Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Mária, Hanulová"'
Autor:
Lukáš Hubčík, Alexander Búcsi, Mária Hanulová, Juan Carlos Martínez, Daniela Uhríková, Sandra Ritz, Tomas Fazekas, Ferdinand Devínsky, Gilda Liskayová, Martin Pisárčik
Publikováno v:
Langmuir. 35:13382-13395
pH-sensitive liposomes composed of homologues of series of N,N-dimethylalkane-1-amine N-oxides (CnNO, n = 8-18, where n is the number of carbon atoms in the alkyl substituent) and neutral phospholipid dioleoylphosphatidylethanolamine (DOPE) were prep
Autor:
Lukáš Hubčík, Dominika Galliková, Petra Pullmannová, Ľubica Lacinová, Zdena Sulová, Mária Hanulová, Sergio S. Funari, Ferdinand Devínsky, Daniela Uhríková
Publikováno v:
General physiology and biophysics 37(1), 57-69 (2018). doi:10.4149/gpb_2017042
General physiology and biophysics 37(1), 57 - 69 (2018). doi:10.4149/gpb_2017042
DNA condensation, structure and transfection efficiency of complexes formed by gemini surfactants alkane-α,ω-diyl-bis(dodecyldimethylammonium bromide)s (CnGS12, n
DNA condensation, structure and transfection efficiency of complexes formed by gemini surfactants alkane-α,ω-diyl-bis(dodecyldimethylammonium bromide)s (CnGS12, n
Autor:
Gilda, Liskayová, Lukáš, Hubčík, Alexander, Búcsi, Tomáš, Fazekaš, Juan Carlos, Martínez, Ferdinand, Devínsky, Martin, Pisárčik, Mária, Hanulová, Sandra, Ritz, Daniela, Uhríková
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids. 35(41)
pH-sensitive liposomes composed of homologues of series of
Publikováno v:
Molecular Cell. 77:3-16.e4
Tracing DNA repair factors by fluorescence microscopy provides valuable information about how DNA damage processing is orchestrated within cells. Most repair pathways involve single-stranded DNA (ssDNA), making replication protein A (RPA) a hallmark
Autor:
Kalina Peneva, Mária Hanulová, Andreas Vonderheit, Kaloian Koynov, Klaus Müllen, Yulian Zagranyarski, Sandra Ritz, Stefka Kaloyanova
Publikováno v:
Journal of the American Chemical Society
Biocompatible organic dyes emitting in the near-infrared are highly desirable in fluorescence imaging techniques. Herein we report a synthetic approach for building novel small peri-guanidine-fused naphthalene monoimide and perylene monoimide chromop
Autor:
Mária Hanulová, Matthias Weiss
Publikováno v:
Molecular Membrane Biology. 29:177-185
Sorting of membrane proteins in eukaryotic cells is a complex yet vital task that involves several 10,000 molecular players. Sorting takes place not only along the early secretory pathway, i.e., between the endoplasmic reticulum and the Golgi apparat
Autor:
Thomas Gutsmann, Sérgio S. Funari, Jörg Howe, Klaus Brandenburg, Claudia Olak, Patrick Garidel, Mária Hanulová, Jörg Andrä
Publikováno v:
Anti-Infective Agents in Medicinal Chemistry. 8:17-27
Up to now the details of the mechanisms of melittin action on biological bilayer model sys- tems in dependence on lipid composition, in particular on the kind of head groups, temperature, and ionic strength are not well understood. In particular, the
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 38:11-14
Small-angle neutron scattering on extruded unilamellar vesicles in water was used to study bilayer thickness when cholesterol (CHOL) was added at 44.4 mol% to 1,2-dimyristoleoylphosphatidylcholine (diC14:1PC) and 1,2-dierucoylphosphatidylcholine (diC
Autor:
Matthias Weiss, Mária Hanulová
Publikováno v:
Biophysical reviews. 4(2)
Sorting of membrane proteins is of vital importance for living cells. Indeed, roughly one-third of a eukaryotic cell’s proteome consists of peripheral and transmembrane proteins. These need to be properly distributed and dynamically maintained at d
Publikováno v:
European biophysics journal 36, 363-375 (2007). doi:10.1007/s00249-006-0086-2
We investigate the structure of aggregates formed due to DNA interaction with saturated neutral phosphatidylcholines [dipalmitoylphosphatidylcholine (DPPC) and dimyristoylphosphatidylcholine] in presence of Ca(2+) and Mg(2+) cations using simultaneou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2a64e6e95d0310803f70a89559e82d4
https://bib-pubdb1.desy.de/record/81252
https://bib-pubdb1.desy.de/record/81252