin and GM1 have been shown to promote aggregation of Aβ; howe
Publikováno v:
Angewandte Chemie. 128:9557-9562
Autor:
Natalia R. Onishchenko, Evgeniy G. Evtushenko, Ivan A. Boldyrev, Alexander B. Tuzikov, Ilya Mikhalyov, Daria Tretiakova, Nicolai V. Bovin, Elena L. Vodovozova
Publikováno v:
Colloids and surfaces. B, Biointerfaces. 166
Previously, we proposed a liposomal formulation of melphalan (Mlph)—a chemotherapeutic alkylating agent—incorporated in a fluid lipid bilayer in the form of dioleoylglyceride ester. In this work, we compared the stabilizing effect of different am
Autor:
Martin Hof, Radek Šachl, Gokcan Aydogan, Philip T. F. Williamson, Ilya Mikhalyov, Gerhard Gröbner, Alena Koukalová, Mariana Amaro
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Scientific Reports
Scientific Reports
It is a fundamental question in cell biology and biophysics whether sphingomyelin (SM)- and cholesterol (Chol)- driven nanodomains exist in living cells and in model membranes. Biophysical studies on model membranes revealed SM and Chol driven microm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48e36a353f6cd6923b9a83788830f9ad
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-139014
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-139014
Publikováno v:
Molecular Membrane Biology. 24:102-112
We demonstrate that the ganglioside G(M1) in lipid bilayers of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) exhibits a non-uniform lateral distribution, i.e., enriched regions of GM(1) molecules are formed, which is an argument in favour of self-a
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 13:675-678
Our study deals with the interaction of CD33 related-siglecs-5,-7,-8,-9,-10 with gangliosides GT1b, GQ1b, GD3, GM2, GM3 and GD1a. Siglec-5 bound preferentially to GQ1b, but weakly to GT1b, whereas siglec-10 interacted only with GT1b ganglioside. Sigl